The Protein Folding Transition State: What Are φ-Values Really Telling Us?

Daniel   P.   Raleigh; Kevin   W.   Plaxco

Abstract

Protein engineering-based studies of the folding transition state have accelerated significantly in the last decade, and more than a half dozen proteins have been subjected to extensive φ-value analysis. A general picture is emerging from these studies of a transition state in which the large majority of experimentally characterized side chains participate in relatively homogeneous and energetically weak interactions playing only a relatively small role in defining relative folding rates.

Keywords: Protein Folding Transition, homogeneous

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Protein & Peptide Letters

Title: The Protein Folding Transition State: What Are φ-Values Really Telling Us?

Volume: 12 Issue: 2

Author(s): Daniel P. Raleigh and Kevin W. Plaxco

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Keywords: Protein Folding Transition, homogeneous

Abstract: Protein engineering-based studies of the folding transition state have accelerated significantly in the last decade, and more than a half dozen proteins have been subjected to extensive φ-value analysis. A general picture is emerging from these studies of a transition state in which the large majority of experimentally characterized side chains participate in relatively homogeneous and energetically weak interactions playing only a relatively small role in defining relative folding rates.

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Raleigh P. Daniel and Plaxco W. Kevin, The Protein Folding Transition State: What Are φ-Values Really Telling Us?, Protein & Peptide Letters 2005; 12 (2) . https://dx.doi.org/10.2174/0929866053005809