ALPHA-HELIX FORMATION IN C-PEPTIDE RNASE-A INVESTIGATED BY PARALLEL TEMPERING SIMULATIONS

DOI10.1142/S0129183107010292MaRDI QIDQ3434331zbMATH OpenOpenAlexFDO

Authors Gökhan Gökoğlu, Tarik Çelik

Publication date 25 April 2007

Published in International Journal of Modern Physics C (Search for Journal in Brave)

Full work available at URL https://doi.org/10.1142/s0129183107010292

zbMATH Keywords

parallel temperinggeneralized ensemblesc-peptide ribonuclease-A

Mathematics Subject Classification ID

Statistical mechanics of polymers (82D60)

Recommendations

• Multicanonical simulations of some peptides
• Molecular dynamics simulation of the nascent peptide chain in the ribosomal exit tunnel
• A replica-exchange approach to computing peptide conformational free energies
• Molecular dynamics simulation study on the structural stabilities of polyglutamine peptides
• Characterization of alpha helices interacting with nucleic acids
• Amino acid composition of parallel helix-helix interfaces
• Computational Science – ICCS 2005
• COMPOSITIONAL AND ENVIRONMENTAL DEPENDENCE OF THE STABILITY OF α-HELICES

Cites work

• CONFORMATION AND PHASE TRANSITION OF POLY-GLUTAMINE
• Practical Markov Chain Monte Carlo

Cited in

(3)

• Rational design, conformational analysis and membrane-penetrating dynamics study of Bac2A-derived antimicrobial peptides against gram-positive clinical strains isolated from pyemia
• Impact of temperature and pH value on the stability of hGHRH: an MD approach
• COMPOSITIONAL AND ENVIRONMENTAL DEPENDENCE OF THE STABILITY OF α-HELICES

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