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Titolo:
FOLDING-UNFOLDING ENERGY CHANGE OF A SIMPLE SPHERE MODEL PROTEIN AND AN ENERGY LANDSCAPE OF THE FOLDING PROCESS
Autore:
FUKUNISHI Y;
Indirizzi:
RIKEN LIFE SCI TSUKUBA CTR,GENOM SCI LAB,3-1-1 KOYADAI TSUKUBA IBARAKI 305 JAPAN RUTGERS STATE UNIV,DEPT CHEM PISCATAWAY NJ 00000
Titolo Testata:
Proteins
fascicolo: 3, volume: 33, anno: 1998,
pagine: 408 - 416
SICI:
0887-3585(1998)33:3<408:FECOAS>2.0.ZU;2-G
Fonte:
ISI
Lingua:
ENG
Soggetto:
TRANSITION-STATE; CYTOCHROME-C; 2-STATE; WATER; THERMODYNAMICS; PARAMETERS; PATHWAYS; FUNNELS; STEP;
Keywords:
PROTEIN FOLDING; POTENTIAL ENERGY CURVE; 2 STATE MODEL; SEMIEMPIRICAL CALCULATION;
Tipo documento:
Article
Natura:
Periodico
Settore Disciplinare:
Science Citation Index Expanded
Science Citation Index Expanded
Citazioni:
35
Recensione:
Indirizzi per estratti:
Citazione:
Y. Fukunishi, "FOLDING-UNFOLDING ENERGY CHANGE OF A SIMPLE SPHERE MODEL PROTEIN AND AN ENERGY LANDSCAPE OF THE FOLDING PROCESS", Proteins, 33(3), 1998, pp. 408-416

Abstract

We have calculated the free energy of a spherical model of a protein or part of a protein generated in the way of protein folding, Two spherical models are examined; one is a homogeneous model consisting of only one residue type-hydrophobic. The other is a heterogeneous model consisting of two residue types-strong hydrophobic and weak hydrophobic. Both models show a folding transition state, and the latter model reproduces the trend of the experimental folded-unfolded energy change. The heterogeneous model suggests that in the folding process of a protein of more than 70 residues, a specific region of the protein folds first to form a stable region, then the other residues follow the folding process. The energy landscape of folding of a small protein is approximately a funnel model, whereas a flatter energy landscape is suggested for larger proteins of more than 55-70 residues. Proteins 33:408-416, 1998. (C) 1998 Wiley-Liss, Inc.

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Documento generato il 19/09/20 alle ore 13:30:13