Protein flexibility of dimers: do symmetric motions play a role in allosteric interactions?

Schulze, Bernd and Sljoka, Adnan and Whiteley, Walter (2011) Protein flexibility of dimers: do symmetric motions play a role in allosteric interactions? In: AIP Conference Proceedings of Advances in Mathematical and Computational Methods : Addressing Modern Challenges of Science, Technology, and Society 2011. American Institute of Physics, pp. 135-138.

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Abstract

How a protein functions depends both on having basic stable forms (tertiary structure) and having some residual flexibility supported within that structure. The modeling of protein flexibility and rigidity in terms imported from physics and engineering has been developed through the theory of generically rigid frameworks and a fast combinatorial algorithm is available in programs such as FIRST. Recent theoretical work on rigidity of frameworks has modified this generic analysis to include the basic symmetry and to predict additional motions. In particular, a framework which would normally count to be combinatorially minimally rigid in generic realizations has been shown to become flexible when realized with 2‐fold rotational symmetry in 3‐space. Protein dimers, formed by two copies of a protein are a good case study for impact of this added flexibility due to 2‐fold rotational symmetry, as dimers generally self‐assemble with a 2‐fold rotational axis, for reasons of minimal energy. We describe an algorithm for predicting possible additional flexibility and consider the question: What is the significance of this for the behavior of dimers, such as tryptophan repressor?

Item Type:
Contribution in Book/Report/Proceedings
ID Code:
63641
Deposited By:
Deposited On:
25 Apr 2013 09:24
Refereed?:
Yes
Published?:
Published
Last Modified:
08 Jul 2020 10:14