Clinical biochemistry Essay Example | Topics and Well Written Essays - 750 words

Clinical biochemistry - Essay Example ncerned with the whole disease range, and it mainly relies on detection of changes in the various components such as proteins, electrolytes and enzymes in blood serum and the other body fluids (Varcoe 2001). Clinical biochemistry also relies on the laboratory tests carried out on samples of patients’ body fluids. Obesity is an illness that results when the body accumulates excess fats to levels that cause a great deal of effects on the health of the person. This occurs when the body mass index of the person is above 30kg/m2. Obesity is mainly caused by excessive intake of carbohydrates and fats and lack of physical exercise of the body, and in some cases it is genetic while in others, it may result from endocrine disorders and medical complications. Obesity is a major threat to the lives of persons since most people do not realize that they have the condition until it is in its late severe stages. However, obesity can be treated or managed by dieting and doing physical exercises. Other models of managing obesity are the use of medical drugs that many people have opted to use. However, with the advancement and growth in the technological industry; and its wide application in almost every field, in the world, the medical discipline is no exception. The development of equipment that are used in treatment and management of various medical conditions has been a great boost in the fight towards a healthy society. The health of individuals is very critical, and thus the development of the field of clinical biochemistry has really advanced that fight. The incorporation of this advanced technology in the fight against obesity is clearly a great boost to helping the obese patient. The application of the clinical biochemistry technology in dealing with the obese patient is very wide. Biochemical analysis contribute in management of the obese patient since through the various tests carried out on samples of the patient’s blood; the condition is detected. Some of the

Examine the structure and function of proteins Essay

Examine the structure and function of proteins - Essay Example Proteins are amino acids’ polymers, which are covalently bonded through peptide bonds forming a chain.In and outside cells, proteins have several functions including acting as transporters to ferry molecuules and ions across membranes, structural roles for instance cytoskeleton, acting as hormones, 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 structure. These are the primary structure, secondary structure, tertiary structure, and quaternary structu re. 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 bonding 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 involve 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 combined 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-terminus. 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 particular 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 always 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 normally identified by the hydrogen bonding pattern between the key chains of peptide groups (Lukaczer D et