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Author Straub, F. B.
Source CiteSeerX
Content type Text
File Format PDF
Subject Domain (in DDC) Computer science, information & general works ♦ Data processing & computer science
Subject Keyword Chemical Topography Sidechains Enzyme ♦ Polypeptide Chain ♦ Reactive Sh Group ♦ Appropriate Reagent ♦ Subunit Interaction ♦ Sequence Study ♦ Sidechain Modification ♦ Pancreatic Amylase ♦ Single Residue ♦ Chemical Modification Process ♦ Rigorous Kinetic Analysis ♦ Complex Analysis ♦ Buried Sh Group ♦ Second Reactive Sh Group ♦ Similar Reaction ♦ Sh Group ♦ Structural Flexibility ♦ Native Enzyme ♦ Lactate Dehydrogenase ♦ Active Site ♦ Similar Consideration
Abstract Information concerning the structure and the structural flexibility, the motility, of polypeptide chains in an enzyme may be obtained by use of the method of sidechain modification. Evaluation of such information requires a rigorous kinetic analysis of the chemical modification process. The need to restrict the study to a single residue is emphasized and illustrated with examples. It is shown that the reaction of the second reactive SH group of triosephosphatedehydrogen-ase with an appropriate reagent is the result of the fluctuation of the polypeptide chain in the native enzyme. A similar reaction due to the same cause is described for the reaction of the buried SH group of pancreatic amylase. The complex analysis of the carboxymethylation of aldolase, using correlated kinetic, enzy-mological and sequence studies, has established in the author's laboratory, the relation of a less reactive SH group to the active site. Similar considerations have been applied to the study of SH groups involved in subunit interaction within lactate dehydrogenase.
Educational Role Student ♦ Teacher
Age Range above 22 year
Educational Use Research
Education Level UG and PG ♦ Career/Technical Study