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18 February 2025
 
  » arxiv » 1605.0350

 Article overview



Thermodynamics of the collapse transition of the all-backbone peptide Gly15
D. Asthagiri ;
Date 2 May 2016
AbstractSimulations show Gly15, a polypeptide lacking any side-chains, can collapse in water. Peptide hydration greatly favors the expanded state of the chain, despite primitive hydrophobic effects favoring chain collapse. The net free energy of collapse is seen to be a delicate balance between opposing intra-peptide and hydration effects, with intra-peptide contributions favoring collapse by a small margin. The favorable intra-peptide interactions are primarily electrostatic in origin. Favorable interaction between between C=O dipoles, hydrogen bonding interaction between C=O and N-H groups, and favorable interaction between N-H groups are found to be important in the electrostatic interaction.
Source arXiv, 1605.0350
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