The designability hypothesis and protein evolution

Edo Kussell

doi:10.2174/0929866053005881

The designability hypothesis and protein evolution

Edo Kussell

Biology and Genomics

Research output: Contribution to journal › Review article › peer-review

Abstract

The usage of protein folds in nature is known to be non-uniform: a few folds are used often, while most others are used relatively rarely. What makes one fold more successful than another? The designability explanation, which posits that successful folds have an exponentially larger number of compatible sequences, is critically reviewed, and compared with other structural and functional explanations. It is argued that designability is one component of fold fitness, but most likely not a dominant one.

Original language	English (US)
Pages (from-to)	111-116
Number of pages	6
Journal	Protein and Peptide Letters
Volume	12
Issue number	2
DOIs	https://doi.org/10.2174/0929866053005881
State	Published - Feb 2005

Keywords

Designability
In vitro evolution
Protein design
Protein evolution
Protein folding

ASJC Scopus subject areas

Structural Biology
Biochemistry

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10.2174/0929866053005881

Cite this

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KW - Protein evolution

KW - Protein folding

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The designability hypothesis and protein evolution

Abstract

Keywords

ASJC Scopus subject areas

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