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Molecular Dynamics of Some Pentapeptides Having a Strong Tendency to Helical Conformation

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Some pentapeptides with higher alpha-helical tendency possess typical sequence pattern, such as “+ - + + - - +”, “+ - - + - - +”, “+ - + - - - +”, and “- + + - - - +” (“+” = D,N,E,Q,K,R,T,C, or H; “-” = L,I,V, or A), especially symmetrical motifs (a pair of reverse sequences beside palindromic segments), such as ALALA, QQAQE/EQAQQ, and REALE/ELAER, hint that the nascent peptide can fold a certain conformation in a two-way folding fashion.

Keywords: Folding models; molecular dynamics; symmetrical motifs

Document Type: Research Article


Publication date: March 1, 2010

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  • Protein & Peptide Letters publishes short papers in all important aspects of protein and peptide research, including structural studies, recombinant expression, function, synthesis, enzymology, immunology, molecular modeling, drug design etc. Manuscripts must have a significant element of novelty, timeliness and urgency that merit rapid publication. Reports of crystallisation, and preliminary structure determinations of biologically important proteins are acceptable. Purely theoretical papers are also acceptable provided they provide new insight into the principles of protein/peptide structure and function.

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