Downhill protein folding: Evolution meets physics

Martin Gruebele

doi:10.1016/j.crvi.2005.02.007

Downhill protein folding: Evolution meets physics

Research output: Contribution to journal › Short survey › peer-review

Abstract

Proteins can be redesigned to fold downhill on a free energy surface characterized by only a few coordinates, confirming a principal prediction of the 'energy-landscape' model. Nonetheless, natural proteins have small but significant barriers. Spectroscopy and kinetics reveal potential biological causes for activation barriers during protein folding: evolution against protein aggregation and for protein function.

Original language	English (US)
Pages (from-to)	701-712
Number of pages	12
Journal	Comptes Rendus - Biologies
Volume	328
Issue number	8
DOIs	https://doi.org/10.1016/j.crvi.2005.02.007
State	Published - Aug 2005

Keywords

Activation barrier
Hydrophobicity
Protein function
Temperature jump

ASJC Scopus subject areas

General Medicine

Online availability

10.1016/j.crvi.2005.02.007

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title = "Downhill protein folding: Evolution meets physics",

abstract = "Proteins can be redesigned to fold downhill on a free energy surface characterized by only a few coordinates, confirming a principal prediction of the 'energy-landscape' model. Nonetheless, natural proteins have small but significant barriers. Spectroscopy and kinetics reveal potential biological causes for activation barriers during protein folding: evolution against protein aggregation and for protein function.",

keywords = "Activation barrier, Hydrophobicity, Protein function, Temperature jump",

author = "Martin Gruebele",

note = "Funding Information: This work was supported by National Science Foundation grant MCB 0316925. ",

year = "2005",

month = aug,

doi = "10.1016/j.crvi.2005.02.007",

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AU - Gruebele, Martin

N1 - Funding Information: This work was supported by National Science Foundation grant MCB 0316925.

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N2 - Proteins can be redesigned to fold downhill on a free energy surface characterized by only a few coordinates, confirming a principal prediction of the 'energy-landscape' model. Nonetheless, natural proteins have small but significant barriers. Spectroscopy and kinetics reveal potential biological causes for activation barriers during protein folding: evolution against protein aggregation and for protein function.

AB - Proteins can be redesigned to fold downhill on a free energy surface characterized by only a few coordinates, confirming a principal prediction of the 'energy-landscape' model. Nonetheless, natural proteins have small but significant barriers. Spectroscopy and kinetics reveal potential biological causes for activation barriers during protein folding: evolution against protein aggregation and for protein function.

KW - Activation barrier

KW - Hydrophobicity

KW - Protein function

KW - Temperature jump

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Downhill protein folding: Evolution meets physics

Abstract

Keywords

ASJC Scopus subject areas

Online availability

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