Thermodynamic Studies of Macromolecular Models
(1997) Abstract
 The thermodynamic properties of single chain polyelectrolyte and protein models are studied using Monte Carlo simulations and (for the polyelectrolyte models) variational calculations and high and lowtemperature expansions. A variational method is used for minimizing LennardJones energies and for estimating endtoend distances for a rigid Coulomb chain at finite temperatures. A polyelectrolyte chain is viewed as Gaussian chain augmented with a Coulomb or screened Coulomb (DebyeHuckel) interaction between all pairs of monomers. Variational calculations are also used together with Monte Carlo simulations to study the behavior of a titrating polyelectrolyte. Furthermore a method for mapping the original polymer to a smaller one by... (More)
 The thermodynamic properties of single chain polyelectrolyte and protein models are studied using Monte Carlo simulations and (for the polyelectrolyte models) variational calculations and high and lowtemperature expansions. A variational method is used for minimizing LennardJones energies and for estimating endtoend distances for a rigid Coulomb chain at finite temperatures. A polyelectrolyte chain is viewed as Gaussian chain augmented with a Coulomb or screened Coulomb (DebyeHuckel) interaction between all pairs of monomers. Variational calculations are also used together with Monte Carlo simulations to study the behavior of a titrating polyelectrolyte. Furthermore a method for mapping the original polymer to a smaller one by introducing a corrective nearestneighbor interaction is presented. The underlying assumptions for this approach is examined using high and lowtemperature expansions. The effect of the screening length on the stiffness, defined by the persistence length, of a screened Coulomb chain is studied. Moreover a three dimensional offlattice model for protein folding is presented. The model has two types of residues, hydrophobic and hydrophilic respectively, that interact via a sequence dependent LennardJones potential. The influence of sequence independent local interactions is studied as well as the folding properties and the formation of the native state. (Less)
Please use this url to cite or link to this publication:
http://lup.lub.lu.se/record/29367
 author
 Sommelius, Ola
 opponent

 Marinari, Enzo, Italy
 organization
 publishing date
 1997
 type
 Thesis
 publication status
 published
 subject
 keywords
 classical mechanics, Mathematical and general theoretical physics, termodynamik, klassisk mekanik, Matematisk och allmän teoretisk fysik, statistisk fysik, gravitation, kvantmekanik, relativitet, quantum mechanics, relativity, statistical physics, thermodynamics, Fysicumarkivet A:1997:Sommelius
 pages
 15 pages
 publisher
 Department of Theoretical Physics, Lund University
 defense location
 Auditorium, Dept. of Theoretical Physics
 defense date
 19970529 10:15
 external identifiers

 Other:ISRN: LUNFD6/(NFTF1033)/115/(1997)
 ISBN
 9162825461
 language
 English
 LU publication?
 yes
 id
 0f7a418aca1541b69ba63c4b63ef2728 (old id 29367)
 date added to LUP
 20070613 13:22:51
 date last changed
 20160919 08:45:11
@misc{0f7a418aca1541b69ba63c4b63ef2728, abstract = {The thermodynamic properties of single chain polyelectrolyte and protein models are studied using Monte Carlo simulations and (for the polyelectrolyte models) variational calculations and high and lowtemperature expansions. A variational method is used for minimizing LennardJones energies and for estimating endtoend distances for a rigid Coulomb chain at finite temperatures. A polyelectrolyte chain is viewed as Gaussian chain augmented with a Coulomb or screened Coulomb (DebyeHuckel) interaction between all pairs of monomers. Variational calculations are also used together with Monte Carlo simulations to study the behavior of a titrating polyelectrolyte. Furthermore a method for mapping the original polymer to a smaller one by introducing a corrective nearestneighbor interaction is presented. The underlying assumptions for this approach is examined using high and lowtemperature expansions. The effect of the screening length on the stiffness, defined by the persistence length, of a screened Coulomb chain is studied. Moreover a three dimensional offlattice model for protein folding is presented. The model has two types of residues, hydrophobic and hydrophilic respectively, that interact via a sequence dependent LennardJones potential. The influence of sequence independent local interactions is studied as well as the folding properties and the formation of the native state.}, author = {Sommelius, Ola}, isbn = {9162825461}, keyword = {classical mechanics,Mathematical and general theoretical physics,termodynamik,klassisk mekanik,Matematisk och allmän teoretisk fysik,statistisk fysik,gravitation,kvantmekanik,relativitet,quantum mechanics,relativity,statistical physics,thermodynamics,Fysicumarkivet A:1997:Sommelius}, language = {eng}, pages = {15}, publisher = {ARRAY(0x79d4620)}, title = {Thermodynamic Studies of Macromolecular Models}, year = {1997}, }