Capital Punishment in America Research Paper Example | Topics and Well Written Essays - 1000 words

Capital Punishment in America - Research Paper Example Deterrence is regarded as a means of discouraging individuals from engagement in criminal activities. This involves illustrating to offenders that harsh consequences would result for their criminal actions. Such consequences include one being imprisoned. As such, deterrence illustrates that punishment should be provided as a consequence of crime. Since human beings are rational, contemplation of the severity and consequences of punishment would deter people from temptations of engaging in criminal activities. This validates the use of deterrence as the means of punishment for criminal activities in society. On the other hand, retribution indicates an action of repairing or repaying something as price of criminal activities of an individual. Such a punishment makes an individual develop individual responsibility towards social structures and â€Å"keep off† criminal activities. As such, the most effective means of deterring crime is retribution. This is because an individual is subject to payment of the criminal acts. This acts as an effective means of making an individual not to engage in criminal activities. This type of punishment is more significant in cases where the individual commits a crime for the first time than in cases of subsequent crimes. The American society believes in punishment as a consequence of criminal activities. This depicts that people are aware of what kind of punishment they may receive in case they engage in criminal activities. Moreover, retribution provides a means of punishment, which depends on the degree of the crime committed by an individual. Therefore, the punishment administered to the criminal is equivalent to the crime committed and the criminal does not receive excessive or less punishment in comparison to the magnitude of the crime committed. However, in situations where an individual is engaged in multiple crimes and retribution does not prove effective. Such an individual should be subjected to rehabilitation for m of punishment. This is because this form of punishment allows effective cross-examination of the psychological needs and reactions of an individual, which could be the factors, which makes such an individual to engage in criminal activities. After such a cross-examination, an individual is guided under a controlled environment, which allows consistent monitoring of behavior of an individual. This leads to a change in the conduct of an individual in society. Furthermore, rehabilitation provides an opportunity of offering moral education to an individual who is engaged in criminal activities. This may also include provision of vocation training, which equips an individual with skills, which would keep such an individual from engagement in criminal activities, in society. Deterrence is not an effective means of punishment since it leads to the development of fear among individuals, which impacts the decision-making process of individuals in society (Lund, 2002). As such, using deterr ence as a form of punishment would create an American society, which is composed of an element of fear.

The Impact of Teenage Pregnancy Essay Example for Free

The Impact of Teenage Pregnancy Essay The reality TV series 16 and pregnant and Teen Mom are two great examples showing the everyday struggles of teenage pregnancy and a day in the life of a teenage mother. By no means do these two shows glorify teen pregnancy. Teens seem to think that they are inevitable and nothing will happen to them. All it takes is one time to have sexual intercourse to become pregnant. While being wrapped up in the excitement, lust, adrenaline, rush and at times even under the influence these young teens do not seem to think about the outcome that may occur from making the decision to partake in intercourse. The Big Brother sister Program has proved to steer children in the right direction, have a positive impact on these children and encourage these kids to be all they can be. The Big Sister program should address the issue of teen pregnancy by providing sexual education, guidance, free contraception and a respected role model to young females. Providing these teens with sexual education concerning the impact of teenage pregnancy regarding the wellbeing of a teen mother and child, loss of education, and the lack of parenting skills will influence young teens to make better decisions and teen pregnancy will decrease in our community. Teenage pregnancy may seriously impact the wellbeing of their child as well as themselves by not seeking proper medical care which may cause high blood pressure, anemia, toxemia, and Placenta Previa (Bodeeb 2011). Many teens do not even realize they are pregnant until about three or four months, Due to the fact that teens are unaware of the physical and internal changes the body makes to prepare a home in the womb for the baby. It is important for a mother to seek medical attention as soon as possible to make sure of a healthy pregnancy. The early stages of pregnancy are the most important. A mother needs to be aware of the pregnancy for such reasons as: taking prenatal vitamins, smoking cigarettes, drinking or any prescription taking while being pregnant (Bodeeb 2011). Those