The Role of Mobility in the Substrate Binding and Catalytic Machinery of Enzymes
- 1 January 1983
- book chapter
- Published by Wiley in Novartis Foundation Symposia
- Vol. 93, 4-24
- https://doi.org/10.1002/9780470720752.ch2
Abstract
This chapter contains section titled: Enzymes As Machines Proteins are Flexible in the Crystalline State The Problem of Ligand Access The Problem of Response to Changing Substrate Structure When Tight Binding is Not So Tight Directed Fluctuations: Fact or Fantasy? Conclusion: Enzyme Mobility is Important for Enzyme Function ReferencesThis publication has 17 references indexed in Scilit:
- On the disordered activation domain in trypsinogen: chemical labelling and low-temperature crystallographyActa Crystallographica Section B: Structural Science, Crystal Engineering and Materials, 1982
- X‐Ray CryoenzymologyPublished by Wiley ,1981
- Conformational flexibility and its functional significance in some protein moleculesTrends in Biochemical Sciences, 1979
- Crystallographic studies of the dynamic properties of lysozymeNature, 1979
- A simple hydrogen exchange method for cross-linked protein crystalsCarlsberg Research Communications, 1979
- Perfection in enzyme catalysis: the energetics of triosephosphate isomeraseAccounts of Chemical Research, 1977
- Crystal structure of bovine trypsinogen at 1·8 Å resolutionJournal of Molecular Biology, 1977
- A restrained-parameter structure-factor least-squares refinement procedure for large asymmetric unitsActa Crystallographica Section A, 1976
- Structure of chicken muscle triose phosphate isomerase determined crystallographically at 2.5Å resolution: using amino acid sequence dataNature, 1975
- Solvent content of protein crystalsJournal of Molecular Biology, 1968