Linguistic analysis of protein folding

FEBS Letters

Groß, Michael¹ 

[1] Oxford Centre for Molecular Sciences, New Chemistry Laboratory, Oxford OX1 3QT, UK

关键词: β-Sheet;    Folding problem;    Nascent chain;    Tendamistat;    Topology;    3D;    three-dimensional;    CI-2;    chymotrypsin inhibitor 2;    CspB;    cold shock protein B from Bacillus subtilis;    IgG CH;    constant heavy domain of immunoglobulin G;    IgG VH;    variable heavy domain of immunoglobulin G;    n;    any number 1…6 (refers to position of β-strand in sequence);    TBSV;    tomato bushy stunt virus;    TNF α;    alpha domain of tumour necrosis factor;    X;    any letter A…F (refers to position of β-strand in space);   

DOI  :  10.1016/0014-5793(96)00727-2

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 摘 要 】

Folding of nascent chains resembles the decoding of spoken language in that information is emitted as a unidirectional, one-dimensional string of elements, with higher structures and long-distance interactions emerging with time. Applying a ‘pseudolinguistic’ analysis of structure to a set of all 36 possible six-stranded antiparallel β-sandwich topologies reveals new order principles and reduces the complexity of this family significantly. The simple connectivity diagrams (‘linguistic trees’) proposed here allow predictions of the speed and cooperativity of β-sheet folding and help understanding the cotranslational folding from the N-terminus.

【 授权许可】

Unknown