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- Title
On the Emergence of Orientational Order in Folded Proteins with Implications for Allostery.
- Authors
Chakraborty, Debayan; Mugnai, Mauro Lorenzo; Thirumalai, D.; Odijk, Theo; van der Schoot, Paul; Chakraborty, Abhijit
- Abstract
The beautiful structures of single- and multi-domain proteins are clearly ordered in some fashion but cannot be readily classified using group theory methods that are successfully used to describe periodic crystals. For this reason, protein structures are considered to be aperiodic, and may have evolved this way for functional purposes, especially in instances that require a combination of softness and rigidity within the same molecule. By analyzing the solved protein structures, we show that orientational symmetry is broken in the aperiodic arrangement of the secondary structure elements (SSEs), which we deduce by calculating the nematic order parameter, P 2 . We find that the folded structures are nematic droplets with a broad distribution of P 2 . We argue that a non-zero value of P 2 , leads to an arrangement of the SSEs that can resist external forces, which is a requirement for allosteric proteins. Such proteins, which resist mechanical forces in some regions while being flexible in others, transmit signals from one region of the protein to another (action at a distance) in response to binding of ligands (oxygen, ATP, or other small molecules).
- Subjects
ALLOSTERIC proteins; SMALL molecules; PROTEIN structure; PROTEINS; GROUP theory; PURINERGIC receptors
- Publication
Symmetry (20738994), 2021, Vol 13, Issue 5, p770
- ISSN
2073-8994
- Publication type
Article
- DOI
10.3390/sym13050770