Effects of temperature and salt concentration on the structural stability of human lymphotactin: insights from molecular simulations.

ABSTRACT: Extensive molecular dynamics (MD) simulations ( approximately 70 ns total) with explicit solvent molecules and salt ions are carried out to probe the effects of temperature and salt concentration on the structural stability of the human Lymphotactin (hLtn). The distribution of ions near the protein surface and the stability of various structural motifs are observed to exhibit interesting dependence on the local sequence and structure. Whereas chloride association to the protein is overall enhanced as the temperature increases, the sodium distribution in the C-terminal helical region and, to a smaller degree, the chloride distribution in the same region are found higher at the lower temperature. The similar trend is also observed in nonlinear Poisson-Boltzmann calculations with a temperatur

SUBMITTER: Formaneck MS 

PROVIDER: S-EPMC2600855 | biostudies-literature | 2006 Jul

REPOSITORIES: biostudies-literature