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Titolo:
Interactions between subdomains in the partially folded state of staphylococcal nuclease
Autore:
Ye, KQ; Jing, GZ; 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:
BIOCHIMICA ET BIOPHYSICA ACTA-PROTEIN STRUCTURE AND MOLECULAR ENZYMOLOGY
fascicolo: 1-2, volume: 1479, anno: 2000,
pagine: 123 - 134
SICI:
0167-4838(20000615)1479:1-2<123:IBSITP>2.0.ZU;2-B
Fonte:
ISI
Lingua:
ENG
Soggetto:
N-TERMINAL FRAGMENTS; FOLDING INTERMEDIATE; DENATURED STATE; RESIDUAL STRUCTURE; NMR-SPECTROSCOPY; PROTEIN; STABILITY; MUTANTS; COMPACT; CHAIN;
Keywords:
staphylococcal nuclease; fragment; tryptophan mutation; protein stability; intermediate state; subdomain;
Tipo documento:
Article
Natura:
Periodico
Settore Disciplinare:
Life Sciences
Citazioni:
36
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 et al., "Interactions between subdomains in the partially folded state of staphylococcal nuclease", BBA-PROT ST, 1479(1-2), 2000, pp. 123-134

Abstract

Staphylococcal nuclease can be roughly divided into a beta-subdomain in N-terminal and an alpha-subdomain in C-terminal. They fold sequentially undercertain conditions, causing a partially folded intermediate state in whichthe native-like beta-barrel persists while alpha-helix regions largely disorder. To investigate the possible long-range interactions between the two subdomains in the intermediate, N-terminal fragments have been used as intermediate analogues, with polypeptide ending at positions 102, 110, 121 and 135 and with a tryptophan substitution at position 66 or 88 to facilitate the observation of the beta-barrel. Segment-resolved interactions between beta-barrel and residues 103-135 were identified by comparing their spectroscopic properties of fluorescence, circular dichroism and NMR and by their stability. Except for unstable V66W102, the guanidine and thermal denaturation of fragments are cooperative and well approximated by the two-state transition. Minimal stable structure units of both tryptophan-containing fragments comprise residues 1-110. With the main interaction in segment 103-135, residues 103-110 contribute approximate 2 kcal/mol to the stability. Elongation of C-terminal from 110 residue neither increases the stability nor alters the structure core of the G88W fragments. However, residues 111-121 influence the tertiary structure of the V66W fragments suggesting its minor interactions with beta-barrel. (C) 2000 Elsevier Science B.V. All rights reserved.

ASDD Area Sistemi Dipartimentali e Documentali, Università di Bologna, Catalogo delle riviste ed altri periodici
Documento generato il 12/07/20 alle ore 02:43:48