On the intrinsic propensity of the Asn-Gly sequence to fold into type I′ β-turn: molecular dynamics simulations of Asn-Gly β-turn containing peptide sequences-Reference-Cited by-同舟云学术

On the intrinsic propensity of the Asn-Gly sequence to fold into type I′ β-turn: molecular dynamics simulations of Asn-Gly β-turn containing peptide sequences

Published:2017-11-22 Issue:15 Volume:36 Page:3916-3925
ISSN:0739-1102
Container-title:Journal of Biomolecular Structure and Dynamics
language:en
Short-container-title:Journal of Biomolecular Structure and Dynamics

Author:

Sharadadevi Ambure¹,Nagaraj Ramakrishnan¹

Affiliation:

1. CSIR – Centre for Cellular and Molecular Biology, Hyderabad, India

Funder

Department of Science and Technology, Government of Kerala

J C Bose Fellowship, DST

Publisher

Informa UK Limited

Subject

Molecular Biology,General Medicine,Structural Biology

Link

https://www.tandfonline.com/doi/pdf/10.1080/07391102.2017.1403958

Reference17 articles.

1. Formation and stability of β-hairpin structures in polypeptides

2. Extension of the classical classification of β-turns

3. Nascent β -Hairpin Formation of a Natively Unfolded Peptide Reveals the Role of Hydrophobic Contacts

4. Thermodynamics and Kinetics of Folding of Two Model Peptides Investigated by Molecular Dynamics Simulations

5. Minimal model systems for β-sheet secondary structure in proteins

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1. A molecular dynamics simulation study on the propensity of Asn-Gly-containing heptapeptides towards β-turn structures: Comparison with ab initio quantum mechanical calculations;PLOS ONE;2020-12-03

2. Identification of protegrin-1 as a stable and nontoxic scaffold among protegrin family – a computational approach;Journal of Biomolecular Structure and Dynamics;2018-12-05