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Early events in the folding of an amphipathic peptide: A multinanosecond molecular dynamics study
Author(s) -
Chipot Christophe,
Maigret Bernard,
Pohorille Andrew
Publication year - 1999
Publication title -
proteins: structure, function, and bioinformatics
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.699
H-Index - 191
eISSN - 1097-0134
pISSN - 0887-3585
DOI - 10.1002/(sici)1097-0134(19990901)36:4<383::aid-prot2>3.0.co;2-p
Subject(s) - amphiphile , folding (dsp implementation) , peptide , dynamics (music) , protein folding , chemistry , molecular dynamics , physics , biochemistry , engineering , computational chemistry , organic chemistry , copolymer , polymer , acoustics , electrical engineering
Folding of the capped LQQLLQQLLQL peptide is investigated at the water–hexane interface by molecular dynamics simulations for 161.5 ns. Initially placed in the aqueous phase as a β‐strand, the peptide rapidly adsorbs to the interface, where it adopts an amphipathic conformation. The marginal presence of nonamphipathic structures throughout the complete trajectory indicates that the corresponding conformations are strongly disfavored at the interface. It is further suggestive that folding in an interfacial environment proceeds through a pathway of successive amphipathic intermediates. The energetic and entropic penalties involved in the conformational changes along this pathway markedly increase the folding time scales of LQQLLQQLLQL, explaining why the α‐helix, the hypothesized lowest free energy structure for a sequence with a hydrophobic periodicity of 3.6, has not been reached yet. The formation of a type I β‐turn at the end of the simulation confirms the importance of such motifs as initiation sites allowing the peptide to coalesce towards a secondary structure. Proteins 1999;36:383–399. © 1999 Wiley‐Liss, Inc.