acts may cause serious long term birth defects and medical complications for the baby. Certain tests need to be performed while in the first few months of a pregnancy as well to make sure there are not any complications. At four months the Down syndrome test is performed on the child while in the womb. That is an issue that any mother would like to know about their unborn child so proper decisions can be made and the mother can find out where to go from then. Un Expecting bleeding may occur and a young mother may seem to think it is an abnormal period, but really it may be a miscarriage and if proper procedures aren’t taken it can result to the loss of the mother. A proper DNC must be performed. Teen pregnancy will be a challenge due to the fact that teens are not provided the skills that are needed to handle a pregnancy and mother hood. This may very well affect the wellbeing of the mother and the child. It is necessary for a teen mother to portray skills for pregnancy. Patience, maturity, and the ability to handle stress is a part of pregnancy. Pregnant teens are at more of a higher risk of postpartum depression syndrome, which starts after delivering the baby. According to CDC, girls who feel down and sad, either while pregnant or after birth should talk openly to someone they trust. Depression can absolutely interfere with taking care of a newborn (â€Å"Teen Pregnancy: Medical Risks and Realities†, 2005-2012). Postpartum depression affects many mothers life while trying to care for their child. This depression makes it hard for a mother to have the want or need to take care of their baby, cry consistently, and may cause the mother to shut herself out away from the rest of the world(†Teen Pregnancy :Medical Risks and Realities†, 2005-2012). Teens are at higher risk of this depression because they are less experienced, scared, the lack of social life and simply because they just do not know how to handle a helpless child depending on the young mother. Teens most of the time lack these skills to obtain a successful pregnancy. Bodeeb also states that according to The U. S Centers for Disease Control and Prevention notes that babies born to teen mothers may have weaker intellectual development and may have on going medical complications. Babies born to teen mothers may have medical complications such as: The growth of the child, which is called premature birth. The earlier a baby is born the more risk there is of respiratory, digestive, vision, cognitive, and other problems (â€Å"Teen Pregnancy: Medical Risks and Realities†, 2005-2012). It is not easy attending high school while expecting a child, especially having to deal with being judged by classmates. Regardless if any teen mother is affected by the comments or snickering being made by the other students, it does not help the situation or make it any easier. These acts that occur all the time in school may cause the young mother to no longer want to attend school . Finding a sitter for the child is a burden because not all parents of a young mother are supportive of the situation. In some cases a young girl getting pregnant while still living at home and attending school may result in her getting thrown out of her home , which makes it even more complicated to attend classes. After having a child the mother is usually given six weeks for recovery and to spend time with the mother. The time missed by the student may result to failure of classes or getting behind. This is when most teens decide to not come back to school because they figure it is more of a hassle and simply do not know what to do. There are some high schools that have day cares located inside the school, but not all. It is a struggle for teens to put their child in day care, especially if they cannot find a job that will work around the school schedule and spending time with the baby. The government does provide assistance in child care but they do not pay for the whole thing. It was recently reported by CBS 2 News that Chicago’s South Side Paul Robenson High School has 115 girls who are pregnant out of 800 girls who attend the school (Roush, 2009). According to The Centers for Disease Control and Prevention statistics, teen pregnancy is not just local problem and birth rates have been rising during the past few years after more than a decade of decline (Roush, 2009). Soo Ji Min, executive director of the Illinois Caucus for adolescent Health, an organization that advocates for policies to promote sexual health and education among teens said that; the No child Left- behind is the culprit for eliminating sexual education in school. She claimed the lack of information in the schools led to the increase in teen pregnancies (Roush, 2009). If schools are teaching about abstinence and not giving teens the knowledge they need to know about sex and protection, these children are not receiving any information to protect themselves. To continue to discuss the importance of the statistics of pregnancy among teen girls and the impact on their education, less than half of young women who have had a child as a teenager go on to finish high school or let alone go on to pursue studies in college (Roush, 2009). It is becoming harder for anyone to find a job without a college education or nevertheless the bare minimum of a GED or diploma. Bill albert ,a chief Program