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Essay on the structure of protein
Structure of protein essay
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The Structure of Proteins Introduction Campbell and Farrell define proteins as polymers of amino acids that have been covalently joined through peptide bonds to form amino acid chains (61). A short amino acid chain comprising of thirty amino acids forms a peptide, and a longer chain of amino acids forms a polypeptide or a protein. Each of the amino acids making up a protein, has a fundamental design that comprises of a central carbon or alpha carbon that is bonded to a hydrogen element, an amino grouping, a carboxyl grouping, and a unique side chain or the R-group (Campbell and Farrell 61). Proteins serve a myriad of functions whether within or outside of the cells. These functions include structural roles (cytoskeleton), transport of molecules and ions across membranes, catalysis (enzymes), and hormonal roles. Proteins have structural features that can be described at four levels of complexity. This paper summarizes the structure of proteins. Protein Structure Bettelheim, Brown, Campbell and Farrell view proteins as intricate three-dimensional entities whose structural features can be discerned at four levels of increasing complexity (599). These levels are the primary, secondary, tertiary, and quaternary structure levels. The primary structure forms the simplest structures among the four levels. The structure levels become more complex from the secondary to the most organized quaternary protein structure level. 1. Primary Structure of Proteins Bettelheim, Brown, Campbell and Farrell define the primary protein structure as the series of amino acid groups in a polypeptide chain that have been joined through peptide bonds forming the covalent backbone of proteins (599). This structure usually determines the three-dimension... ... middle of paper ... ...clusion, proteins have four structural features including the primary, secondary, tertiary, and quaternary protein structures. The tertiary, quaternary, and secondary structures are the results of proteins being stabilized by electrostatic, covalent, hydrophobic, or hydrogen bonds. These structures are the ones that determine the functions of the proteins through their interactions with other molecules. The function of a protein can be changed through denaturation, a permanent and irreversible process in which it is exposed to heat or extreme PH values. Works Cited Bettelheim, Frederick, William Brown, Mary Campbell, and Shawn Farrell. Introduction to General, Organic, and Biochemistry. 9th ed. Belmont, CA: Brooks/Cole Cengage Learning, 2010. Print. Campbell, Mary, and Shawn Farrell. Biochemistry. 7th ed. Belmont, CA: Brooks/Cole Cengage Learning, 2011. Print.
The shape of the protein chains that produce the building blocks and other structures used in life is mostly determined by weak chemical bonds that are easily broken and remade. These chains can shorten, lengthen, and change shape in response to the input or withdrawal of energy. The changes in the chains alter the shape of the protein and can also alter its function or cause it to become either active or inactive. The ATP molecule can bond to one part of a... ... middle of paper ... ...
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).
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.
Wissmueller S., Font J., Liew C.W., Cram E., Schroeder T., Turner J., Crossley M., Mackay J.P. and Matthews J.M. (2011). Protein-protein interactions: analysis of a false positive GST pulldown result. Proteins. 79 (8), pp. 2365-2371.
Rang, H. P., Dale, M. M., Ritter, J. M., Flower, R. J., & Henderson, G. (2012). Pharmacology (7 ed.). London: Elsevier Inc.
Sansone, Randy A., and Lori A. Sansone. "Abstract." National Center for Biotechnology Information. U.S. National Library of Medicine, n.d. Web. 09 Apr. 2014.
Protein have connection with amino acid to help in functions of: skin, muscle, hair and bones
Schulman, Joshua M., and David E. Fisher. "Abstract." National Center for Biotechnology Information. U.S. National Library of Medicine, 28 Aug. 0005. Web. 24 Apr. 2014.
Pauly, S. (2011, February). News from ABC: changes and challenges. Analytical & Bioanalytical Chemistry. pp. 1003-1004. doi:10.1007/s00216-010-4459-0.
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.
Protein domains occur in large polypeptides, (proteins that have more than 200 residues). These proteins have two or more globular clusters which in turn have domains composed of 100-200 amino acids. Thus many domains are structurally independent units that have the characteristics of small globular proteins.
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...
Each unlike protein is made up of different amino acids set simultaneously in irregular array with about infinite combination. Mainly proteins are huge molecules that might include a number of hundred amino acids given in chains and branches.
Proteins are considered to be the most versatile macromolecules in a living system. This is because they serve crucial functions in all biological processes. Proteins are linear polymers, and they are made up of monomer units that are called amino acids. The sequence of the amino acids linked together is referred to as the primary structure. A protein will spontaneously fold up into a 3D shape caused by the hydrogen bonding of amino acids near each other. This 3D structure is determined by the sequence of the amino acids. The 3D structure is referred to as the secondary structure. There is also a tertiary structure, which is formed by the long-range interactions of the amino acids. Protein function is directly dependent on this 3D structure.
A model is constructed outside of Protein Explorer with tools such as SWISS-Model and Deep View and then the saved PDB file is loaded into Protein Explorer for visualization. Addition of this feature into Protein Explorer will assist the users to determine the unknown structure of a protein and they do not need to use another software for this attempt.