Computational scrutiny of the effect of N-terminal proline and residue stereochemistry in the nucleation of α-helix fold

Bhupesh Goyal; Anil Kumar; Kinshuk Raj Srivastava; Susheel Durani

doi:10.1039/c6ra10934a

January 1, 2016RSC Advances

Computational scrutiny of the effect of N-terminal proline and residue stereochemistry in the nucleation of α-helix fold

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Key Points

The research investigates how N-terminal residue mutations influence the nucleation of alpha-helix structures in specific peptides.
Utilized computational tools to analyze the effects of N-terminal proline and residue stereochemistry.
Studied variants of peptides containing D-Ala and D-Pro residues.
Assessed the folding behavior of peptides Ac–DAla3–NHMe, Ac–DPro–Ala3–NHMe, and Ac–DPro–LPro–Ala2–NHMe.
N-terminal proline mutations significantly influence helix formation in the analyzed peptide sequences.
Distinct differences were observed in the nucleation behaviors across the peptide variants, emphasizing the role of stereochemistry.

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Implication

Computational analysis explores nucleation of helical folds in peptides, suggesting implications for protein folding.

Abstract

N-Terminal l- to d-residue mutation nucleate helical fold in Ac–DAla–LAla₃–NHMe (Ib, m2), Ac–DPro–LAla₃–NHMe (IIb, m1), and Ac–DPro–LPro–LAla₂–NHMe (IIIb, m2) peptides.

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Goyal et al. (2016) studied this question.

synapsesocial.com/papers/6a2195f9cdf8429e7e5fd619 https://doi.org/10.1039/c6ra10934a

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Computational scrutiny of the effect of N-terminal proline and residue stereochemistry in the nucleation of α-helix fold

Key Points

Ask about this paper

Implication

Abstract

Discussion

Cite This Study

Computational scrutiny of the effect of N-terminal proline and residue stereochemistry in the nucleation of α-helix fold

Key Points

Ask about this paper

Implication

Abstract

Discussion

Cite This Study

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