officer of the National Campaign founded in 1996 to help women stated that; a teenage girl has a three in ten chance of becoming pregnant before turning 20 (Roush , 2009). Without saying adolescent mothers are bad mothers it is safe to say that young mothers lack the ability for proper parenting skills that will play a role in the impact of teen pregnancy on young mothers. The earlier stages of parenting behavior tend to occur from the risk process of stress. Diversion of attention away from socialization, urgent goals of providing shelter and substance, lack of social support, and lack of opportunities to enhance parenting skills all may contribute to the preventing difficulties faced by young mothers living in disadvantaged circumstances. Again these examples provided may be symptoms of postpartum depression syndrome. Teen mothers may simply face a barrier providing for their child and get discouraged in the process and tend to lead to the lack of judgment in providing for the child (Socio Economic Disadvantages and child Development pp185-204). Child parenting skills may consist of aggressive behavior from the child. If a child is acting out, simply unruly, often angry, gets in trouble in school, or defies the parents, these may be signs of aggressive behavior. Aggressive behavior from the child is more likely to occur due to a teen having a child at such a young age (Socio Economic Disadvantages and Child Development pp185-204). A teen mothers harsh discipline strategies may also play a role in aggressive behavior from the child. It is hard for a child to discipline a child in the correct manner. In many cases young mothers tend to get overwhelmed and accidently hurt or abuse the child because they get frustrated. Just like their mothers the child of a teen is more likely to experience abuse and neglect and become pregnant as a teen as well (Cheour, 2011). In high school prom was a big deal, but if being pregnant during the occasion it may take away the memories and the pleasure of enjoying the high school experience. Time is limited with friends and sports are completely out of the option while being pregnant. Not only does a child need to remain a child with less stress as possible, there is no need for a young girl to carry the burden of having to take care of a helpless child when some of these teens can barely take care of themselves. The impact of teen pregnancy on young mothers is a more serious issue than some may seem to realize. The concern is of course in regards to a young adult having the proper education provided to decrease teen pregnancy, even if the issue may not be eliminated altogether. The children are our future and by bringing forth the Big sister program filled with volunteers that are willing to guide, assist in young teens making the right decisions, and simply just making a fun positive way of learning about safe sex the numbers of these pregnant girls in school have a chance to decrease. If this program only changes one young woman’s perspective and makes her realize the outcome that may occur from bringing a beautiful life into this world the goal will be accomplished.

Hydrophobic And Hydrophilic Interaction In Protein Folding Biology Essay

Hydrophobic And Hydrophilic Interaction In Protein Folding Biology Essay Review the mechanism of protein folding Module: Enzyme Technology and Biocatalysts Module leader: Prof. Steve Forsythe Proteins are the bio molecules which play pivotal role in this living world. They are responsible for expression of certain characters in different types of cells and constitute around 50% of the total cell dried mass. Proteins are the chain of amino acids which binds with polypeptide backbone and then fold in a unique 3D (native) structure by which protein expression takes place. Various forces and factors are responsible for protein folding .If right expression of the protein will not take place, it will cause disorders in human body. Many diseases like Alzheimers; Parkinson, cystic fibrosis etc (Baldwin 2007) is caused due to improper folding of proteins. For proper expression of protein, the amino acid chain should be in its unique 3D structure. Sometimes proteins require assistance in folding, molecules which help in the folding are known as chaperones. These molecules help in the folding of the certain protein molecules and also prevent the unfolding of the molecules. In this assignment, I have tried to describe the mechanism of the protein folding and effect of various factors which influence protein folding by taking into consideration the present developments in our understanding of thermodynamics and kinetics of protein. INTRODUCTION Protein folding refers to the process by which a protein assumes its characteristic structure, known as the native state. Protein folding is very complex mechanism and great development in its understanding has been achieved in last 20years due to the development and use of some sophisticated modern techniques like X Ray Crystallography, N.M.R, and Mass Spectrometry etc. In the last few decades, we have managed to find the 3D structure of various proteins and how actually protein folding takes place. In the complex process of protein folding, various factors act together to construct specific 3D structure of a protein. Protein folding is a very quick process taking