Design of Peptide Models for β-Hairpins and Equilibrating Helix-Hairpin Structures

<p>It is well established that synthetic peptides containing a centrally positioned Type-I or Type-II β-turn can form well folded peptide hairpins (1). Earlier studies from this laboratory have established that D-Pro-Xxx segments nucleate β-hairpin structures, with formation of a central Type-...

Description complète

Enregistré dans:
Détails bibliographiques
Auteurs principaux: Chinnasamy Selvakkumar (Auteur), Eashwarwark Vikram Reddy (Auteur), Kesavanarayanan Krishnan Selvarajan (Auteur), Nazeerullah Rahamuthullah (Auteur), Muftha Mohamed Zarmouh (Auteur)
Format: Livre
Publié: International Journal of Nanomaterials, Nanotechnology and Nanomedicine - Peertechz Publications, 2016-05-04.
Sujets:
Accès en ligne:Connect to this object online.
Tags: Ajouter un tag
Pas de tags, Soyez le premier à ajouter un tag!

MARC

LEADER 00000 am a22000003u 4500
001 peertech__10_17352_2455-3492_000009
042 |a dc 
100 1 0 |a Chinnasamy Selvakkumar  |e author 
700 1 0 |a  Eashwarwark Vikram Reddy  |e author 
700 1 0 |a  Kesavanarayanan Krishnan Selvarajan  |e author 
700 1 0 |a  Nazeerullah Rahamuthullah  |e author 
700 1 0 |a Muftha Mohamed Zarmouh  |e author 
245 0 0 |a Design of Peptide Models for β-Hairpins and Equilibrating Helix-Hairpin Structures 
260 |b International Journal of Nanomaterials, Nanotechnology and Nanomedicine - Peertechz Publications,   |c 2016-05-04. 
520 |a <p>It is well established that synthetic peptides containing a centrally positioned Type-I or Type-II β-turn can form well folded peptide hairpins (1). Earlier studies from this laboratory have established that D-Pro-Xxx segments nucleate β-hairpin structures, with formation of a central Type-II β-turn (2). The octapeptide (Boc-Leu-Phe-Val-Aib-D-Ala-Leu-Phe- Val-OMe) is a rare example of a synthetic peptide hairpin, containing a central Type-I β-turn. Hairpins with Type-I turns are considerably more twisted than their Type-II counterparts. The Aib-Xxx segment has also been shown to adopt a Type-I β-turn structure, resulting in incorporation into the centre of a long synthetic, helical peptide (3) (Figures 1,2). </p><p><br></p> 
540 |a Copyright © Chinnasamy Selvakkumar et al. 
546 |a en 
655 7 |a Research Article  |2 local 
856 4 1 |u https://doi.org/10.17352/2455-3492.000009  |z Connect to this object online.