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Amino-acid substitutions in a surface turn modulate protein stability

Nature Structural Biology volume 3, pages 54–58 (1996)Cite this article

A Corrigendum to this article was published on 01 December 1996

Abstract

A surface turn position in a four-helix bundle protein, Rop, was selected to investigate the role of turns in protein structure and stability. Although all twenty amino acids can be substituted at this position to generate a correctly folded protein, they produce an unusually large range of thermodynamic stabilities. Moreover, the majority of substitutions give rise to proteins with enhanced thermal stability compared to that of the wild type. By introducing the same twenty mutations at this position, but in a simplified context, we were able to deconvolute intrinsic preferences from local environmental effects. The intrinsic preferences can be explained on the basis of preferred backbone dihedral angles, but local environmental context can significantly modify these effects.

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Author notes

  1. Paul F. Predki

    Present address: CuraGen Corporation Branford, Connecticut, 06405, USA

Authors and Affiliations

  1. Howard Hughes Medical Institute Yale University, New Haven, Connecticut, 06520, USA

    Vishal Agrawal & Axel T. Brünger

  2. Department of Molecular Biophysics and Biochemistry Yale University, New Haven, Connecticut, 06520, USA

    Lynne Regan

Authors
  1. Paul F. Predki
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  2. Vishal Agrawal
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  3. Axel T. Brünger
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  4. Lynne Regan
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Predki, P., Agrawal, V., Brünger, A. et al. Amino-acid substitutions in a surface turn modulate protein stability. Nat Struct Mol Biol 3, 54–58 (1996). https://doi.org/10.1038/nsb0196-54

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