Coupling the Folding of Homologous Proteins

Chen Keasar; Dror Tobi; Ron Elber; Jeff Skolnick

Coupling the Folding of Homologous Proteins

Chen Keasar, Dror Tobi, Ron Elber, Jeff Skolnick

Research output: Contribution to journal › Article › peer-review

9 Scopus citations

Abstract

The empirical observation that homologous proteins fold to similar structures is used to enhance the capabilities of an ab initio algorithm to predict protein conformations. A penalty function that forces homologous proteins to look alike is added to the potential and is employed in the coupled energy optimization of several homologous proteins. Significant improvement in the quality of the computed structures (as compared with the computational folding of a single protein) is demonstrated and discussed.

Original language	English
Pages (from-to)	5880-5833
Number of pages	4
Journal	Proceedings of the National Academy of Sciences of the United States of America
Volume	95
Issue number	11
State	Published - 26 May 1998
Externally published	Yes

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title = "Coupling the Folding of Homologous Proteins",

abstract = "The empirical observation that homologous proteins fold to similar structures is used to enhance the capabilities of an ab initio algorithm to predict protein conformations. A penalty function that forces homologous proteins to look alike is added to the potential and is employed in the coupled energy optimization of several homologous proteins. Significant improvement in the quality of the computed structures (as compared with the computational folding of a single protein) is demonstrated and discussed.",

author = "Chen Keasar and Dror Tobi and Ron Elber and Jeff Skolnick",

year = "1998",

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day = "26",

language = "English",

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pages = "5880--5833",

journal = "Proceedings of the National Academy of Sciences of the United States of America",

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TY - JOUR

T1 - Coupling the Folding of Homologous Proteins

AU - Keasar, Chen

AU - Tobi, Dror

AU - Elber, Ron

AU - Skolnick, Jeff

PY - 1998/5/26

Y1 - 1998/5/26

N2 - The empirical observation that homologous proteins fold to similar structures is used to enhance the capabilities of an ab initio algorithm to predict protein conformations. A penalty function that forces homologous proteins to look alike is added to the potential and is employed in the coupled energy optimization of several homologous proteins. Significant improvement in the quality of the computed structures (as compared with the computational folding of a single protein) is demonstrated and discussed.

AB - The empirical observation that homologous proteins fold to similar structures is used to enhance the capabilities of an ab initio algorithm to predict protein conformations. A penalty function that forces homologous proteins to look alike is added to the potential and is employed in the coupled energy optimization of several homologous proteins. Significant improvement in the quality of the computed structures (as compared with the computational folding of a single protein) is demonstrated and discussed.

UR - http://www.scopus.com/inward/record.url?scp=11544374453&partnerID=8YFLogxK

M3 - Article

C2 - 9600887

AN - SCOPUS:0032568501

SN - 0027-8424

VL - 95

SP - 5880

EP - 5833

JO - Proceedings of the National Academy of Sciences of the United States of America

JF - Proceedings of the National Academy of Sciences of the United States of America

IS - 11

ER -

Coupling the Folding of Homologous Proteins

Abstract

ASJC Scopus subject areas

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