milliseconds to seconds. Due to high speed of folding, it is not possible to find each and every possible conformation in fractions of time. Levinthal stated that each protein can possibly have millions of pathway by which a desired 3D pattern can be achieved. By study of intermediates we can understand the mechanism or pattern on which protein folding works. But it is impossible to find out all possible structure of protein molecules. Protein folding study uses denaturants which help to denature the protein. The logic is to use denaturing conditions viz. high pH, Temp, Pressure etc to stop folding at intermediate stages (Stop flow technique) to study these intermediates, thereby generating an overview of the whole process. Fully folded structure is also known as native structure. Protein folding studies have also been done in in-vivo and in-vitro conditions. In in- vivo protein folding, some metal ions act as cofactors. These cofactors stabilise and accelerate protein folding and finally help to achieve native stage .Macromolecules like chaperones initiate protein folding, helping the protein molecule to retain its folded confirmation and making it stable. In-vitro concentration of macromolecules is very less, around 1% of what is originally present in the cell. So inside cell, these molecules also affect protein stability and make them more stable than in vitro (Rumfeldt et al. 2008) Protein folding can be a two stages or multistage process, depending upon the type of sequence. A single point mutation can change folding from two stages to multistage and vice-versa .Some previous studies show that protein sequences of less than 80 amino acids prefer two stage folding and large protein sequences having more than 130 amino acids prefer multi stage folding. Later studies have shown that sequences rich in F and G amino acids prefer two stages folding where as sequences rich in C, H, L and R amino acids prefer multistage folding (Ma, Chen Zhang 2007) PROTEINS FOLDING Hydrophobic and hydrophilic interaction Proteins are made of amino acids and joined by polypeptide bonds leads to formation of polypeptide backbone. We have only 20 type of the amino acids .whose combinations code for such complex structure and folding .These amino acids can be divide in two groups one is hydrophilic or polar group and other is hydrophobic or nonpolar group and their interaction with the cytoplasm make them folded(Trevino, Scholtz Pace 2007) POLAR OR HYDROPHILIC AMINO ACID NON-POLAR OR HYDROPHOBIC AMINO ACID ASPARTIC ACID D ALANINE A GLUTAMIC ACID E GLYCINE G ARGNIN R VALINE V LYSINE K LEUCINE L HISTIDINE H ISOLEUCINE I ASPARAGINE N PROLINE P GLUTAMINE Q PHENYLALANINE F SERINE S METHIONINE M THREONINE T TRYPTOPHAN W TYROSENE Y CYSTEINE C In the early stages of research, problem was why protein folds to a specific structure and which part of the protein carried information for the folding and later on this was find that primary structure of the protein code for the final 3D structure. Hydrophilic and hydrophobic interactions of the amino acids adjust protein it such a way that it suffers minimum repulsion and problem from the surrounding. In folded state of protein all hydrophilic amino acid molecules come at the other side and interact with water in the cytoplasm and hydrophobic molecule come at the inner side of the molecule and dont show any reaction and attraction with water molecules and ultimately protein folding take place in such a way that suffer minimum repulsion (Baldwin 2007) All amino acids have different energetic in secondary structure. There are many chameleon sequences in protein structure which can be taken as alpha helix or beta sheets depending upon the tertiary structure of protein. These chameleon are stabilised by hydrophobic forces (Chen et al. 2008) Fig.a shows yellow colour hydrophobic molecules inner side of structure Fig.b shows folding takes place and keeps hydrophobic molecules in inner side (Chen et al. 2008) Apart from these interactions hydrogen bonding is very important in the protein folding. Hydrogen bonding takes place between hydrogen and electronegative atoms In the maintenance of the native structure hydrogen bonding present in between the polypeptide amino acid chain which helpful in the formation of the secondary, tertiary and quaternary structure of the proteins. Hydrogen bonding also interacts between polar and side chain residues with the surrounding water molecules. During the denaturing of the protein hydrogen bond between protein molecules break and native structure of protein disturbed (Djikaev, Ruckenstein 2010) Hydrophobic interactions are also responsible for the protein folding. During hydrophobic interactions amino acids which are non polar or hydrophobic they align themselves in such a way that all hydrophobic come together and all hydrophilic molecules make hydrogen bonds with water molecules, all hydrophobic amino acid come in to inner side of the protein molecules and formation of the nuclei take place which is hydrophobic these interaction further helpful in the secondary, tertiary structure and due to this protein sta bilise and help to achieve native structure because hydrophobic molecules will not interact with water and always have repulsive attitude toward water and let the protein in the folded form and finally such type of the folding