ISSN:
0006-3525
Keywords:
β-thymosins
;
actin-binding peptide
;
conformation
;
nmr
;
Chemistry
;
Polymer and Materials Science
Source:
Wiley InterScience Backfile Collection 1832-2000
Topics:
Chemistry and Pharmacology
Notes:
The conformation of thymosin β9 in solution of 40% (v/v) 1,1,1,3,3,3-hexafluoro-2-propanol-d2 in water has been investigated by two-dimensional 1H-nmr spectroscopy. Under this condition thymosin β9 adopts an ordered structure. The determination of the conformation of the peptide was based on a set of 304 approximate interproton distance constraints derived from nuclear Overhauser enhancement measurements. The conformation of thymosin β9 includes two helical regions from residues 4 to 27 and 32 to 41. The two helices are separated by a poorly defined loop region between amino acids 28 and 31; the N-terminus of thymosin B9 shows random-coil structure only. © 1997 John Wiley & Sons, Inc. Biopoly 41: 623-634, 1997
Additional Material:
6 Ill.
Type of Medium:
Electronic Resource
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