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Titolo:
Genetically directed synthesis and spectroscopic analysis of a protein polymer derived from a flagelliform silk sequence
Autore:
Zhou, YT; Wu, SX; Conticello, VP;
Indirizzi:
Emory Univ, Dept Chem, Atlanta, GA 30322 USA Emory Univ Atlanta GA USA 30322 ry Univ, Dept Chem, Atlanta, GA 30322 USA
Titolo Testata:
BIOMACROMOLECULES
fascicolo: 1, volume: 2, anno: 2001,
pagine: 111 - 125
SICI:
1525-7797(200121)2:1<111:GDSASA>2.0.ZU;2-J
Fonte:
ISI
Lingua:
ENG
Soggetto:
CLAVIPES DRAGLINE SILK; CENTRAL REPETITIVE DOMAIN; WEIGHT GLUTEN PROTEINS; MAJOR AMPULLATE SILK; II BETA-TURNS; SPIDER SILK; CONFORMATIONAL-ANALYSIS; MOLECULAR-DYNAMICS; CIRCULAR-DICHROISM; C-13 NMR;
Tipo documento:
Article
Natura:
Periodico
Settore Disciplinare:
Life Sciences
Physical, Chemical & Earth Sciences
Citazioni:
70
Recensione:
Indirizzi per estratti:
Indirizzo: Conticello, VP Emory Univ, Dept Chem, 1515 Pierce Dr, Atlanta, GA 30322 USA Emory Univ 1515 Pierce Dr Atlanta GA USA 30322 GA 30322 USA
Citazione:
Y.T. Zhou et al., "Genetically directed synthesis and spectroscopic analysis of a protein polymer derived from a flagelliform silk sequence", BIOMACROMOL, 2(1), 2001, pp. 111-125

Abstract

The flagelliform silk protein underlies the unique elastomeric properties displayed by the capture spiral of arachnid webs. To investigate molecular mechanism underlying the elastomeric recovery of the capture spiral, a model polypeptide based upon the elastomeric repeat sequence of Nephila clavipes flagelliform silk protein has been synthesized using recombinant DNA techniques. Polypeptide 1 contains 11 repeats of the 25 amino acid sequence [(Gly-Pro-Gly-Gly-Ser-Gly-Pro-Gly-Gly-Tyr)(2)-Gly-Pro-Gly-Gly-Lys] and was expressed in Escherichia coil strain BL21(DE3) as a C-terminal fusion to a decahistidine leader sequence. A combination of H-1-H-1 COSY, DEPT,H-1-C-13 HETCOR, and H-1-C-13 HMBC NMR spectroscopy was employed on polypeptides 1 andthe [1-C-13]glycine-labeled analogue 1G to assign the H-1 and C-13 NMR resonances of the amino acid residues comprising the flagelliform silk repeat sequence. The conformational properties of 1 in aqueous solution were investigated using a combination of CD, FTIR, VT-NMR, and two-dimensional NOESY NMR. These techniques were consistent with the presence of small but detectable population of beta -turn conformers between Gly(1) and Gly(4) of the pentapeptide units of 1. FTIR and CD studies of solid films of 1 indicated an increase in beta -turn population in the solid state, which coincided with the decrease in hydration level of the polypeptide. The spectroscopic information suggests that the pentapeptide segments of the flagelliform silk protein adopt a beta -turn conformation in the fiber and that the mechanism of elasticity may resemble that proposed for other beta -turn forming polypeptides including elastin.

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Documento generato il 06/04/20 alle ore 12:07:27