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Thermodynamics of peptide aggregation processes: An analysis from perspectives of three statistical ensembles.

Junghans, Christoph; Bachmann, Michael LU and Janke, Wolfhard (2008) In Journal of Chemical Physics 128(8).
Abstract
We employ a mesoscopic model for studying aggregation processes of proteinlike hydrophobic-polar heteropolymers. By means of multicanonical Monte Carlo computer simulations, we find strong indications that peptide aggregation is a phase separation process, in which the microcanonical entropy exhibits a convex intruder due to non-negligible surface effects of the small systems. We analyze thermodynamic properties of the conformational transitions accompanying the aggregation process from the multicanonical, canonical, and microcanonical perspective. It turns out that the microcanonical description is particularly advantageous as it allows for unraveling details of the phase-separation transition in the thermodynamic region, where the... (More)
We employ a mesoscopic model for studying aggregation processes of proteinlike hydrophobic-polar heteropolymers. By means of multicanonical Monte Carlo computer simulations, we find strong indications that peptide aggregation is a phase separation process, in which the microcanonical entropy exhibits a convex intruder due to non-negligible surface effects of the small systems. We analyze thermodynamic properties of the conformational transitions accompanying the aggregation process from the multicanonical, canonical, and microcanonical perspective. It turns out that the microcanonical description is particularly advantageous as it allows for unraveling details of the phase-separation transition in the thermodynamic region, where the temperature is not a suitable external control parameter anymore. (Less)
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author
organization
publishing date
type
Contribution to journal
publication status
published
subject
in
Journal of Chemical Physics
volume
128
issue
8
publisher
American Institute of Physics
external identifiers
  • pmid:18315086
  • wos:000254047200060
  • scopus:40149099893
ISSN
0021-9606
DOI
10.1063/1.2830233
language
English
LU publication?
yes
id
c97825bb-6bf7-4611-b974-7efcceba52e5 (old id 1052850)
date added to LUP
2008-04-03 11:11:12
date last changed
2017-10-01 03:42:31
@article{c97825bb-6bf7-4611-b974-7efcceba52e5,
  abstract     = {We employ a mesoscopic model for studying aggregation processes of proteinlike hydrophobic-polar heteropolymers. By means of multicanonical Monte Carlo computer simulations, we find strong indications that peptide aggregation is a phase separation process, in which the microcanonical entropy exhibits a convex intruder due to non-negligible surface effects of the small systems. We analyze thermodynamic properties of the conformational transitions accompanying the aggregation process from the multicanonical, canonical, and microcanonical perspective. It turns out that the microcanonical description is particularly advantageous as it allows for unraveling details of the phase-separation transition in the thermodynamic region, where the temperature is not a suitable external control parameter anymore.},
  articleno    = {085103},
  author       = {Junghans, Christoph and Bachmann, Michael and Janke, Wolfhard},
  issn         = {0021-9606},
  language     = {eng},
  number       = {8},
  publisher    = {American Institute of Physics},
  series       = {Journal of Chemical Physics},
  title        = {Thermodynamics of peptide aggregation processes: An analysis from perspectives of three statistical ensembles.},
  url          = {http://dx.doi.org/10.1063/1.2830233},
  volume       = {128},
  year         = {2008},
}