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Titolo:
Self-association reaction of denatured staphylococcal nuclease fragments characterized by heteronuclear NMR
Autore:
Ye, KQ; Wang, JF;
Indirizzi:
Chinese Acad Sci, Inst Biophys, Natl Lab Biomacromol, Beijing 100101, Peoples R China Chinese Acad Sci Beijing Peoples R China 100101 100101, Peoples R China
Titolo Testata:
JOURNAL OF MOLECULAR BIOLOGY
fascicolo: 1, volume: 307, anno: 2001,
pagine: 309 - 322
SICI:
0022-2836(20010316)307:1<309:SRODSN>2.0.ZU;2-Y
Fonte:
ISI
Lingua:
ENG
Soggetto:
EQUILIBRIUM FOLDING PATHWAY; LONG-RANGE STRUCTURE; BACKBONE DYNAMICS; PARAMAGNETIC RELAXATION; 131-RESIDUE FRAGMENT; PROTEIN; STATE; SPECTROSCOPY; DOMAIN; UREA;
Keywords:
staphylococcal nuclease; protein self-association; backbone dynamics; residual structure; denatured protein;
Tipo documento:
Article
Natura:
Periodico
Settore Disciplinare:
Life Sciences
Citazioni:
46
Recensione:
Indirizzi per estratti:
Indirizzo: Wang, JF Chinese Acad Sci, Inst Biophys, Natl Lab Biomacromol, 15 Datun Rd, Beijing100101, Peoples R China Chinese Acad Sci 15 Datun Rd Beijing Peoples R China 100101 hina
Citazione:
K.Q. Ye e J.F. Wang, "Self-association reaction of denatured staphylococcal nuclease fragments characterized by heteronuclear NMR", J MOL BIOL, 307(1), 2001, pp. 309-322

Abstract

The self-association reaction of denatured staphylococcal nuclease fragments, urea-denatured G88W110, containing residues 1-110 and mutation G88W, and physiologically denatured 131-residue Delta 131 Delta, have been characterized by NMR at close to neutral pH. The two fragments differ in the extentand degree of association due to the different sequence and experimental conditions. Residues 13-39, which show significant exchange line broadening,constitute the main association interface in both fragments. A second weakassociation region was identified involving residues 79-105 only in the case of urea-denatured G88W110. For residues involved in the association reaction, significant suppression of the line broadening and small but systematic chemical shift variation of the amide protons were observed as the protein concentration decreased. The direction of chemical shift change suggeststhat the associated state adopts mainly P-sheet-like conformation, and theP-hairpin formed by strands beta2 and beta3 is native-like. The apparent molecular size obtained by diffusion coefficient measurements shows a weak degree of association for Delta 131 Delta below 0.4 mM protein concentrationand for G88W110 in 4 M urea. In both cases the fragments are predominantlyin the monomeric state. However, the weak association reaction can significantly influence the transverse relaxation of residues involved in the association reaction. The degree of association abruptly increases for Delta 131 Delta above 0.4 mM concentration, and it is estimated to form a 4 to 8 mer at 2 mM. It is proposed that the main region involved in association forms the core structure, with the remainder of residues largely disordered in the associated state. Despite the obvious influence of the association reaction on the slow motion of the backbone, the restricted mobility on the nanosecond timescale around the region of strand beta5 is essentially unaffected by the association reaction and degree of denaturation. (C) 2001 Academic Press.

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Documento generato il 08/07/20 alle ore 08:12:25