title: Molecular dynamics of some pentapeptides having a strong tendency to helical conformation.
abstract: 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.
authors.affiliation: State Key Laboratory of Pharmaceutical Biotechnology, College of Life Sciences, Nanjing University, Nanjing 210093, China.
authors.forename: Zhuo-Ran
authors.initials: ZR
authors.lastname: Huang
authors.forename: Tong-Yang
authors.initials: TY
authors.lastname: Zhu
authors.forename: Ting-Ting
authors.initials: TT
authors.lastname: Wang
authors.forename: Xiao-Ning
authors.initials: XN
authors.lastname: Wang
authors.forename: Jie
authors.initials: J
authors.lastname: Yang
mesh_terms: D000595:Amino Acid Sequence; D015233:Models, Statistical; D056004:Molecular Dynamics Simulation; D009010:Monte Carlo Method; D009842:Oligopeptides / Q000737:chemistry* / Q000235:genetics; D017433:Protein Structure, Secondary
chemical_list: D009842:Oligopeptides