Abstract:
:The solvent-exposed regions of (U-13C)ascomycin when bound to its putative target protein, FKBP, have been identified based on the different proton longitudinal relaxation rates (R1 = 1/T1) measured in the absence and presence of the paramagnetic relaxation reagent, 4-hydroxy-2,2,6,6-tetramethyl-piperidinyl-1-oxy (HyTEMPO). The proton T1S of bound ascomycin were determined using a pulse sequence (T1-HMQC) which consists of a 180 degree proton pulse and a variable delay (tau) followed by a heteronuclear multiple quantum correlation (HMQC) experiment. The solvent-exposed regions of ascomycin determined by these experiments are compared to NOE data in which ascomycin/FKBP contacts were identified and to the X-ray structure of the FK-506/FKBP complex.
journal_name
J Biomol NMRjournal_title
Journal of biomolecular NMRauthors
Petros AM,Neri P,Fesik SWdoi
10.1007/BF02192797subject
Has Abstractpub_date
1992-01-01 00:00:00pages
11-8issue
1eissn
0925-2738issn
1573-5001journal_volume
2pub_type
杂志文章abstract::A new method, a restrained Monte Carlo (rMC) calculation, is demonstrated for generating high-resolution structures of DNA oligonucleotides in solution from interproton distance restraints and bounds derived from complete relaxation matrix analysis of two-dimensional nuclear Overhauser effect (NOE) spectral peak inten...
journal_title:Journal of biomolecular NMR
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journal_title:Journal of biomolecular NMR
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journal_title:Journal of biomolecular NMR
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pub_type: 杂志文章
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journal_title:Journal of biomolecular NMR
pub_type: 杂志文章
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