Determination of the solution structures of domains II and III of protein G from Streptococcus by 1H nuclear magnetic resonance
- 20 December 1992
- journal article
- Published by Elsevier in Journal of Molecular Biology
- Vol. 228 (4), 1219-1234
- https://doi.org/10.1016/0022-2836(92)90328-h
Abstract
No abstract availableKeywords
This publication has 22 references indexed in Scilit:
- Localization of bound water in the solution structure of the immunoglobulin binding domain of streptococcal protein G: Evidence for solvent-induced helical distortion in solutionJournal of Molecular Biology, 1992
- Similarity of Protein G and UbiquitinScience, 1991
- Sequential proton NMR assignments and secondary structure of an IgG-binding domain from protein GBiochemistry, 1991
- High-resolution three-dimensional structure of reduced recombinant human thioredoxin in solutionBiochemistry, 1991
- Efficient computation of three-dimensional protein structures in solution from nuclear magnetic resonance data using the program DIANA and the supporting programs CALIBA, HABAS and GLOMSAJournal of Molecular Biology, 1991
- Determination of three‐dimensional structures of proteins from interproton distance data by hybrid distance geometry‐dynamical simulated annealing calculationsFEBS Letters, 1988
- Structure of ubiquitin refined at 1.8 Å resolutionJournal of Molecular Biology, 1987
- Solvation energy in protein folding and bindingNature, 1986
- Molecular dynamics of native proteinJournal of Molecular Biology, 1983
- Packing of α-Helices onto β-Pleated sheets and the anatomy of proteinsJournal of Molecular Biology, 1980