take place in which molecule have hydrophobic core and all hydrophilic molecules in periphery of the folded structure(Berezovsky et al. 2001) Free energy and entropy (G, E) Gibbs free energy (G) is also defined as the amount of the energy which is free and this can also be defined as the measure of unstableness and this measured by simple equation G= H-TS G=free energy, H=enthalpy, S=entropy, T= temperature Entropy (S) is defined as degree of randomness in any system, in terms of protein folding this can be define as the measure of the possible structure in the protein molecule at that value of the entropy. Entropy is responsible for the possible out come of protein as much high would be entropy as much high number of the confirmation would form. To minimise the entropy in the protein folding various force come in play like hydrogen bonds, salt bridges, disulphide bonds etc. these bonds help to reduce the entropy and favour protein folding(Brady, Sharp 1997)BOLTZMANN worked on the entropy and give us a very useful relation between atomic theory and entropy. Boltzmann proposed an equation which shows that entropy in any unfolded protein structure is equal to the product of his constant(KB) and natural log of number of all possible states which any protein can adopt(S) S = KB * NATURAL LOG (S) KB=Boltzmann constant Protein folding prefers low value of entropy and follows that smallest path in which value of entropy is low. At different value of the entropy different number of structure could be present and finally all structure will vanished and one structure would be present at the minimum value of entropy, which is our native structure (Weikl, Dill 2003) Enthalpy (H) is also responsible for protein folding. This is also known as the measure of the total energy of the system including internal energy (U). P and V are the pressure and volume of system H= U+P*V So, we should search for such structure which have low value of enthalpy then the free energy, because which structure have low value of enthalpy that will have low value of free energy too(Brockwell, Smith Radford 2000) Gibbs free energy equation is the single solution for all protein folding problem. Gibbs equation shows that in case of protein folding, stable state will have minimum value of G. unfolded state have higher free energy then the folded one and protein folding have many intermediates, This stage is less populated stage and have maximum energy in the whole system, all above mention factor in the Gibbs equation adjust and finally provide such folded state in which value of G is minimum and this is known as fully folded and stable confirmation(Finkelstein, Badretdinov 1997) (www.biology-online.org/articles/statistical_thermodynamics_taking_walk.html) Chaperones Chaperones are bio molecules which participate in the protein folding. Proteins need assistance in the folding and binds with cofactors .which allow them to fold properly .these cofactor known as chaperones. These chaperones bind with the protein as N terminus of the protein formed and leave ribosome and until and unless protein gain his fully active 3D state and become functional(Tomala, Korona 2008) Chaperones are not only helping in the correct protein folding but they also help protein to maintain its correct 3D structure and prevent them to unfold .these molecules comes in to play when cell is under stress due to favourable conditions are not present and they also known as the H.S.P (heat shock protein).these molecular chaperones are HSP40(Dnaj), HSP60(GroEl), HSP70(Dnak) etc.(Rikhvanov, Romanova Chernoff 2007) Copied from Yon, Betton 1991 Mode of action Chaperones recognise non native protein structure by their exposed hydrophobic regions Chaperones action is driven by ATP and for the activity of the chaperones assistance protein folding need of energy, which is provided by the ATP. These chaperones bind with the intermediate and unfolded protein structure by the utilisation of the ATP intermediates or random coil structure are unfolded and again they are fold in the correct 3D structure (NATIVE structure). Chaperones molecules are task specific that are different molecules perform different functions. For example: HSP70/40 They prevent aggregation and misfolding of newly synthesised protein molecules. HSP60 They unfold intermediate and then fold them properly in to native structure Chaperones are like catalyst, they enhance rate of protein folding and assist protein folding to native structure and after the formation of the native structure they separated. As like catalyst they required energy for the initiation of the process Chaperones activity is much specialised, in stress condition protein get mutated, denature, and aggregate. Which may cause some wrong expression and code for some disease .In such situations they are enough capable to provide personalised treatment to different protein (Yon, Betton 1991)They can easily point out that which protein intermediate structure need to be degraded and which protein intermediate to be stabilise in the native structure and path should be follow for this process. In some mutation destabilise protein can be easily stabilized by HSP70 and some over expression of the specific chaperones. For example: In bacteria HSP70 bind with the protein polypeptide chain during translation after the synthesis