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May 29, 1999Journal of the American Chemical Society

Alanine Is an Intrinsic α-Helix Stabilizing Amino Acid

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Authors

ESErik J. SpekVedantra Pharmaceuticals (United States)COC. Anders OlsonUniversity of California, San FranciscoZSZhengshuang ShiBioLegend (United States)

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Implication

Biochemical analysis demonstrates intrinsic alpha-helix stabilization by alanine in peptides, highlighting key determinants of protein folding.

Key Points

  • To evaluate the intrinsic capacity of alanine residues to promote and stabilize alpha-helical secondary structure in model peptide systems.
  • Assessed the conformational energetics and secondary structure formation of alanine-substituted peptide models.
  • Analyzed structural stabilization effects using peptide spectroscopic and chemical analysis methods.
  • Identified alanine as an intrinsically favorable residue for promoting alpha-helix stabilization in polypeptide chains.
  • Demonstrated that the compact chemical structure of alanine facilitates optimal helical backbone conformation without unfavorable steric hindrance.

Cite This Study

Spek et al. (1999) studied this question.

synapsesocial.com/papers/6a0da2cb6e03bc61cb09d787https://doi.org/10.1021/ja990056x
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Also Consider

Synapse has enriched 5 closely related papers on similar clinical questions. Consider them for comparative context:

  1. 1Conformational studies of poly‐<scp>L</scp>‐alanine in water1968 · 151 citations
  2. 2Residue helix parameters obtained from dichroic analysis of peptides of defined sequence1993 · 95 citations
  3. 3Helix propagation and N‐cap propensities of the amino acids measured in alanine‐based peptides in 40 volume percent trifluoroethanol1996 · 260 citations
  4. 4High Helicities of Lys-Containing, Ala-Rich Peptides Are Primarily Attributable to a Large, Context-Dependent Lys Stabilization1998 · 40 citations
  5. 5The role of context on α‐helix stabilization: Host‐guest analysis in a mixed background peptide model1997 · 51 citations