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Article overview
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Thermodynamics of the collapse transition of the all-backbone peptide Gly15 | D. Asthagiri
; | Date: |
2 May 2016 | Abstract: | Simulations 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 | Services: | Forum | Review | PDF | Favorites |
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