Hydrogen Bonds, Hydrophobicity Forces and the Character of the Collapse Transition

Details Hydrogen Bonds, Hydrophobicity Forces and the Character of the Collapse Transition Hydrogen Bonds, Hydrophobicity Forces and the Character of the Collapse Transition

2001-07-09

arxiv.org/abs/cond-mat/0107177v1

J. Biol. Phys. 27 (2001) 169-179

Physics

Condensed Matter

Soft Condensed Matter

14 pages, 8 figures

Scientific paper

We study the thermodynamic behavior of a model protein with 54 amino acids that is designed to form a three-helix bundle in its native state. The model contains three types of amino acids and five to six atoms per amino acid, and has the Ramachandran torsion angles as its only degrees of freedom. The force field is based on hydrogen bonds and effective hydrophobicity forces. We study how the character of the collapse transition depends on the strengths of these forces. For a suitable choice of these two parameters, it is found that the collapse transition is first-order-like and coincides with the folding transition. Also shown is that the corresponding one- and two-helix segments make less stable secondary structure than the three-helix sequence.

Affiliated with

Also associated with

No associations

Rating

Hydrogen Bonds, Hydrophobicity Forces and the Character of the Collapse Transition does not yet have a rating. At this time, there are no reviews or comments for this scientific paper.

If you have personal experience with Hydrogen Bonds, Hydrophobicity Forces and the Character of the Collapse Transition, we encourage you to share that experience with our LandOfFree.com community. Your opinion is very important and Hydrogen Bonds, Hydrophobicity Forces and the Character of the Collapse Transition will most certainly appreciate the feedback.

Rate now

Comments { 0 }

Profile ID: LFWR-SCP-O-366569