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Titolo:
C-13 cross-polarization/magic angle spinning NMR studies of alpha-elastin preparations show retention of overall structure and reduction of mobility with a decreased number of cross-links
Autore:
Kumashiro, KK; Kim, MS; Kaczmarek, SE; Sandberg, LB; Boyd, CD;
Indirizzi:
Univ Hawaii Manoa, Dept Chem, Honolulu, HI 96822 USA Univ Hawaii Manoa Honolulu HI USA 96822 Dept Chem, Honolulu, HI 96822 USA Loma Linda Univ, Jerry L Pettis Mem Vet Hosp, Connect Tissue Lab, Loma Linda, CA 92357 USA Loma Linda Univ Loma Linda CA USA 92357 sue Lab, Loma Linda, CA 92357 USA Univ Hawaii Manoa, Pacific Biomed Res Ctr, Honolulu, HI 96822 USA Univ Hawaii Manoa Honolulu HI USA 96822 d Res Ctr, Honolulu, HI 96822 USA
Titolo Testata:
BIOPOLYMERS
fascicolo: 4, volume: 59, anno: 2001,
pagine: 266 - 275
SICI:
0006-3525(20011005)59:4<266:CCASNS>2.0.ZU;2-V
Fonte:
ISI
Lingua:
ENG
Soggetto:
NUCLEAR-MAGNETIC-RESONANCE; SOLID-STATE; SECONDARY STRUCTURE; CONFORMATIONAL CHARACTERIZATION; MOLECULAR-MODEL; CHEMICAL-SHIFTS; SPECTROSCOPY; POLYPEPTIDES; OLIGO(L-ALANINE); POLY(L-ALANINE);
Keywords:
high-resolution solid-state C-13 NMR; alpha-elastin; aorta; copper deficiency; cross-linked peptides; undercross-linked peptides;
Tipo documento:
Article
Natura:
Periodico
Settore Disciplinare:
Life Sciences
Citazioni:
38
Recensione:
Indirizzi per estratti:
Indirizzo: Kumashiro, KK Univ Hawaii Manoa, Dept Chem, Honolulu, HI 96822 USA Univ Hawaii Manoa Honolulu HI USA 96822 olulu, HI 96822 USA
Citazione:
K.K. Kumashiro et al., "C-13 cross-polarization/magic angle spinning NMR studies of alpha-elastin preparations show retention of overall structure and reduction of mobility with a decreased number of cross-links", BIOPOLYMERS, 59(4), 2001, pp. 266-275

Abstract

High-resolution solid-state C-13 NMR spectra are presented for samples of a-elastin prepared from the aorta of normal and copper-deficient pigs. Chemical shifts of the various peaks indicate that both the normal and undercross-linked peptides have similar overall structures. However, C-13 T-1, C-13T-1p, and H-1 T-1p measurements indicate that the alpha -elastin peptides obtained from the abnormal elastic fibers samples exhibit altered mobilities, particularly in their side chains. Results from spectra taken with a range of contact times and from dipolar dephasing experiments are consistent with conclusions reached with the relaxation measurements. Namely, the loss of junction associated with the undercross-linked sample is correlated to asmall but measurable difference in relative mobility. (C) 2001 John Wiley & Sons, Inc.

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Documento generato il 01/10/20 alle ore 06:38:13