Conformations of cysteine disulfides of peptide toxins: Advantage of differentiating forward and reverse asymmetric disulfide conformers

Journal of Biomolecular Structure & Dynamics
Panchada Ch V GovinduKonkallu Hanumae Gowd

Abstract

Conformations of cysteine disulfides were analyzed in X-ray, nuclear magnetic resonance (NMR), and co-crystal structures of peptide toxins retrieved from Protein Data Bank. The parameters side chain torsional angles, disulfide strain energy, interatomic Cα/Cβ distances, and Ramachandran angles were used as probes to derive conformational features of cysteine disulfides. Schmidt, Ho, and Hogg ( 2006 ) Allosteric disulfide bonds. Biochemistry, 45, 7429-7433 scheme was adapted to classify the disulfide conformations of peptide toxins. Anomalies were observed while treating "forward" and "reverse" asymmetric disulfide conformers as same disulfide conformation in peptide toxins. Thus, new scheme was proposed to classify "forward" and "reverse" asymmetric disulfide conformers separately. Total available conformers space for classification of toxins disulfides is 32. Interestingly, all 32 disulfide conformations are observed in peptide toxins. -LHSpiral is predominant disulfide conformation of peptide toxins. Significant variations were observed in population of occurrence of disulfide conformers, disulfide strain energy, and distribution of DCα-Cα and DCβ-Cβ values between X-ray, NMR, and co-crystal structures of peptide toxins. The ...Continue Reading

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Apr 4, 2017·Computational Biology and Chemistry·Panchada Ch V GovinduKonkallu Hanumae Gowd

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Citations

Feb 28, 2020·Journal of Peptide Science : an Official Publication of the European Peptide Society·Ashwini DolleKonkallu Hanumae Gowd
Dec 31, 2020·Proteins·K Kasi Amarnath ReddyKonkallu Hanumae Gowd
Aug 15, 2019·Chemical Reviews·Solomon D AppavooAndrei K Yudin

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Methods Mentioned

BETA
X-ray
NMR
electron cryomicroscopy

Software Mentioned

SynLHHook
LHSpiral
ViewerLite
Origin Pro
StatPac
AntiLHHook
RHSpiral

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