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Structural descriptions of ligands in their binding site of integral membrane proteins at near physiological conditions using solid-state NMR

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...

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Publication status:
Published

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Publisher copy:
10.1007/s002490050187

Authors


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Institution:
University of Oxford
Department:
Oxford, MSD, Biochemistry
Burnett, IJ More by this author
Glaubitz, C More by this author
Grobner, G More by this author
Middleton, DA More by this author
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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

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