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Journal Article|Research Support, N.I.H., Extramural|Research Support, Non-U.S. Gov't |
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1476 |
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1520-4995
0006-2960 |
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6 |
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1466-1476 |
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Biochemistry |
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1466 |
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Warshel A, Sharma PK, Chu ZT, Aqvist J. Electrostatic contributions to binding of transition state analogues can be very different from the corresponding contributions to catalysis: phenolates binding to the oxyanion hole of ketosteroid isomerase. Biochemistry. 2007 Feb 13;46(6):1466–76. doi: 10.1021/bi061752u. PMID: 17279612. |
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| date |
2007-01-17-04:00^^<http://www.w3.org/2001/XMLSchema#date> |
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https://pubmed.ncbi.nlm.nih.gov/17279612
https://doi.org/10.1021/bi061752u |
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| language |
English |
| source |
https://www.crossref.org/
https://pubmed.ncbi.nlm.nih.gov/ |
| title |
Electrostatic Contributions to Binding of Transition State Analogues Can Be Very Different from the Corresponding Contributions to Catalysis: Phenolates Binding to the Oxyanion Hole of Ketosteroid Isomerase |
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