De novo protein design: what are we learning?

William F. DeGrado; Daniel P. Raleigh; Tracey Handel

doi:10.1016/0959-440X(91)90095-B

De novo protein design: what are we learning?

William F. DeGrado
, Daniel P. Raleigh
, Tracey Handel

Chemistry

Stony Brook University

DuPont

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

68 Scopus citations

Abstract

The field of de novo design is examined in the light of current theories of protein folding. The most carefully characterized designed proteins show many of the characteristics of molten globules or protein folding intermediates. Thus, it is unclear whether or not the objective of designing proteins that fully mimic the native states of natural proteins has been achieved.

Original language	English
Pages (from-to)	984-993
Number of pages	10
Journal	Current Opinion in Structural Biology
Volume	1
Issue number	6
DOIs	https://doi.org/10.1016/0959-440X(91)90095-B
State	Published - Dec 1991

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10.1016/0959-440X(91)90095-B

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title = "De novo protein design: what are we learning?",

abstract = "The field of de novo design is examined in the light of current theories of protein folding. The most carefully characterized designed proteins show many of the characteristics of molten globules or protein folding intermediates. Thus, it is unclear whether or not the objective of designing proteins that fully mimic the native states of natural proteins has been achieved.",

author = "DeGrado, \{William F.\} and Raleigh, \{Daniel P.\} and Tracey Handel",

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AU - DeGrado, William F.

AU - Raleigh, Daniel P.

AU - Handel, Tracey

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Y1 - 1991/12

N2 - The field of de novo design is examined in the light of current theories of protein folding. The most carefully characterized designed proteins show many of the characteristics of molten globules or protein folding intermediates. Thus, it is unclear whether or not the objective of designing proteins that fully mimic the native states of natural proteins has been achieved.

AB - The field of de novo design is examined in the light of current theories of protein folding. The most carefully characterized designed proteins show many of the characteristics of molten globules or protein folding intermediates. Thus, it is unclear whether or not the objective of designing proteins that fully mimic the native states of natural proteins has been achieved.

UR - https://www.scopus.com/pages/publications/0000593794

U2 - 10.1016/0959-440X(91)90095-B

DO - 10.1016/0959-440X(91)90095-B

M3 - Article

SN - 0959-440X

VL - 1

SP - 984

EP - 993

JO - Current Opinion in Structural Biology

JF - Current Opinion in Structural Biology

IS - 6

ER -

De novo protein design: what are we learning?

Abstract

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