Folding and aggregation of designed proteins

被引：74

作者：

Broglia, RA ^{[1
]}

Tiana, G

Pasquali, S

Roman, HE

Vigezzi, E

机构：

[1] Univ Milan, Dipartimento Fis, I-20133 Milan, Italy

[2] Ist Nazl Fis Nucl, I-20133 Milan, Italy

[3] Univ Copenhagen, Niels Bohr Inst, DK-2100 Copenhagen, Denmark

[4] Tech Univ Denmark, Dept Phys, DK-2800 Lyngby, Denmark

来源：

PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA | 1998年 / 95卷 / 22期

关键词：

D O I：

10.1073/pnas.95.22.12930

中图分类号：

O [数理科学和化学]; P [天文学、地球科学]; Q [生物科学]; N [自然科学总论];

学科分类号：

07 ; 0710 ; 09 ;

摘要：

Protein aggregation is studied by following the simultaneous folding of two designed identical 20-letter amino acid chains within the framework of a lattice model and using Monte Carlo simulations. It is found that protein aggregation is determined by elementary structures (partially folded intermediates) controlled by local contacts among some of the most strongly interacting amino acids and formed at an early stage in the folding process.

引用

页码：12930 / 12933

页数：4

共 31 条

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