IDENTIFICATION OF NATIVE PROTEIN FOLDS AMONGST A LARGE NUMBER OF INCORRECT MODELS - THE CALCULATION OF LOW-ENERGY CONFORMATIONS FROM POTENTIALS OF MEAN FORCE

被引：266

作者：

HENDLICH, M ^{[1
]}

LACKNER, P ^{[1
]}

WEITCKUS, S ^{[1
]}

FLOECKNER, H ^{[1
]}

FROSCHAUER, R ^{[1
]}

GOTTSBACHER, K ^{[1
]}

CASARI, G ^{[1
]}

SIPPL, MJ ^{[1
]}

机构：

[1] SALZBURG UNIV,INST GEN BIOL BIOCHEM & BIOPHYS,DEPT BIOCHEM,HELLBRUNNERSTR 34,A-5020 SALZBURG,AUSTRIA

来源：

JOURNAL OF MOLECULAR BIOLOGY | 1990年 / 216卷 / 01期

关键词：

D O I：

10.1016/S0022-2836(05)80068-3

中图分类号：

Q5 [生物化学]; Q7 [分子生物学];

学科分类号：

071010 ; 081704 ;

摘要：

We present an approach that is able to detect native folds amongst a large number of non-native conformations. The method is based on the compilation of potentials of mean force of the interactions of the Cβ atoms of all amino acid pairs from a database of known three-dimensional protein structures. These potentials are used to calculate the conformational energy of amino acid sequences in a number of different folds. For a substantial number of proteins we find that the conformational energy of the native state is lowest amongst the alternatives. Exceptions are proteins containing large prosthetic groups, Fe-S clusters or polypeptide chains that do not adopt globular folds. We discuss briefly potential applications in various fields of protein structural research. © 1990 Academic Press Limited.

引用

页码：167 / 180

页数：14

共 45 条

[41]

SZEBENYI DME, 1986, J BIOL CHEM, V261, P8761

[42]

TERWILLIGER TC, 1982, J BIOL CHEM, V257, P6010

[43] CRYSTALLOGRAPHIC REFINEMENT OF RUBREDOXIN AT 1.2 A RESOLUTION [J].

WATENPAUGH, KD ;

SIEKER, LC ;

JENSEN, LH .

JOURNAL OF MOLECULAR BIOLOGY, 1980, 138 (03) :615-633

[44] MOLECULAR MODELING OF THE HIV-1 PROTEASE AND ITS SUBSTRATE BINDING-SITE [J].

WEBER, IT ;

MILLER, M ;

JASKOLSKI, M ;

LEIS, J ;

SKALKA, AM ;

WLODAWER, A .

SCIENCE, 1989, 243 (4893) :928-931

[45]

Wuthrich K., 1986, NMR PROTEINS NUCLEIC

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