Examine the structure and function of proteins Essay

Examine the structure and function of proteins - Essay ExampleProteins atomic number 18 amino group acids polymers, which are covalently bonded through peptide bonds forming a chain.In and outside cells, proteins prolong several functions including acting as transporters to ferry molecuules and ions across membranes, structural roles for instance cytoskeleton, acting as horm angiotensin-converting enzymes, and catalyzing other biological body reactions Biotechnology entails understanding, exploiting, and modifying proteins for useful purposes. In order to accomplish this, one needs to understand various fuctions of proteins and their structure. The focus of this paper is to summarize various structures of proteins, various funcions of protein molecule in the cell, the link between molecular structure of proteins and their function, and how proteins as a whole contribute to health and/or disease. Studies conducted in this field have shown that there are four categories of protein st ructure. These are the primary structure, supplemental structure, tertiary structure, and quaternary structure. The amino acids are made up of a backbone section which is available in the different types of amino acids, together with a side chain for each residue (Nelson, L. & Cox, M. 2008). Since the carbon atom remains bound to the four categories, one isomer would happen in the biological protein. In this case, the molecules would be chiral. Glycine fails to be chiral due to the fact that it has a side chain that is an atom of hydrogen. The amino acids are bonded by a covalent bond chain which are referred to as the peptide bonds (Brown EC et al. 2004). Whenever the chain is short, such a chain is called a peptide. The chains that are long are referred to as proteins or polypeptides. In many cases, the peptide bind is established in between the one amino acid carboxyl group together with the amino group. The bonding of peptides happens in the reactions of condensation, which in volve the loss of a molecule of water. Primary structure of proteins. The primary structure proteins is the amino acid polypeptide chain sequence. The basic structure is have together using the covalent bonding just like the case of the peptide bonds, which are often established in the translation process of proteins. The two ends of a polypeptides are referred to as the C- period. In this, the carboxyl terminus, and the N-terminus are the amino terminus (Mahn K et al. 2005). In order to count the residues, one would begin at the N-terminus, which involves the terminus where the group of amino acid fails to be involved in the peptide boding (Nelson, L. & Cox, M. 2008). This type of structure is identified by the corresponding gene to the protein molecule. A particular nucleotide sequence in DNA is normally shifted to the mRNA that is interpreted by ribosome in a process referred to as translation (Mahn K et al. 2005). In this case, the protein sequence is specific to the particula r protein, and identifies the structure and the roles of the protein molecule. Protein sequence could be determined through tandem spectrometry tandem mass, and Ednan degradation (Nelson, L. & Cox, M. 2008). In most cases, it is unendingly interpreted directly from the gene sequence through the utility of the genetic code. The post-translational modifications including the formation of disulfide, glycosylation, is considered as a section of the primary structure hence cannot be identified from the specific gene. For instance Insulin has fifty one amino acids classified in two chains, one having thirty one amino acids, and the other one having twenty amino acids (Mahn K et al. 2005). The primary structure is displayed in diagram 1. Diagram 1. Secondary structure. This is the second structure of proteins displaying the regular local sub-structures. The two categories of secondary structure include the betastrand, and the alpha helix (Nelson, L. & Cox, M. 2008). These structures are n ormally identified by the hydrogen bonding pattern between the key chains of peptide groups (Lukaczer D et