Probing protein structure by solvent perturbation of NMR spectra: the surface accessibility of bovine pancreatic trypsin inhibitor
- 31 July 1997
- journal article
- research article
- Published by Elsevier in Biophysical Journal
- Vol. 73 (1) , 382-396
- https://doi.org/10.1016/s0006-3495(97)78078-0
Abstract
No abstract availableKeywords
This publication has 25 references indexed in Scilit:
- Structure of form III crystals of bovine pancreatic trypsin inhibitorJournal of Molecular Biology, 1987
- Secondary structure determination of human .beta.-endorphin by proton NMR spectroscopyBiochemistry, 1987
- Protein structures in solution by nuclear magnetic resonance and distance geometryJournal of Molecular Biology, 1987
- Two-dimensional proton NMR of three spin-labeled derivatives of bovine pancreatic trypsin inhibitorBiochemistry, 1986
- Amide‐proton exchange studies by two‐dimensional correlated 1H NMR in two chemically modified analogs of the basic pancreatic trypsin inhibitorEuropean Journal of Biochemistry, 1984
- Interaction of beta-endorphin with sodium dodecyl sulfate in aqueous solution 1H-NMR investigationEuropean Journal of Biochemistry, 1984
- Distances of tyrosine residues from a spin-label hapten in the combining site of a specific monoclonal antibodyBiochemistry, 1984
- Distance measurements in spin-labeled lysozymeBiochemistry, 1984
- Carbon-13 nuclear magnetic resonance relaxation studies of internal mobility of the polypeptide chain in basic pancreatic trypsin inhibitor and a selectively reduced analogBiochemistry, 1980
- Spin-label-induced nuclear relaxation. Distances between bound saccharides, histidine-15, and tryptophan-123 on lysozyme in solutionBiochemistry, 1972