Protein Recognition by Synthetic Receptors
Proteins are macromolecules made up of one or more chains of amino acids (polypeptide) and each amino acid in a polypeptide chain links by peptide bond. Major biochemical functions of protein include catalysis (enzymes), molecular switches and structural components of cells and organisms. Each organism has a unique amino acid sequence in their protein that is encoded in their genes. Proteins have four levels of structure.
Primary structure
Twenty, different types of amino acids are present and these amino acids form more than 10000 proteins in human body. The sequence of the different amino acids in a polypeptide chain is known as primary structure.
Secondary structure
This can take the form of α-helix or β-sheets. Hydrogen bonding between -N-H and -C=O groups holds together the secondary structure of protein. In nature most abundant secondary structure is α-helix (over 30%)5. α-helix contains 3.4 amino acid residues in one turn. Side chains of i, i+4, i+7 and i+11 residues are at the same face and form intra molecular H-bond. This bond stabilizes the α-helix structure. β-sheets form inter molecular H-bond with adjacent peptide in either parallel or anti parallel format. Side chains are at perpendicular to the plane of the hydrogen bonding axis.
Tertiary structure
This determines the overall three dimensional shape of a single polypeptide chain molecule and can be stabilized by hydrogen bonds, disulphide bonds.
Quartenary structure
Association of more than one poly peptide chains constitutes the quaternary structure.
Protein Recognition
Proteins play a vital role in most of the biologically important processes for example molecular recognition and catalysis. Molecular recognition is ...
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The complete experimental procedure is available in the General Chemistry Laboratory Manual for CSU Bakersfield, CHEM 213, pages 20-22, 24-25. Experimental data are recorded on the attached data pages.
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It is composed of polymers of amino acids. An enzyme has an optimum pH and temperature. When an enzyme is at its optimum conditions, the rate of reaction is the fastest. In their globular structure, one or more polypeptide chains twist and fold, bringing together a small number of amino acids to form the active site, or the location on the enzyme where the substrate binds and the reaction takes place. An enzyme has an active site, which has a unique shape into which only a substrate of the exact same unique shape can fit.
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We thank the University of Oklahoma and the chemistry faculty for providing the space, instructions, and equipment for the development of this report and experiment.
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