- Abstract:
-
Using solid-state NMR approaches, it is now possible to define the structure and dynamics of binding for a small, isotopically (2H, 13C, 19F, 15N) labelled ligand, prosthetic group or solute in its binding site of a membrane-bound protein at near physiological conditions in natural membrane fragments or in reconstituted complexes. Studies of oriented membranes permit the orientational bond vectors of labelled groups to be determined to good precision, as shown for retinal in bacteriorhodopsin...
Expand abstract - Publication status:
- Published
- Publisher copy:
- 10.1007/s002490050187
-
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- Journal:
- EUROPEAN BIOPHYSICS JOURNAL WITH BIOPHYSICS LETTERS
- Volume:
- 28
- Issue:
- 1
- Pages:
- 84-90
- Publication date:
- 1998
- DOI:
- EISSN:
-
1432-1017
- ISSN:
-
0175-7571
- URN:
-
uuid:c083b995-8a9b-4038-83af-38aebfa5f34f
- Source identifiers:
-
410505
- Local pid:
- pubs:410505
- Language:
- English
- Keywords:
- Copyright date:
- 1998
Journal article
Structural descriptions of ligands in their binding site of integral membrane proteins at near physiological conditions using solid-state NMR
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