Can Helical Peptides Unwind One Turn at a Time? - Controlled Conformational Transitions in α,β(2,3)-Hybrid Peptides

Dhayalan Balamurugan; Kannoth M Muraleedharan

doi:10.1002/chem.201501198

Can Helical Peptides Unwind One Turn at a Time? - Controlled Conformational Transitions in α,β(2,3)-Hybrid Peptides

Chemistry. 2015 Jun 22;21(26):9332-8. doi: 10.1002/chem.201501198. Epub 2015 May 15.

Authors

Dhayalan Balamurugan¹, Kannoth M Muraleedharan²

Affiliations

¹ Department of Chemistry, Indian Institute of Technology Madras, Chennai, 600036 (India).
² Department of Chemistry, Indian Institute of Technology Madras, Chennai, 600036 (India). [email protected].

PMID: 25980664
DOI: 10.1002/chem.201501198

Abstract

Unfolding of helical trans-β(2,3) -hybrid peptides with (α-β)n α composition, when executed by increasing solvent polarity or temperature, proceeded in a systematic manner with the turns unwinding sequentially; C-terminal region of these peptides were first to unwind and the process propagated towards N terminus with more and more β residues equilibrating from the gauche to the anti rotameric state across Cα-Cβ . This is evidenced by clear change in their Cβ H signal splitting, (3)JCαH-CβH values, and sequential disappearance of i,i+2 NOEs.

Keywords: alpha/beta-hybrid peptides; amino acids; foldamers; helix-strand hybrid; protein folding.

Publication types

Research Support, Non-U.S. Gov't

MeSH terms

Amino Acids / chemistry*
Helix-Turn-Helix Motifs
Hydrogen Bonding
Magnetic Resonance Spectroscopy
Models, Molecular
Peptides / chemistry*
Protein Conformation
Solvents / chemistry

Substances

Amino Acids
Peptides
Solvents