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Umeyama, H., Hirono, S., Nakagawa, S. (1984) Charge state of His-57-Asp-102 couple in a transition state analogue-trypsin complex: a molecular orbital study. Proceedings of the National Academy of Sciences, 81 (20) 6266-6270 doi:10.1073/pnas.81.20.6266

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Reference TypeJournal (article/letter/editorial)
TitleCharge state of His-57-Asp-102 couple in a transition state analogue-trypsin complex: a molecular orbital study.
JournalProceedings of the National Academy of Sciences
AuthorsUmeyama, H.Author
Hirono, S.Author
Nakagawa, S.Author
Year1984 (October 1)Volume81
Issue20
PublisherProceedings of the National Academy of Sciences
DOIdoi:10.1073/pnas.81.20.6266Search in ResearchGate
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Mindat Ref. ID1437528Long-form Identifiermindat:1:5:1437528:8
GUID0
Full ReferenceUmeyama, H., Hirono, S., Nakagawa, S. (1984) Charge state of His-57-Asp-102 couple in a transition state analogue-trypsin complex: a molecular orbital study. Proceedings of the National Academy of Sciences, 81 (20) 6266-6270 doi:10.1073/pnas.81.20.6266
Plain TextUmeyama, H., Hirono, S., Nakagawa, S. (1984) Charge state of His-57-Asp-102 couple in a transition state analogue-trypsin complex: a molecular orbital study. Proceedings of the National Academy of Sciences, 81 (20) 6266-6270 doi:10.1073/pnas.81.20.6266
In(1984, October) Proceedings of the National Academy of Sciences Vol. 81 (20) Proceedings of the National Academy of Sciences

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Krajewski, W. W., Jones, T. A., Mowbray, S. L. (2005) Structure of Mycobacterium tuberculosis glutamine synthetase in complex with a transition-state mimic provides functional insights. Proceedings of the National Academy of Sciences, 102 (30) 10499-10504 doi:10.1073/pnas.0502248102
Tate, S. S., Meister, A. (1978) Serine-borate complex as a transition-state inhibitor of gamma-glutamyl transpeptidase. Proceedings of the National Academy of Sciences, 75 (10) 4806-4809 doi:10.1073/pnas.75.10.4806
Kokubun, S., Reuter, H. (1984) Dihydropyridine derivatives prolong the open state of Ca channels in cultured cardiac cells. Proceedings of the National Academy of Sciences, 81 (15) 4824-4827 doi:10.1073/pnas.81.15.4824
Christianson, D. W., Lipscomb, W. N. (1985) Binding of a possible transition state analogue to the active site of carboxypeptidase A. Proceedings of the National Academy of Sciences, 82 (20) 6840-6844 doi:10.1073/pnas.82.20.6840
Brill, A. S., Sandberg, H. E. (1967) SPIN-STATE-DEPENDENT HEMOPROTEIN ULTRAVIOLET-ABSORPTION BANDS. Proceedings of the National Academy of Sciences, 57 (1) 136-140 doi:10.1073/pnas.57.1.136
Kozlowski, K. A., Wezeman, F. H., Schultz, R. M. (1984) Tumor cell proteinase visualization and quantification using a fluorescent transition-state analog probe. Proceedings of the National Academy of Sciences, 81 (4) 1135-1139 doi:10.1073/pnas.81.4.1135
Subramaniam, S., Marti, T., Khorana, H. G. (1990) Protonation state of Asp (Glu)-85 regulates the purple-to-blue transition in bacteriorhodopsin mutants Arg-82----Ala and Asp-85----Glu: the blue form is inactive in proton translocation. Proceedings of the National Academy of Sciences, 87 (3) 1013-1017 doi:10.1073/pnas.87.3.1013
Takagi, M., Fukui, T., Shimomura, S. (1982) Catalytic mechanism of glycogen phosphorylase: pyridoxal(5')diphospho(1)-alpha-D-glucose as a transition-state analogue. Proceedings of the National Academy of Sciences, 79 (12) 3716-3719 doi:10.1073/pnas.79.12.3716
Auerbach, A. (2005) Gating of acetylcholine receptor channels: Brownian motion across a broad transition state. Proceedings of the National Academy of Sciences, 102 (5) 1408-1412 doi:10.1073/pnas.0406787102
Ghosh, S. K., Berkowitz, M., Parr, R. G. (1984) Transcription of ground-state density-functional theory into a local thermodynamics. Proceedings of the National Academy of Sciences, 81 (24) 8028-8031 doi:10.1073/pnas.81.24.8028
Borchers, C. H., Marquez, V. E., Schroeder, G. K., Short, S. A., Snider, M. J., Speir, J. P., Wolfenden, R. (2004) Fourier transform ion cyclotron resonance MS reveals the presence of a water molecule in an enzyme transition-state analogue complex. Proceedings of the National Academy of Sciences, 101 (43) 15341-15345 doi:10.1073/pnas.0406781101
 
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