Solid-state NMR studies of proteins: the view from static 2H NMR experiments
- PMID: 9923710
- DOI: 10.1139/bcb-76-2-3-411
Solid-state NMR studies of proteins: the view from static 2H NMR experiments
Abstract
The application of solid-state 2H NMR spectroscopy to the study of protein and peptide structure and dynamics is reviewed. The advantages of solid-state NMR for the study of proteins are considered, and the particular advantages of solid-state 2H NMR are summarized. Examples of work on the integral membrane protein bacteriorhodopsin, and the membrane peptide gramicidin, are used to highlight the major achievements of the 2H NMR technique. These examples demonstrate that through the use of oriented samples, it is possible to obtain both structural and dynamic information simultaneously.
Similar articles
-
Dynamics of an integral membrane peptide: a deuterium NMR relaxation study of gramicidin.Biophys J. 1994 May;66(5):1429-40. doi: 10.1016/S0006-3495(94)80933-6. Biophys J. 1994. PMID: 7520294 Free PMC article.
-
Determination of membrane Peptide orientation by 1H-detected 2H NMR spectroscopy.J Magn Reson. 2002 Apr;155(2):244-50. doi: 10.1006/jmre.2002.2517. J Magn Reson. 2002. PMID: 12036335
-
Structure determination of the cyclohexene ring of retinal in bacteriorhodopsin by solid-state deuterium NMR.Biochemistry. 1992 Oct 27;31(42):10390-9. doi: 10.1021/bi00157a029. Biochemistry. 1992. PMID: 1420157
-
NMR studies on fully hydrated membrane proteins, with emphasis on bacteriorhodopsin as a typical and prototype membrane protein.Biochim Biophys Acta. 2007 Dec;1768(12):3145-61. doi: 10.1016/j.bbamem.2007.08.026. Epub 2007 Sep 8. Biochim Biophys Acta. 2007. PMID: 17964534 Review.
-
Conformation and backbone dynamics of bacteriorhodopsin revealed by (13)C-NMR.Biochim Biophys Acta. 2000 Aug 30;1460(1):39-48. doi: 10.1016/s0005-2728(00)00128-6. Biochim Biophys Acta. 2000. PMID: 10984589 Review.
Cited by
-
Role of side-chain conformational entropy in transmembrane helix dimerization of glycophorin A.Biophys J. 2003 Feb;84(2 Pt 1):1263-71. doi: 10.1016/S0006-3495(03)74941-8. Biophys J. 2003. PMID: 12547806 Free PMC article.
-
Backbone dynamics of bacteriorhodopsin as studied by (13)C solid-state NMR spectroscopy.Eur Biophys J. 2003 Sep;32(6):578-84. doi: 10.1007/s00249-003-0305-z. Epub 2003 Jun 26. Eur Biophys J. 2003. PMID: 12830331
-
Studying Dynamics by Magic-Angle Spinning Solid-State NMR Spectroscopy: Principles and Applications to Biomolecules.Prog Nucl Magn Reson Spectrosc. 2016 Aug;96:1-46. doi: 10.1016/j.pnmrs.2016.02.001. Epub 2016 Feb 15. Prog Nucl Magn Reson Spectrosc. 2016. PMID: 27110043 Free PMC article. Review.
-
Organization of model helical peptides in lipid bilayers: insight into the behavior of single-span protein transmembrane domains.Biophys J. 2002 Jul;83(1):345-58. doi: 10.1016/S0006-3495(02)75174-6. Biophys J. 2002. PMID: 12080125 Free PMC article.
-
Helix packing and orientation in the transmembrane dimer of gp55-P of the spleen focus forming virus.Biophys J. 2005 Aug;89(2):1194-202. doi: 10.1529/biophysj.104.057844. Epub 2005 May 13. Biophys J. 2005. PMID: 15894629 Free PMC article.
Publication types
MeSH terms
Substances
LinkOut - more resources
Full Text Sources