The DOI matches its Crossref record; 77 of the 77 references it cites were found in a registry or an index.
Aspects of Protein Reaction Dynamics: Deviations from Simple Behavior
Abstract
Proteins are complex systems so that their reactions may have characteristics not often observed in small molecules. Two common aspects of small molecule reactions are an exponential time dependence and Arrhenius-like temperature dependence. This review shows that corresponding behavior is not always observed in reactions involving proteins. Bond-making and bond-breaking reactions, as well as conformational changes, which do not involve chemical bonds, are discussed. As examples of bond making, bond breaking reactions, enzyme catalysis by triosephosphate isomerase and ligand binding by myoglobin are considered. Several reactions involving conformational changes are described. They include aromatic side chain rotations, loop/lid opening and closing motions, quaternary structural changes in hemoglobin, and protein folding. In some of these cases, deviations from simple small molecule behavior have been observed, but it is evident that more information is needed for a complete understanding. The protein folding reaction, which is most complex because it involves the entire polypeptide chain, is analyzed in some detail.
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1 retracted
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Structural properties of nanoclusters: Energetic, thermodynamic, and kinetic effects
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Tang, Z., & Kotov, N. A. (2005) · Advanced Materials · doi:10.1002/adma.200401593 · Cited by 770
Binding Affinities of Host–Guest, Protein–Ligand, and Protein–Transition‐State Complexes
Houk, K. N., Leach, A. G., Kim, S. P., & Zhang, X. (2003) · Angewandte Chemie International Edition · doi:10.1002/anie.200200565 · Cited by 586
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Metadata
- Authors
- Karplus, M.
- Venue
- The Journal of Physical Chemistry B
- Publisher
- American Chemical Society (ACS)
- Published
- 1999-12-11
- Volume
- 104
- Issue
- 1
- Pages
- 11-27
- ISSN
- 1520-5207 (ISSN-L)
- 1520-6106
- OpenAlex
- W2064810205
- Cited by
- 306
- References
- 77
- FWCI
- 8.37
- Type
- journal article
- Language
- en
- Open access
- closed
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Bibliographic data: Semantic Scholar, OpenAlex, Crossref.
Contains information from the Semantic Scholar Academic Graph Datasets, made available under the ODC Attribution License (ODC-BY 1.0).
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