Determination of the positions of bound water molecules in the solution structure of reduced human thioredoxin by heteronuclear three-dimensional nuclear magnetic resonance spectroscopy
- 20 July 1991
- journal article
- research article
- Published by Elsevier in Journal of Molecular Biology
- Vol. 220 (2) , 209-216
- https://doi.org/10.1016/0022-2836(91)90004-p
Abstract
No abstract availableKeywords
This publication has 16 references indexed in Scilit:
- Determination of three‐dimensional structures of proteins from interproton distance data by dynamical simulated annealing from a random array of atoms Circumventing problems associated with foldingPublished by Wiley ,2001
- High-resolution three-dimensional structure of reduced recombinant human thioredoxin in solutionBiochemistry, 1991
- Identification and localization of bound internal water in the solution structure of interleukin 1.beta. by heteronuclear three-dimensional proton rotating-fram Overhauser nitrogen-15-proton multiple quantum coherence NMR spectroscopyBiochemistry, 1990
- Crystal structure of thioredoxin from Escherichia coli at 1.68 Å resolutionJournal of Molecular Biology, 1990
- Studies on the solution conformation of human thioredoxin using heteronuclear nitrogen-15-proton nuclear magnetic resonance spectroscopyBiochemistry, 1990
- A proton nuclear magnetic resonance assignment and secondary structure determination of recombinant human thioredoxinBiochemistry, 1989
- Studies of protein hydration in aqueous solution by direct NMR observation of individual protein-bound water moleculesJournal of the American Chemical Society, 1989
- Determination of Three-Dimensional Structures of Proteins and Nucleic Acids in Solution by Nuclear Magnetic Resonance SpectroscopCritical Reviews in Biochemistry and Molecular Biology, 1989
- Determination of three‐dimensional structures of proteins from interproton distance data by hybrid distance geometry‐dynamical simulated annealing calculationsFEBS Letters, 1988
- Solution conformation of a heptadecapeptide comprising the DNA binding helix F of the cyclic AMP receptor protein of Escherichia coliJournal of Molecular Biology, 1985