Mechanisms of cooperativity and allosteric regulation in proteins
Author(s)
Bibliographic Information
Mechanisms of cooperativity and allosteric regulation in proteins
Cambridge University Press, 1990
- : pbk
Available at / 15 libraries
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INTERNATIONAL CHRISTIAN UNIVERSITY LIBRARY図
: pbk464.9/P432m,464.9/P432m03992424,
464.9/P432m03992424 -
Graduate School of Pharmaceutical Sciences, Pharmaceutical Sciences Library, University of Tokyo図書
: pbk439.4:P435810171180
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Note
Bibliography: p. 86-98
Includes index
Description and Table of Contents
Description
In this book Max Perutz, who won the Nobel Prize in 1962 for his work on the structure of haemoglobin, shows how the functions of several allosteric proteins can be understood on the basis of their molecular mechanisms.
Table of Contents
Preface 1. Introduction 2. Haemoglobin: Dependence of allosteric equilibrium on spin state and coordination of the haem iron 3. Haemocyanin: Dependence of allosteric equilibrium on coordination and valency of a binuclear copper complex 4. Haemerythrin: Cooperativity in a binuclear iron complex 5. Glycogen phosphorylase: Control of glycolysis 6. Phosphofructokinase: Further control of glycolysis 7. Feedback inhibition of a biosynthetic pathway: Aspartate Transcarbamoylase 8. Control of nitrogen metabolism: Glutamine synthetase 9. Cooperativity and feedback inhibition without change of quaternary structure: The "trp" and "met" repressors of E. Coli 10. Immunoglobulins: Cooperative binding to multivalent antigens 11. Allosteric membrane proteins.
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