Thermodynamics of peptide aggregation processes: An analysis from perspectives of three statistical ensembles.
(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)
Please use this url to cite or link to this publication:
https://lup.lub.lu.se/record/1052850
- author
- Junghans, Christoph ; Bachmann, Michael LU and Janke, Wolfhard
- organization
- publishing date
- 2008
- type
- Contribution to journal
- publication status
- published
- subject
- in
- Journal of Chemical Physics
- volume
- 128
- issue
- 8
- article number
- 085103
- publisher
- American Institute of Physics (AIP)
- external identifiers
-
- pmid:18315086
- wos:000254047200060
- scopus:40149099893
- pmid:18315086
- 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
- 2016-04-01 11:53:06
- date last changed
- 2025-04-04 14:47:12
@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.}},
author = {{Junghans, Christoph and Bachmann, Michael and Janke, Wolfhard}},
issn = {{0021-9606}},
language = {{eng}},
number = {{8}},
publisher = {{American Institute of Physics (AIP)}},
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}},
doi = {{10.1063/1.2830233}},
volume = {{128}},
year = {{2008}},
}