The binding of a non-specific ‘transition state analogue’ to α-chymotrypsin
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چکیده
منابع مشابه
from linguistics to literature: a linguistic approach to the study of linguistic deviations in the turkish divan of shahriar
chapter i provides an overview of structural linguistics and touches upon the saussurean dichotomies with the final goal of exploring their relevance to the stylistic studies of literature. to provide evidence for the singificance of the study, chapter ii deals with the controversial issue of linguistics and literature, and presents opposing views which, at the same time, have been central to t...
15 صفحه اولAtomic dissection of the hydrogen bond network for transition-state analogue binding to purine nucleoside phosphorylase.
Immucillin-H (ImmH) and immucillin-G (ImmG) were previously reported as transition-state analogues for bovine purine nucleoside phosphorylase (PNP) and are the most powerful inhibitors reported for the enzyme (K(i) = 23 and 30 pM). Sixteen new immucillins are used to probe the atomic interactions that cause tight binding for bovine PNP. Eight analogues of ImmH are identified with equilibrium di...
متن کاملEnzymatic transition state theory and transition state analogue design.
The incredible catalytic rate enhancements caused by enzymes led Linus Pauling (1) to suggest that enzymes bind tightly to substrates distorted toward the transition state, thereby concentrating them and enforcing catalysis. Wolfenden (2) explained that chemically stable analogues that resemble the transition state would be expected to bind more tightly than substrate by factors resembling the ...
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...
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: 1975
ISSN: 0014-5793
DOI: 10.1016/0014-5793(75)81037-4