Note to users. If you're seeing this message, it means that your browser cannot find this page's style/presentation instructions -- or possibly that you are using a browser that does not support current Web standards. Find out more about why this message is appearing, and what you can do to make your experience of our site the best it can be.

Site Tools

  • AAAS
  • Subscribe
  • Feedback

Site Search

Search Advanced

Science 6 January 1989:
Vol. 243. no. 4887, pp. 45 - 50
DOI: 10.1126/science.2911719
Prev | Table of Contents | Next

Articles

Science, Vol 243, Issue 4887, 45-50
Copyright © 1989 by American Association for the Advancement of Science

articles

Protein structure determination in solution by nuclear magnetic resonance spectroscopy

K Wuthrich

Eidgenossiche Technische Hochschule, Zurich, Switzerland.

Knowledge of three-dimensional protein structures is one of the foundations of protein design and protein engineering. Nuclear magnetic resonance spectroscopy was recently introduced as a second method for protein structure determination, in addition to the well-established diffraction techniques with protein single crystals. This new approach enables one to carry out detailed structural studies of proteins in solution and other noncrystalline states, which may be similar or identical to the physiological environment, and promises new insights into the dynamics of protein molecules and the protein-folding problem.


THIS ARTICLE HAS BEEN CITED BY OTHER ARTICLES:
Characterisation of transition state structures for protein folding using 'high', 'medium' and 'low' {Phi}-values.
C. D. Geierhaas, X. Salvatella, J. Clarke, and M. Vendruscolo (2008)
Protein Eng. Des. Sel. 21, 215-222
   Abstract »    Full Text »    PDF »
A PDZ domain recapitulates a unifying mechanism for protein folding.
S. Gianni, C. D. Geierhaas, N. Calosci, P. Jemth, G. W. Vuister, C. Travaglini-Allocatelli, M. Vendruscolo, and M. Brunori (2007)
PNAS 104, 128-133
   Abstract »    Full Text »    PDF »
Solution NMR Structure Investigation for Releasing Mechanism of Neocarzinostatin Chromophore from the Holoprotein.
H. Takashima, T. Yoshida, T. Ishino, K. Hasuda, T. Ohkubo, and Y. Kobayashi (2005)
J. Biol. Chem. 280, 11340-11346
   Abstract »    Full Text »    PDF »
Probing solvent accessibility of amyloid fibrils by solution NMR spectroscopy.
J. H. Ippel, A. Olofsson, J. Schleucher, E. Lundgren, and S. S. Wijmenga (2002)
PNAS 99, 8648-8653
   Abstract »    Full Text »    PDF »
Hydration of Biological Macromolecules in Solution: Surface Structure and Molecular Recognition.
K. Wuthrich (1993)
Cold Spring Harb Symp Quant Biol 58, 149-157
   Abstract »    PDF »
NMR determination of residual structure in a urea-denatured protein, the 434-repressor.
D Neri, M Billeter, G Wider, and K Wuthrich (1992)
Science 257, 1559-1563
   Abstract »    PDF »
Combining experimental information from crystal and solution studies: joint X-ray and NMR refinement.
B Shaanan, A. Gronenborn, G. Cohen, G. Gilliland, B Veerapandian, D. Davies, and G. Clore (1992)
Science 257, 961-964
   Abstract »    PDF »
Protein hydration in aqueous solution.
G Otting, E Liepinsh, and K Wuthrich (1991)
Science 254, 974-980
   Abstract »    PDF »
Structures of larger proteins in solution: three- and four-dimensional heteronuclear NMR spectroscopy.
G. Clore and A. Gronenborn (1991)
Science 252, 1390-1399
   Abstract »    PDF »
An antibody binding site on cytochrome c defined by hydrogen exchange and two-dimensional NMR.
Y Paterson, S. Englander, and H Roder (1990)
Science 249, 755-759
   Abstract »    PDF »
Transmembrane protein structure: spin labeling of bacteriorhodopsin mutants.
C Altenbach, T Marti, H. Khorana, and W. Hubbell (1990)
Science 248, 1088-1092
   Abstract »    PDF »
Some Developments in Nuclear Magnetic Resonance of Solids.
B. F. Chmelka, B. F. CHMELKA, and A. PINES (1989)
Science 246, 71-77
   Abstract »    PDF »


To Advertise     Find Products

Science. ISSN 0036-8075 (print), 1095-9203 (online)