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Homochiral Stereochemistry: The Missing Link of Structure to Energetics in Protein Folding

DSpace at IIT Bombay

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Title Homochiral Stereochemistry: The Missing Link of Structure to Energetics in Protein Folding
 
Creator KUMAR, A
RAMAKRISHNAN, V
RANBHOR, R
PATEL, K
DURANI, S
 
Subject density-functional theory
alpha-helix formation
particle mesh ewald
polyproline-ii
conformational preferences
polypeptide-chains
unfolded proteins
hydrogen-bonds
amino-acids
gas-phase
 
Description The notion is tested that homochiral stereochemistry being ubiquitous to protein Structure could be critical to protein folding as well, causing it to become frustrated energetically providing the basis for its solvent- and sequence-mediated control. The proof. in support of the notion is found in a consensus of experiment and computation according to which suitable oligopeptides are in their folding-unfolding equilibria, at both macrostate and microstate levels, susceptible to dielectric because of the conflict of peptide-chain electrostatics with interpeptide hydrogen bonds when the structure is poly-L but not when it is alternating-L,D. The argument is thus made that homochiral stereochemistry may in protein folding provide the unifying basis for its solvent- and sequence-mediated control based on screening of peptide-chain electrostatics Under conflict with folding of the chain due to homochiral stereochemistry. Dielectric is brought into spotlight as the effect comparatively obscure but presumably critical to the folding in protein structure for its control.
 
Publisher AMER CHEMICAL SOC
 
Date 2011-07-14T06:55:23Z
2011-12-26T12:48:14Z
2011-12-27T05:47:12Z
2011-07-14T06:55:23Z
2011-12-26T12:48:14Z
2011-12-27T05:47:12Z
2009
 
Type Article
 
Identifier JOURNAL OF PHYSICAL CHEMISTRY B, 113(51), 16435-16442
1520-6106
http://dx.doi.org/10.1021/jp906811k
http://dspace.library.iitb.ac.in/xmlui/handle/10054/3887
http://hdl.handle.net/10054/3887
 
Language en