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Updated: Mar 17, 2026

Residue-Specific Exchange of Proline by Proline Analogs in Fluorescent Proteins: How "Molecular Surgery" of the Backbone Affects Folding and Stability
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Structural and thermodynamic basis of proline-induced transmembrane complex stabilization

Thomas Schmidt1, Alan J Situ1, Tobias S Ulmer1

  • 1Department of Biochemistry &Molecular Biology and Zilkha Neurogenetic Institute, Keck School of Medicine, University of Southern California, 1501 San Pablo Street, Los Angeles, CA 90033, USA.

Scientific Reports
|July 21, 2016
PubMed
Summary

Proline substitutions in membrane proteins can stabilize structure by altering helix packing. This study reveals how a specific proline change in integrin αIIbβ3 enhances transmembrane complex stability.

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