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Weak substrate binding to transport proteins studied by NMR.

Abstract:

The weak binding of sugar substrates fails to induce any quantifiable physical changes in the L-fucose-H+ symport protein, FucP, from Escherichia coli, and this protein lacks any strongly binding ligands for competitive binding assays. Access to substrate binding behavior is however possible using NMR methods which rely on substrate immobiliza-tion for detection. Cross-polarization from proton to carbon spins could detect the portion of 13C-labeled substrate associated with 0.2 micromol of th...

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Publication status:
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Authors


Spooner, PJ More by this author
O'Reilly, WJ More by this author
Homans, SW More by this author
Rutherford, NG More by this author
Henderson, PJ More by this author
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Journal:
Biophysical journal
Volume:
75
Issue:
6
Pages:
2794-2800
Publication date:
1998-12-05
DOI:
EISSN:
1542-0086
ISSN:
0006-3495
URN:
uuid:172676df-e815-473e-acc9-2ba1415bd02f
Source identifiers:
410484
Local pid:
pubs:410484

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