A simple method for delineating well‐defined and variable regions in protein structures determined from interproton distance data
- 13 July 1987
- journal article
- Published by Wiley in FEBS Letters
- Vol. 219 (1), 11-16
- https://doi.org/10.1016/0014-5793(87)81181-x
Abstract
No abstract availableKeywords
This publication has 19 references indexed in Scilit:
- Application of molecular dynamics with interproton distance restraints to three-dimensional protein structure determinationJournal of Molecular Biology, 1986
- Studies by 1H nuclear magnetic resonance and distance geometry of the solution conformation of the α-amylase inhibitor TendamistatJournal of Molecular Biology, 1986
- Polypeptide fold in the two metal clusters of metallothionein-2 by nuclear magnetic resonance in solutionJournal of Molecular Biology, 1986
- Calculation of protein conformations by proton-proton distance constraintsJournal of Molecular Biology, 1985
- Solution conformation of a heptadecapeptide comprising the DNA binding helix F of the cyclic AMP receptor protein of Escherichia coliJournal of Molecular Biology, 1985
- A protein structure from nuclear magnetic resonance data: lac Repressor headpieceJournal of Molecular Biology, 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
- Conformation of glucagon in a lipid-water interphase by 1H nuclear magnetic resonanceJournal of Molecular Biology, 1983
- Sequential resonance assignments as a basis for determination of spatial protein structures by high resolution proton nuclear magnetic resonanceJournal of Molecular Biology, 1982