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IntroductionProteins form the majority of the natural catalysts in most of the biological reactions such as in the digestion process The structure of the enzymes determines the activity and the specificity of the protein This field has been widely studied in the form of structure function assays to elucidate how protein-protein interactions occur This practical focuses on the structure of key enzymes in the serine proteases family chymotrypsin and subtilisin The active site of the two enzymes which determines their peptide specificity will be studied with the help of software for manipulating the structure of the proteins enzymesChymotrypsinChymotrypsin belongs to the trypsin family of serine proteases and is usually secreted in inactive form zymogen in the small intestine The structure of chymotrypsin was elucidated via the X-ray crystallography Below is the structure of chymotrypsinogen see f1Figure 1Active sitePeptide specificityMaterials and Methods By the use of Swiss-Pdb Viewer softwareResultsThe complete protein structure of chymotrypsin f2Figure 3the active site groups the residue numbers 57 102 and 195 f3f4Figure 4Figure 5the critical distances between the His and Ser 299A f5Figure 6the critical distances between the His and Asp 270A f6It is a hydrogen bondFigure 7Both Figure 8the bound peptide residues A250-A252 This peptide represents the product peptide following regeneration of the active site the distance from the active Ser oxygen to the C-terminal carbonyl carbon of the peptide 197 A 197 A considered a small distance H N will stabilized the structureFigure 9the positions of the backbone nitrogens The residues are Ser195 and Gly 193the distances from these nitrogens to the peptide carbonyl oxygenIts means its close to do interactionsFigure 10the mouth of the specificity pocket residues 214216 the two loops including positions 185188 and 221225 f10 f11 f12Figure 11Figure 12Figure 13The catalytic triad in subtilisin contains residues 32 64 and 221 the oxyanion hole comprises the sidechain of Asn 155 and the backbone NH of Ser 221 the mouth of the
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