Catalogo Articoli (Spogli Riviste)

OPAC HELP

Titolo:
Selection of side-chain carbons in a high-molecular-weight, hydrophobic peptide using solid-state spectral editing methods
Autore:
Kumashiro, KK; Niemczura, WP; Kim, MS; Sandberg, LB;
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
Titolo Testata:
JOURNAL OF BIOMOLECULAR NMR
fascicolo: 2, volume: 18, anno: 2000,
pagine: 139 - 144
SICI:
0925-2738(200010)18:2<139:SOSCIA>2.0.ZU;2-3
Fonte:
ISI
Lingua:
ENG
Soggetto:
CPMAS NMR;
Keywords:
CPMAS; elastin; solid-state NMR; spectral editing;
Tipo documento:
Article
Natura:
Periodico
Settore Disciplinare:
Life Sciences
Citazioni:
13
Recensione:
Indirizzi per estratti:
Indirizzo: Kumashiro, KK Univ Hawaii Manoa, Dept Chem, 2545 Mall, Honolulu, HI 96822 USA Univ Hawaii Manoa 2545 Mall Honolulu HI USA 96822 96822 USA
Citazione:
K.K. Kumashiro et al., "Selection of side-chain carbons in a high-molecular-weight, hydrophobic peptide using solid-state spectral editing methods", J BIOM NMR, 18(2), 2000, pp. 139-144

Abstract

Solid-state spectral editing techniques have been used by others to simplify C-13 CPMAS spectra of small organic molecules, synthetic organic polymers, and coals. One approach utilizes experiments such as cross-polarization-with-polarization-inversion and cross-polarization-with-depolarization to generate subspectra. This work shows that this particular methodology is also applicable to natural-abundance C-13 CPMAS NMR studies of high-molecular-weight biopolymers. The editing experiments are demonstrated first with model peptides and then with alpha -elastin, a high-molecular-weight peptidylpreparation obtained from the elastic fibers in mammalian tissue. The latter has a predominance of small, nonpolar residues, which is evident in the crowded aliphatic region of typical C-13 CPMAS spectra. Spectral editing isparticularly useful for simplifying the aliphatic region of the NMR spectrum of this elastin preparation.

ASDD Area Sistemi Dipartimentali e Documentali, Università di Bologna, Catalogo delle riviste ed altri periodici
Documento generato il 18/09/20 alle ore 10:08:15