NMR analysis of main-chain conformational preferences in an unfolded fibronectin-binding protein
- 1 November 1997
- journal article
- editorial
- Published by Elsevier in Journal of Molecular Biology
- Vol. 274 (2) , 152-159
- https://doi.org/10.1006/jmbi.1997.1369
Abstract
No abstract availableKeywords
This publication has 52 references indexed in Scilit:
- Analysis of Main Chain Torsion Angles in Proteins: Prediction of NMR Coupling Constants for Native and Random Coil ConformationsJournal of Molecular Biology, 1996
- NACP, A Protein Implicated in Alzheimer's Disease and Learning, Is Natively UnfoldedBiochemistry, 1996
- Comparison between the φ Distribution of the Amino Acids in the Protein Database and NMR Data Indicates that Amino Acids have Various φ Propensities in the Random Coil ConformationJournal of Molecular Biology, 1995
- Elucidating the Folding Problem of Helical Peptides using Empirical Parameters. II†. Helix Macrodipole Effects and Rational Modification of the Helical Content of Natural PeptidesJournal of Molecular Biology, 1995
- Stabilization of a type VI turn in a family of linear peptides in water solutionJournal of Molecular Biology, 1994
- Helix propensities of the amino acids measured in alanine‐based peptides without helix‐stabilizing side‐chain interactionsProtein Science, 1994
- Local Structure Due to an Aromatic-Amide Interaction Observed by 1H-Nuclear Magnetic Resonance Spectroscopy in Peptides Related to the N Terminus of Bovine Pancreatic Trypsin InhibitorJournal of Molecular Biology, 1993
- Relationship between nuclear magnetic resonance chemical shift and protein secondary structureJournal of Molecular Biology, 1991
- HMQC-NOESY-HMQC, a three-dimensional NMR experiment which allows detection of nuclear overhauser effects between protons with overlapping signalsJournal of Magnetic Resonance (1969), 1990
- Calibration of the angular dependence of the amide proton-Cα proton coupling constants, 3JHNα, in a globular proteinJournal of Molecular Biology, 1984