Molecular dynamics study of the active site of methylamine dehydrogenase

Article Abstract:

Molecular dynamics simulations of methylamine dehydrogenase (MADH) were performed by obtaining AMBER94 force field parameters in order to characterize the dynamics of the active site prior to the proton transfer step. It was found that the average distance between the hydrogen nucleus to be transferred and the acceptor atom, when the imino group was protonated were smaller than the distances found when the imino group was not protonated.

Oxidoreductases, Atomic properties

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Solution structure of the aqueous model peptide N-methylacetamide

Article Abstract:

A study performed classical molecular dynamics simulations of aqueous N-methylacetamide (NMA) is conducted across a concentration range at 308 K. Results reveal that with increases in NMA concentration water molecules become progressively more isolated, forming dimers and trimers hydrogen-bonded to NMA.

Observations, Peptides, Hydrogen bonding, Hydrogen bonds, Structure

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