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Titolo:
ARE PROTEIN FOLDS ATYPICAL
Autore:
LI H; TANG C; WINGREEN NS;
Indirizzi:
NEC RES INST,4 INDEPENDENCE WAY PRINCETON NJ 08540 NEC RES INST PRINCETON NJ 08540
Titolo Testata:
Proceedings of the National Academy of Sciences of the United Statesof America
fascicolo: 9, volume: 95, anno: 1998,
pagine: 4987 - 4990
SICI:
0027-8424(1998)95:9<4987:>2.0.ZU;2-E
Fonte:
ISI
Lingua:
ENG
Soggetto:
GLOBULAR-PROTEINS; SURFACE-AREA; MONTE-CARLO; PATTERNS; PACKING; CLASSIFICATION; SOLUBILITY; SIMULATION; POTENTIALS; SHEETS;
Tipo documento:
Article
Natura:
Periodico
Settore Disciplinare:
Science Citation Index Expanded
Citazioni:
29
Recensione:
Indirizzi per estratti:
Citazione:
H. Li et al., "ARE PROTEIN FOLDS ATYPICAL", Proceedings of the National Academy of Sciences of the United Statesof America, 95(9), 1998, pp. 4987-4990

Abstract

Protein structures are a very special class among all possible structures. It has been suggested that a ''designability principle'' plays acrucial role in nature's selection of protein sequences and structures. Here, we provide a theoretical base for such a selection principle,using a simple model of protein folding based on hydrophobic interactions. A structure is reduced to a string of 0s and 1s, which representthe surface and core sites, respectively, as the backbone is traced. Each structure is therefore associated with one point in a high dimensional space. Sequences are represented by strings of their hydrophobicities and thus can be mapped into the same space. A sequence that liescloser to a particular structure in this space than to any other structures will have that structure as its ground state. Atypical structures, namely those far away from other structures in the high dimensional space, have more sequences that fold into them and are thermodynamically more stable. We argue that the most common folds of proteins are the most atypical in the space of possible structures.

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Documento generato il 10/04/20 alle ore 02:22:48