Density functional theory study of the conformational space of an infinitely long polypeptide chain

作者：Ireta Joel^*; Scheffler Matthias

来源：Journal of Chemical Physics, 2009, 131(8): 085104.

DOI：10.1063/1.3207815

• density functional theory
• hydrogen bonds
• molecular biophysics
• molecular configurations
• potential energy surfaces
• proteins

The backbone conformational space of infinitely long polyalanine is investigated with density-functional theory and mapping the potential energy surface in terms of (L, theta) cylindrical coordinates. A comparison of the obtained (L, theta) Ramachandran-like plot with results from an extended set of protein structures shows excellent conformity, with the exception of the polyproline II region. It is demonstrated the usefulness of infinitely long polypeptide models for investigating the influence of hydrogen bonding and its cooperative effect on the backbone conformations. The results imply that hydrogen bonding together with long-range electrostatics is the main actuator for most of the structures assumed by protein residues.

• 出版日期2009-8-28