Proteins are the most abundant molecules in animals, playing important roles in all aspects of cell structure and function (Wamser, 2009). When a polymer of different amino acids are joined by a peptide bonds it will formed a protein molecule. Amino acids, is the word that comes from the words ‘amino’ and ‘carboxylic acids’. These two words are related to each other where amino itself is derive from carboxylic acids. There are twenty common amino acids can be found in almost all proteins and it is divided into three major groups which are differentiating based on their characteristics. Kundu (2005), in their study on the amino acids network within protein states that protein structures is made of three classes of amino acids, known as hydrophobic (non-polar), hydrophilic (polar uncharged) and polar charged (refer to Figure 1 in Appendix 1). The first type of amino acids is non-polar amino acids. Orphardt (2003) mentioned that non-polar are side chains which have pure hydrocarbon alkyl groups (alkane branches) or aromatic (benzene rings). Examples include valine (Val), alanine (Ala), leucine (Leu), isoleucine (Ile), and phenylalanine (Phe). They are function as maintaining the three-dimensional structures of protein. Aliphatic or aromatic groups can be as R groups of these amino acids. This makes them hydrophobic (water fearing). In aqueous solutions, globular protein will fold into a three-dimensional shape to bury these hydrophobic side chains in the protein interior (Reddy, 2014). Non-polar of amino acid compound can be determined by high performance liquid chromatography. Molnar (1977) mentioned that there is mechanism that being used to detect the subunit of protein including other small peptide. The second type of... ... middle of paper ... ...nary phases by high-performance liquid chromatography. Journal of chromatography. 142, 623. Moran, L.A., Horton, H.R., Scrimgeour, K.G., & Perry, M.D. (1996). Principles of Biochemistry. Glenview, USA: Pearson Education Inc. Orphardt, C.E. (2003). Characteristics and properties of amino acids. Retrieved from http://www.elmhurst.edu/~chm/vchembook/561aminostructure.html. Pratt, C. W. & Cornely, K. (2004). Essential biochemistry. USA: John Wiley & Sons. Rao, B.M., Bhandore, P., & Rao, N.S (2010). Determination of amino acid without derivatization by using HPLC-HILIC column.Journal of Chemical and Pharmaceutical Research, 2(2) , 372-380 Reddy, K.M. (2014). Group 1: non polar amino acids. Retrieved from http://global.britannica.com/EBchecked/topic/20691/amino-acid/277264/Group-I-Nonpolar-amino-acids. Wamser, C. C. (2009). Organic Chemistry III. New York, NY: Pearson.
Moreover, the class average curve shows a similar trend, as the curve flattens, at 70% but with an enzyme activity of 5.3 x10-3 seconds. This indicates that even though the saturation point is the same it was considerably lower than our results, which could indicate sources of systematic error in the design of the practical.
The primary structure is the sequence of amino acids that make up a polypeptide chain. 20 different amino acids are found in proteins. The exact order of the amino acids in a specific protein is the primary sequence for that protein. [IMAGE] [IMAGE]Protein secondary structure refers to regular, repeated patterns of folding of the protein backbone. The two most common folding patterns are the alpha helix and the beta sheet.
The following essay will outline the 1983 Nobel Prize winner Paul Berg, for his studies of the biochemistry of nucleic acids and recombinant-DNA. The reason why I chose Paul Berg as my Nobel Laureate was because his findings won him the Nobel Prize in the field of Biochemistry. Since he won the prize for Biochemistry, his findings will cover both Biology and Chemistry, which will help me in two of my NCUK courses. In the essay, a discussion consisting of Berg’s biography, research, and the science behind his winning will be covered. Also, a summary of the essay and a critical evaluation will be discussed.
Due to the nature of amino acids, a titration curve can be employed to identify
Zisser, Howard C. "Abstract." National Center for Biotechnology Information. U.S. National Library of Medicine, 13 Sept. 2010. Web. 06 Jan. 2014.
Conditionally essential amino acids: this are present in many foods, but are not always required to be a part of the daily diet. So long as we successfully absorb sufficient amounts of the essential amino acids, the liver is able to synthesise the remaining others conditionally amino acids. At certain times in life and in certain population groups these amino acids must be supplied by the diet to ensure good health. An adequate intake of the conditionally essential amino acids will also help to spare valuable resources of essential amino acids.
n.d. - n.d. Peptides and Proteins. Proteins. Retrieved July 25, 2008, from http://www.cd http://www.cem.msu.edu/reusch/VirtualText/protein2.htm Ophardt, C. E. (2003).
Michener, William K. and Haeuber, Richard A., Bioscience. American Institute of Biological Science. Sep98. Vol. 48. Issue 9. p677.
In total, there are around 20 amino acids that the human body uses to build proteins.
Each protein is a large complex molecule; these molecules are made up of. of a string of amino acids. There are 20 different amino acids that occur naturally to form proteins and they all have the same basic structure. The. The 20 amino acids the body needs can be linked in.
Hydrogen bonding- this bonding occurs between the hydrogen and oxygen or nitrogen between amino acids opposite each other. This bond occurs because the oxygen is slightly negative and the nitrogen/hydrogen is slightly positive so there is an attraction between them when they come close together. This is a fairly weak bond however it forms a vital part in helping the structure stay strong and in the right
Hydrolysis of aspartame under acidic or basic conditions results in aspartic acid, phenylalanine and methanol. Several solutions can be prepared in order to study the amino acids of aspartame. With TLC analysis, we were able to observe the polarity of each of the solutions prepared. Out of all the solutions, aspartic acid has the lowest Rf value because it is a charged amino acid, therefore it is polar. The solution with the highest Rf is phenylalanine because it is a hydrophobic amino acid.
Pauly, S. (2011, February). News from ABC: changes and challenges. Analytical & Bioanalytical Chemistry. pp. 1003-1004. doi:10.1007/s00216-010-4459-0.
There are four main levels of a protein, which make up its native conformation. The first level, primary structure, is just the basic order of all the amino acids. The amino acids are held together by strong peptide bonds. The next level of protein organization is the secondary structure. This is where the primary structure is repeated folded so that it takes up less space. There are two types of folding, the first of which is beta-pleated sheets, where the primary structure would resemble continuous spikes forming a horizontal strip. The seco...
If proteins are the building blocks of life, then amino acids are the building blocks of proteins. Plant cells form amino acids from the compounds which the plant draws up from the ground, such as the nitrates and ammonia salts. Animals, however, cannot perform this conversion of simple inorganic substances to amino acids, so they must ingest them in the form of food-- with herbivorous animals consuming plant proteins in vegetables and carnivorous animals consuming animal proteins in the bodies of their prey.