some protein released for expression and some may attached for some specialised folding and most destabilise polypeptide chain degraded by chaperones (Tomala, Korona 2008) Chaperones activity is not simple they have multiple steps in their folding mechanism. Some chaperones required some other chaperones intermediate as substrate and then they provide native structure. Hsp90/70 mechanism chain Some chaperones may responsible for disease. it has been found that HSP90 enhance cancer development because many mutated protein mature in the presence of the HSP90 and cause cancer , repressing HSP90 such type of cancer can be able to prevent but problem associated with this is due to this action some non mutagenic protein will be degrade and not express and cause problem. But on other side HSP70 acts as good repressor in neurodegenerative disease and prevent this disease in the fruit flies (Tomala, Korona 2008) Models of protein modelling and structure prediction Plaxco and co-worker model: This model shows that high degree of correlation between folding rate and structural properties of protein explain on the basis of contact order (CO). This can be cross validated from various experiments that folding rate and contact order are dependent to each other. ,    L  is the sequence length   N  is the total number of inter-residue atomic contacts   ÃƒÅ½Ã¢â‚¬ Lij  is the sequence separation of contacting residues  i  and  j Kuznetsov and rackovsky showed that structural based determinants can serve as good determinants of folding rate and many other researchers searching for which structural and sequence based determinants can serve as unique predictor of folding rate (Shakhnovich 2006) Dokholyan and co-workers model: They use simple protein model and find out transition state of src homology 3(SH3) to find out contribution of each amino acid in transition state. They calculate ÃŽÂ ¦ value and on this basis they find high correlation between simulation and experimental ÃŽÂ ¦ value .in the end of their experimental model they conclude that L24 and G24 are two most important residues in the folding of proteins Physics and bioinformatics based models: Physics models are very helpful to understand protein folding rate and route to folding. These physics based models help to understand the various forces and their dynamics in protein folding. These models help to understand: Conformational changes in protein Mechanism of folding, enzyme catalysis, mode of action protein Response to ph salt and denaturants(Brockwell, Smith Radford 2000) Bioinformatics is very important tool to find out the structure and folding pattern of the protein molecules. In this we add our computer based program along with these physics model and within the fraction of time provide us 3D structure of protein. Various databases on web are present which contain information regarding proteins only like NCBI, PUBMED etc. these databases contain all information about proteins by the comparison of our unknown sequence using bioinformatics tools with these databases we can find out possible structure and folding pattern and helpful in drug discovery, possible remedy against disease etc. Now, how collectively these factors works After having the knowledge of these factors now we can easily understand how they act and result to the fully folded 3D structure. Primary structure of protein code for 3D structure and all above factors participate to provide a functional unit. initially primary structure of protein are made of different type of amino acids on the poly peptide back bone and just after the production of the N-terminus protein folding starts and secondary structures alpha helix and beta sheets are formed. In alpha helix all amino acid chain remain in the periphery of the helix and this structure formed due to hydrogen bonding and di-sulphide bonding (Trevino, Scholtz Pace 2007) After the formation of secondary structure, tertiary structure these hydrophobic interaction, hydrogen bonding and charge on the molecule come it to the play now this protein molecule structure fold in such a way to minimise all these forces and try to give an stable confirmation to protein(Chen et al. 2008) Free energy and entropy act simultaneously. After attachment of these secondary structures stability is not uniform in the whole tertiary structure. There may be possibility that two stable structures are joining by unstable and less stable strands and in that case folding take place in such a way to minimise the free energy of the system. This type of stage is known as the intermediate stage. In this stage all amino acids are attached in the structure but the entropy of the system is high and due to which this show high presence of free energy and may have the millions of the possibilities of the intermediate structure. Now protein starts folding from intermediate to the stable or native structure by minimising the interaction between the molecules. Due to which all the hydrophobic or non polar amino acid come in the centre of the structure and the formation of hydrophobic core take place of 3D structure and all polar or hydrophilic molecules come at the periphery of the 3D structur e(Chen et al. 2008). Out of millions of the possibilities there are many path which favour this folding in term of having minimum energy and protein