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EXPLORING THE ROLE OF C–H….Π INTERACTIONS ON THE STRUCTURAL STABILITY OF MEMBRANE PROTEINS
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BibTeX
@MISC{Ramanathan_exploringthe,
author = {K. Ramanathan and V. Shanthi and Rao Sethumadhavan},
title = {EXPLORING THE ROLE OF C–H….Π INTERACTIONS ON THE STRUCTURAL STABILITY OF MEMBRANE PROTEINS},
year = {}
}
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Abstract
C–H...π interactions are known to be important contributors to protein stability. In this study, we have analyzed the influence of C–H…π interactions on the structural stability of membrane proteins. In the data set, a total of 408 C–H….π interactions were observed. The most prominent representatives are the interactions between aromatic C–H donor groups and aromatic π acceptors. Ninety four percent of the C–H….π interactions between side chain to side chain and remaining six percent of the C–H….π interactions were observed between sidechain to side-chain five-membered aromatic ring. Long-range C–H….π interactions are the predominant type of interactions in membrane proteins data set. The secondary structure preference, solvent accessibility and stabilization centers of C–H….π interacting residues were estimated. Moreover, the study shows that 72 % of the donor residues and 68 % of the acceptor residues are highly conserved.. It is concluded that the C–H….π interaction can, indeed, be categorized as a true stabilizing force in membrane proteins.
Keyphrases
structural stability membrane protein membrane protein data set secondary structure preference structural stability important contributor predominant type donor residue acceptor residue prominent representative aromatic donor group aromatic acceptor stabilization center side-chain five-membered aromatic ring side chain solvent accessibility membrane protein data set
