Promotion of Folding in Hybrid Peptides through Unconstrained γ Residues: Structural Characterization of Helices in (αγγ)  n   and (αγα)  n   Sequences | Zendy

Basuroy Krishnayan | Zendy; Dinesh Bhimareddy | Zendy; Shamala Narayanaswamy | Zendy; Balaram Padmanabhan | Zendy

Premium

Promotion of Folding in Hybrid Peptides through Unconstrained γ Residues: Structural Characterization of Helices in (αγγ) n and (αγα) n Sequences

Author(s) -

Basuroy Krishnayan,

Dinesh Bhimareddy,

Shamala Narayanaswamy,

Balaram Padmanabhan

Publication year - 2013

Publication title -

angewandte chemie international edition

Language(s) - English

Resource type - Journals

SCImago Journal Rank - 5.831

H-Index - 550

eISSN - 1521-3773

pISSN - 1433-7851

DOI - 10.1002/anie.201209324

Subject(s) - residue (chemistry) , folding (dsp implementation) , hydrogen bond , helix (gastropod) , crystallography , protein folding , sequence (biology) , chemistry , stereochemistry , peptide sequence , amino acid residue , molecule , biochemistry , biology , gene , ecology , organic chemistry , snail , electrical engineering , engineering

The γ‐amino acid residue γ 4 (R)Val promotes helical folding even in short (αγα) n sequences. A mixed C 12 /C 14 helix (in which hydrogen bonds close a ring of 12 or 14 atoms) is established in a 12‐residue (αγγ) 4 sequence (see picture, right). The 6‐residue (αγα) 2 sequence (left), devoid of backbone conformational constraints, folds into a C 12 /C 10 helix.

This content is not available in your region!

Continue researching here.

Having issues? You can contact us here

Accelerating Research