De novo proteins from combinatorial libraries

David A. Moffet; Michael H. Hecht

doi:10.1021/cr000051e

De novo proteins from combinatorial libraries

David A. Moffet, Michael H. Hecht

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

94 Scopus citations

Abstract

The technique used for analyzing De Novo proteins from combinatorial libraries were discussed. The sequences targeted to form a tetrameric α-helical bundle was solved and compared with respect to the calculated structures. The results showed that the binary code strategy for protein design produced a large collection of de Novo sequences that folded into soluble α-helical structures.

Original language	English (US)
Pages (from-to)	3191-3203
Number of pages	13
Journal	Chemical Reviews
Volume	101
Issue number	10
DOIs	https://doi.org/10.1021/cr000051e
State	Published - Oct 2001

All Science Journal Classification (ASJC) codes

General Chemistry

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10.1021/cr000051e

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title = "De novo proteins from combinatorial libraries",

abstract = "The technique used for analyzing De Novo proteins from combinatorial libraries were discussed. The sequences targeted to form a tetrameric α-helical bundle was solved and compared with respect to the calculated structures. The results showed that the binary code strategy for protein design produced a large collection of de Novo sequences that folded into soluble α-helical structures.",

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year = "2001",

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AB - The technique used for analyzing De Novo proteins from combinatorial libraries were discussed. The sequences targeted to form a tetrameric α-helical bundle was solved and compared with respect to the calculated structures. The results showed that the binary code strategy for protein design produced a large collection of de Novo sequences that folded into soluble α-helical structures.

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JO - Chemical Reviews

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De novo proteins from combinatorial libraries

Abstract

All Science Journal Classification (ASJC) codes

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