Substrate activation by non-covalent binding in the active site of chymotrypsin
نویسندگان
چکیده
منابع مشابه
Active Site of alpha-Chymotrypsin Activation by Association-Desolvation.
High reactivity toward alpha-chymotrypsin is observed for derivatives of beta-arylpropionic acids of varied structure-L-alpha-acylamido compounds, D-cyclized compounds, and, now, L-glycolamide esters. Compensating enthalpy and entropy effects are observed which appear to be caused by changes in water of solvation. High reactivity with varied structure, and physical evidence, appear to rule out ...
متن کاملStudies on the Active Site of Chymotrypsin.
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this study investigates the cohesive devices used in the textbook of english for the students of psychology. the research questions and hypotheses in the present study are based on what frequency and distribution of grammatical and lexical cohesive devices are. then, to answer the questions all grammatical and lexical cohesive devices in reading comprehension passages from 6 units of 21units th...
The Specific Binding of Biebrich Scarlet to the Active Site of a-Chymotrypsin*
This paper reports on the presence of a strong binding site for the dye Biebrich Scarlet, (6-[Z-hydroxy-l-naphthyl]azo)3,4’-azodibenzene sulfonic acid, on cr-chymotrypsin. The 1: 1 protein-dye complex is characterized by a Kdiss of 8.8 f 0.1 X 10U5 M in 0.1 M phosphate buffer at pH 7.6 and W’. Complex formation is associated with a red shift in the visible spectrum of the dye, and a characteris...
متن کاملThe Specific Binding of Biebrich Scarlet to the Active Site of a-Chymotrypsin*
This paper reports on the presence of a strong binding site for the dye Biebrich Scarlet, (6-[Z-hydroxy-l-naphthyl]azo)3,4’-azodibenzene sulfonic acid, on cr-chymotrypsin. The 1: 1 protein-dye complex is characterized by a Kdiss of 8.8 f 0.1 X 10U5 M in 0.1 M phosphate buffer at pH 7.6 and W’. Complex formation is associated with a red shift in the visible spectrum of the dye, and a characteris...
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ژورنال
عنوان ژورنال: FEBS Letters
سال: 1970
ISSN: 0014-5793
DOI: 10.1016/0014-5793(70)80314-3