molecule select that path which is shortest and this may contain several steps in folding and ultimately leads to the formation of native 3D structure Copied from Ma, Chen Zhang 2007 There is always some equilibrium in some folded and intermediates state and molecules may be aggregate. this depend upon the pH, Temp, Pressure and denaturation agents and the protein structure destabilise it start affecting other native protein structure in this stage chaperones act as cofactors and help in the and maintaining native structure of protein(Ma, Chen Zhang 2007) SUMMARY In the protein folding 3D structure of protein plays an important role in the protein expression and their function. Information regarding protein folding is present in the primary structure of the protein which bioenergetics can be determined by bound amino acid. Hydrophobic forces play an important role. They all concentrate at the centre of the molecules and hydrophilic at the periphery of the structure. Hydrogen bonding plays an important role due to which all polar molecules bound with the surrounding medium in cell and makes protein molecule structure rigid and compressed. Protein folding is a spontaneous process in which entropy of the molecule is decreasing and finally provides a folded structure. Protein native structure must have low value of Gibbs free energy, entropy, and enthalpy and lower the value, higher will be the degree of protein stability. Protein may unfold due to the presence of the unfavourable condition like temp, pressure, pH, and denaturing agent. In such a case special type of molecules help in the folding known as chaperones and helpful in maintaining native structure of protein.

The Road Not Taken Essay -- Poetry Robert Frost essays research papers

  Ã‚  Ã‚  Ã‚  Ã‚  In analyzing the poem 'The Road Not Taken'; by Robert Frost, it represents 'the classic choice of a moment and a lifetime.';(pg 129) He relies much on the reflections of nature to convey his theme. However, this poem seems to be in essence very simple but opens the door for many interpretations. In using a simple fork in a road, Frost writes much to symbolize life and choices in which one will make. Frost uses unique ability to see an ordinary, everyday activity to portray such a theme. By using such simple endeavors, Frost reaches his audience on a more personal level. However, it is only one's past, present and the attitude with which he or she looks upon the future that determines the shade of light in which the poem will be seen. (pg 621) There is never a straight path for one to follow on life's journey. By using two paths in which to choose from, Frost leaves one to realize that everyone must travel and will reach a point of decision. With stating 'And sorry I could not travel both,'; Frost shows the point in which one will choose because there is only one path in which one may travel. It is most difficult to make a decision on each appealing path because everyone will always seem to question 'what could I or could I not miss out on?'; The fact he is sorry he is sorry he cannot travel, or choose, both paves the way for regret. This will often be reflected upon by an individual in which saying ' what could have been'; leads one to dwelling over the choice of road in which they did not take. In knowing that each one may be influenced in many directions, Frost clearly implies 'And be one traveler, long I stood.'; No matter how each of us may be influenced by family or various sources, there is only 'one traveler'; that will be affected by any decision and there is quite a lengthy thought process involved. Regardless of any outside influence there is only one to be involved and truly affected, as does any choice in life. In somewhat of an attempt to make a decision each person wants to carefully examine the unknown. In using sort of a checks and balances a person would weigh out the risk factor to be involved. Frost uses the line, 'And looked down one as far as I could'; to portray an involved examination. The strain used in 'as far as I could'; symbolizes somewhat of a unknown content of where the path may lead. No matter what one knows... ...o sharply limited.';(pg 496) One would have to agree with his point, because everyone has had to make difficult unalterable decisions of which the outcome could not be foreseen. The narrator must choose between two 'fair'; roads, of which he cannot see the endpoints. Wandering between the two, he finally decides to take the road 'less traveled by.'; Yet, like most people, he later sighs with regret thinking of what he might have missed on the unexplored road. Above all, 'The Road Not Taken'; can truly be interpreted through much symbolism as a clear-sighted representation of two fair choices. The two roads in the poem, although, 'diverging,'; lead in different directions. At the beginning they appear to be somewhat similar, but is apparent that miles away they will grow farther and farther away from each other. Similar to many choices faced in life. It is impossible to foresee the consequences of most major decisions we make and it is often necessary to make these decisions based on a little more than examining which choice 'wanted wear.'; In the end, we look back upon the choices we have made and like the narrator 'sigh,'; observing that they have made 'all the difference.'

