Literature DB >> 17504093

Conformational analysis of Ac-NPGQ-NH(2) and Ac-VPaH-NH(2) by vibrational circular dichroism spectroscopy combined with molecular dynamics and quantum chemical calculations.

Attila Borics1, Richard F Murphy, Sándor Lovas.   

Abstract

Conformational properties of two potentially beta-turn forming peptides were determined using a strategy which combines MD simulations, IR and VCD spectroscopy and quantum chemical calculations. This strategy could be a useful alternative for solution conformational analysis of short flexible peptides and could help to identify VCD features which are as yet unknown.

Entities:  

Mesh：

Substances：

Year:  2007        PMID： 17504093     DOI： 10.2174/092986607780363907

Source DB:  PubMed          Journal:  Protein Pept Lett        ISSN： 0929-8665            Impact factor:   1.890


  4 in total

1.  The CLN025 decapeptide retains a β-hairpin conformation in urea and guanidinium chloride.

Authors:  Marcus P D Hatfield; Richard F Murphy; Sándor Lovas
Journal:  J Phys Chem B       Date:  2011-04-11       Impact factor: 2.991

2.  Molecular dynamics analysis of the conformations of a beta-hairpin miniprotein.

Authors:  Marcus P D Hatfield; Richard F Murphy; Sándor Lovas
Journal:  J Phys Chem B       Date:  2010-03-04       Impact factor: 2.991

3.  VCD spectroscopic properties of the beta-hairpin forming miniprotein CLN025 in various solvents.

Authors:  Marcus P D Hatfield; Richard F Murphy; Sándor Lovas
Journal:  Biopolymers       Date:  2010-05       Impact factor: 2.505

4.  The structure of bioactive analogs of the N-terminal region of gastrin-17.

Authors:  Jeffrey Copps; Richard F Murphy; Sándor Lovas
Journal:  Peptides       Date:  2009-09-18       Impact factor: 3.750
  4 in total

北京卡尤迪生物科技股份有限公司 © 2022-2023.