Protein Design is a Key Factor for Subunit-subunit Association

Details Protein Design is a Key Factor for Subunit-subunit Association Protein Design is a Key Factor for Subunit-subunit Association

1999-02-16

arxiv.org/abs/cond-mat/9902227v1

Physics

Condensed Matter

Statistical Mechanics

submitted to "Proceedings of the National Academy of Sciences, USA"

Scientific paper

Fundamental questions about the role of the quaternary structures are addressed using a statistical mechanics off-lattice model of a dimer protein. The model, in spite of its simplicity, captures key features of the monomer-monomer interactions revealed by atomic force experiments. Force curves during association and dissociation are characterized by sudden jumps followed by smooth behavior and form hysteresis loops. Furthermore, the process is reversible in a finite range of temperature stabilizing the dimer. It is shown that in the interface between the two monomeric subunits the design procedure naturally favors those amino acids whose mutual interaction is stronger. Furthermore it is shown that the width of the hysteresis loop increases as the design procedure improves, i.e. stabilizes more the dimer.

Affiliated with

Also associated with

No associations

Rating

Protein Design is a Key Factor for Subunit-subunit Association 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 Protein Design is a Key Factor for Subunit-subunit Association, we encourage you to share that experience with our LandOfFree.com community. Your opinion is very important and Protein Design is a Key Factor for Subunit-subunit Association will most certainly appreciate the feedback.

Rate now

Comments { 0 }

Profile ID: LFWR-SCP-O-200866