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Updated: Jun 19, 2026

Residue-Specific Exchange of Proline by Proline Analogs in Fluorescent Proteins: How "Molecular Surgery" of the Backbone Affects Folding and Stability
10:31

Residue-Specific Exchange of Proline by Proline Analogs in Fluorescent Proteins: How "Molecular Surgery" of the Backbone Affects Folding and Stability

Published on: February 3, 2022

末端機能群がポリプロリンII構造の安定性に及ぼす影響:実験と理論を組み合わせた研究

Michael Kuemin1, Sabine Schweizer, Christian Ochsenfeld

  • 1Department of Chemistry, University of Basel, St. Johanns-Ring 19, CH-4056 Basel, Switzerland.

Journal of the American Chemical Society
|October 2, 2009
PubMed
まとめ

端末機能群は,ポリプロリンヘリクスの安定性に大きく影響する. 充電された端末は,ポリプロリンII (PPII) ヘリクスを不安定化し,ポリプロリンI (PPI) ヘリクスを好み,キャップされた端末はPPIIを安定させる. 静電相互作用は,これらの形状的好みを支配する.

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Structure and Coordination Determination of Peptide-metal Complexes Using 1D and 2D 1H NMR14:44

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Proteins are chains of amino acids linked together by peptide bonds. Upon synthesis, a protein folds into a three-dimensional conformation, critical to its biological function. Interactions between its constituent amino acids guide protein folding, and hence the protein structure is primarily dependent on its amino acid sequence.
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