Nathaniel Hawthorne and the Great Stone Face

NATHANIEL HAWTHORNE AND THE GREAT STONE FACE RALPH TRANGIA MRS. ARAGON HS4-8 In this paper, every OPINION from someone else has been acknowledge in a parenthetical citation. I realize that the mere presence of a parenthetical citation does not avoid plagiarism. If I have used the exact words, phrases, clauses, or sentences from someone else, I have enclosed that information in quotation marks. If I have paraphrased the opinions of someone else, I have not enclosed the paraphrased portions in quotation marks; but I have stated those opinions in my own words. I have also introduced the paraphrase and have a parenthetical citation to acknowledge the source. ALL FACTUAL INFORMATION (common knowledge or uncontested knowledge), though not credited with a parenthetical citation, has been stated in my sentence structure. I have not used anyone else’s organization of the factual information. Signed:_______________________ Nathaniel Hawthorne And The Great Stone I. Author Background A. Early Life 1. Born in Salem, Massachusets 2. His legs were hit while playing â€Å"bat and ball† 3. Became lame and unable to walk 4. Due to being lame he was able to read many books and this is when he got his some stories B. Education 1. Attended Bowdoin College 2. Became classmate with Longfellow and President F. Pierce 3. Refused to take public speaking C. Career 1. Chosen as the American Adviser at Liverpool England 2. Was given the position as a Surveyor in 1846 D. Achievements 1. Anonymously, Hawthorne’s early stories were published 2. In 1837, the publication of twice told tales somewhat lifted this spell of darkness 3. Hawthorne’s short stories became the best of American classics. . The Great Stone Face 5. Scarlet Letter Nathaniel Hawthorne was one of America’s best writers. Born in Salem, Massachusets on July 4 1804, he grew up with keen awareness of his religious Puritan family, a understanding which inspired many of his works and achievements. He started his career as writer after he graduated in Bowdoin College. For a mean time Hawthorne was picked as surveyor of customs in Salem and later on, a American consul to Liverpool, England. During his free time, he wrote stories and stories.

appeal court essays

appeal court essays Most legal disputes involving state law are initially decided in the trial courts or by an administrative agency. But after such a decision, an individual may turn to the states appeal courts if he or she believes a legal error occurred that harmed the case. In fact, thousands of cases are appealed every year.(1) They include criminal convictions as well as civil cases involving personal injury, contracts, employment, real estate, probate, divorce, child custody and many other issues. Whenever an appellate court reverses a trial court decision, it almost always allows that court to rehear the case using the correct law and procedures. In the vast majority of cases, the decision of a Court of Appeal is final. The state Supreme Court does not review the vast majority of cases it steps in to resolve new or disputed questions of law as well, as to review death penalty cases. Death penalty cases proceed directly to the Supreme Court, bypassing the lower Court of Appeal. The appellate courts of California consist of the Supreme Court and the Courts of Appeal. The judges who serve on these courts are called appellate justices. There are seven justices on the Supreme Court and 93 justices on the Courts of Appeal. The Courts of Appeal are divided into six geographical districts and hear cases arising within the district. Proceedings in appellate courts are very different from those in trial courts. In trial courts a judge or jury hears the testimony of witnesses and reviews physical evidence, exhibits and documents before deciding a case. Appellate courts do not decide an appeal by taking new evidence or reassessing the credibility of the witnesses who testified in the trial court. Instead, they review the written record to determine if the trial court properly interpreted the law and used the correct procedures when considering the case. The opposing parties submit written documents, called briefs, to assert their position....