INVESTIGADORES
VILLARREAL marcos ariel
congresos y reuniones científicas
Título:
Stability of alfa-helical peptides studied by molecular dynamics simulations
Autor/es:
VILLARREAL MA; MONTICH GG
Lugar:
Campinhas, SP, Brasil.
Reunión:
Congreso; IV Congreso de Biofísica del Cono Sur.; 2000
Resumen:
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We present a molecular dynamics simulation study od the
stability of alanine- (A) and Lysine- (K) based hexapeptides in
water. Sixteen runs of 2 ns long each are performed in explicit
solvent and in the NPT ensamble. The simulated sequences are AAAAAA,
AKAAAK, KAAAAK and KKKKKK. The main results are: I) The a-helix
conformation of these peptides have similar stability at 300 K. II)
This stability is noticeably high for peptides of this size when
compared with previus simulations. The observed stability is in line
with with the s value of A and K residues in the Zimm-Brag theory of
helix-coil transitions. We also discuss the interations that
stabilize tha a-helix conformation of this peptides and the
importance of multiple runs to achieve consisten results.