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Titolo:
Conformation transition kinetics of regenerated Bombyx mori silk fibroin membrane monitored by time-resolved FTIR spectroscopy
Autore:
Chen, X; Shao, ZZ; Marinkovic, NS; Miller, LM; Zhou, P; Chance, MR;
Indirizzi:
Yeshiva Univ Albert Einstein Coll Med, Ctr Synchrotron Biosci, Bronx, NY 10461 USA Yeshiva Univ Albert Einstein Coll Med Bronx NY USA 10461 nx, NY 10461 USA Fudan Univ, Key Lab Mol Engn Polymers, Dept Macromol Sci, Shanghai 200433,Peoples R China Fudan Univ Shanghai Peoples R China 200433 anghai 200433,Peoples R China Yeshiva Univ Albert Einstein Coll Med, Dept Physiol & Biophys, Bronx, NY 10461 USA Yeshiva Univ Albert Einstein Coll Med Bronx NY USA 10461 nx, NY 10461 USA Brookhaven Natl Lab, Natl Synchrotron Light Source, Upton, NY 11973 USA Brookhaven Natl Lab Upton NY USA 11973 Light Source, Upton, NY 11973 USA
Titolo Testata:
BIOPHYSICAL CHEMISTRY
fascicolo: 1, volume: 89, anno: 2001,
pagine: 25 - 34
SICI:
0301-4622(20010131)89:1<25:CTKORB>2.0.ZU;2-7
Fonte:
ISI
Lingua:
ENG
Soggetto:
TRANSFORM INFRARED-SPECTROSCOPY; PHYSICAL-PROPERTIES; SOLID-STATE; RIBONUCLEASE-A; I STRUCTURE; FAST EVENTS; WATER; NMR; TEMPERATURE; DIFFRACTION;
Keywords:
time-resolved FTIR spectroscopy; protein conformation transition; Bombyx mori silk fibroin; beta-sheet conformation;
Tipo documento:
Article
Natura:
Periodico
Settore Disciplinare:
Life Sciences
Physical, Chemical & Earth Sciences
Citazioni:
43
Recensione:
Indirizzi per estratti:
Indirizzo: Chance, MR Yeshiva Univ Albert Einstein Coll Med, Ctr Synchrotron Biosci, 1300 MorrisPk Ave, Bronx, NY 10461 USA Yeshiva Univ Albert Einstein Coll Med 1300 Morris Pk Ave Bronx NY USA 10461
Citazione:
X. Chen et al., "Conformation transition kinetics of regenerated Bombyx mori silk fibroin membrane monitored by time-resolved FTIR spectroscopy", BIOPHYS CH, 89(1), 2001, pp. 25-34

Abstract

The ethanol-induced conformation transition of regenerated Bombyx mori silk fibroin membrane from a poorly defined to the well ordered state was monitored by time-resolved Fourier transform infrared spectroscopy (FTIR) for the first time. From the analysis of FTIR difference spectra, taken on time scales as short as 6 s and up to 1 h after addition of ethanol. intensity vs. time plots of an increasing band at 1618 cm(-1) were observed indicatingformation of a beta -sheet coincident with the loss of intensity of a bandat 1668 cm(-1) indicating decreases of random coil and/or silk I structure. Both infrared markers were fitted with identical biphasic exponential decay functions, however, there was a clear burst phase occurring prior to theonset of the observed transitions. The conformation transition process is indicated to either proceed sequentially through (at least) two intermediate states that contain different levels of beta -sheet structure or to have parallel pathways of initial beta -sheet formation followed by a slower 'perfection' phase. The first observed process forms in a burst phase a few seconds after mixing (or even faster), prior to the collection of the first spectrum at 6 s. The second observed process occurs with a time constant of similar to 0.5 min, the intermediate present at this stage then continues with a time constant of 5.5 min completing the observed formation of the beta -sheet. The conformation transition of this slower intermediate is not only indicated by an analysis of the kinetics of the random coil and beta -sheet-specific bands discussed above. it roughly coincides with the appearance of an additional infrared marker at 1695 cm(-1), which may be a marker for p-sheet structure specific to the formation of the perfected structure. The conformation transition of this protein analyzed by infrared spectroscopy provides insight into a part of the fascinating process of cocoon formation in B. mori. (C) 2001 Elsevier Science B.V. All rights reserved.

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Documento generato il 15/07/20 alle ore 07:39:49