Structure refinement of a cyclic peptide from two-dimensional NMR data and molecular modeling
- 7 April 1987
- journal article
- research article
- Published by American Chemical Society (ACS) in Biochemistry
- Vol. 26 (7) , 1851-1859
- https://doi.org/10.1021/bi00381a010
Abstract
Note: In lieu of an abstract, this is the article's first page.This publication has 14 references indexed in Scilit:
- Synthesis and biological activity of pentapeptide analogs of the potent angiotensin converting enzyme inhibitor 5(S)-benzamido-4-oxo-6-phenylhexanoyl-L-prolineJournal of Medicinal Chemistry, 1985
- Dynamics and Conformational Energetics of a Peptide Hormone: VasopressinScience, 1985
- Solution conformation of proteinase inhibitor IIA from bull seminal plasma by 1H nuclear magnetic resonance and distance geometryJournal of Molecular Biology, 1985
- An evaluation of the combined use of nuclear magnetic resonance and distance geometry for the determination of protein conformations in solutionJournal of Molecular Biology, 1985
- Structure of ethanol-inhibited porcine pepsin at 2-A resolution and binding of the methyl ester of phenylalanyl-diiodotyrosine to the enzyme.Journal of Biological Chemistry, 1984
- Structure and refinement of penicillopepsin at 1.8 Å resolutionJournal of Molecular Biology, 1983
- Three-dimensional structure of the complex of the Rhizopus chinensis carboxyl proteinase and pepstatin at 2.5 .ANG. resolutionBiochemistry, 1982
- Comparative model-building of the mammalian serine proteasesJournal of Molecular Biology, 1981
- Computer simulation of the conformational properties of oligopeptides. Comparison of theoretical methods and analysis of experimental resultsJournal of the American Chemical Society, 1979
- Consistent force field studies of intermolecular forces in hydrogen-bonded crystals. 1. Carboxylic acids, amides, and the C:O.cntdot..cntdot..cntdot.H- hydrogen bondsJournal of the American Chemical Society, 1979