Crystal and molecular structure of the bovine α-chymotrypsin-eglin c complex at 2.0 Å resolution-Reference-Cited by-同舟云学术

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Crystal and molecular structure of the bovine α-chymotrypsin-eglin c complex at 2.0 Å resolution

Published:1992-05 Issue:1 Volume:225 Page:107-123
ISSN:0022-2836
Container-title:Journal of Molecular Biology
language:en
Short-container-title:Journal of Molecular Biology

Author:

Frigerio Francesco,Coda Alessandro,Pugliese Luisa,Lionetti Claudia,Menegatti Enea,Amiconi Gino,Schnebli Hans Peter,Ascenzi Paolo,Bolognesi Martino

Publisher

Elsevier BV

Subject

Molecular Biology,Structural Biology

Reference61 articles.

1. Enthalpy-entropy compensation phenomena in serine (pro)enzyme: inhibitor complex formation;Amiconi;Advan. Biosci,1987

2. Interaction between serine pro(enzymes) and macromolecular inhibitors. Thermodynamic and kinetic aspects;Amiconi,1988

3. Transient removal of proflavine inhibition of bovine β-trypsin by the basic pancreatic trypsin inhibitor (Kunitz) A case for chronosteric effect;Antonini;J. Biol. Chem,1983

4. Binding of Kunitz and eglin c inhibitors to serine proteinases: thermodynamic, kinetic and molecular aspects;Ascenzi;J. Mol. Catal,1988

5. Binding of the recombinant proteinase inhibitor eglin c from leech Hirudo medicinalis to human leukocyte elastase, bovine α-chymotrypsin and subtilisin Carlsberg: thermodynamic study;Ascenzi;J. Enz. Inhibit,1988

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