Thermodynamics of Protein Folding and Design

Research output: ThesisDoctoral Thesis (compilation)

Abstract

The protein folding and protein design problems are addressed, using coarse-grained models with only two types of amino acids, hydrophobic and hydrophilic. In addition to hydrophobicity forces, the models contain sequence-independent local interactions which are found to strongly influence the thermodynamics of these models. The models are studied using the dynamical-parameter Monte Carlo method. A Monte Carlo approach to protein design based on this method is developed, and the usefulness of the method for another difficult problem in computational biology, sequence assembly, is explored. Finally, the statistical distribution of hydrophobicity in real and model protein sequences is studied.

Details

Authors
  • Erik Sandelin
Organisations
Research areas and keywords

Subject classification (UKÄ) – MANDATORY

  • Biophysics

Keywords

  • protein folding, hydrophobicity, Monte Carlo, sequence analysis, sequence assembly, shotgun sequencing, Mathematical and general theoretical physics, classical mechanics, quantum mechanics, relativity, gravitation, statistical physics, Matematisk och allmän teoretisk fysik, thermodynamics, termodynamik, Fysicumarkivet A:2000:Sandelin, statistisk fysik, relativitet, protein design, klassisk mekanik, kvantmekanik
Original languageEnglish
QualificationDoctor
Awarding Institution
Supervisors/Assistant supervisor
  • [unknown], [unknown], Supervisor, External person
Award date2000 Oct 20
Publisher
  • Theoretical Physics, Lund University, Sölvegatan 14A, 223 62 Lund, Sweden
Print ISBNs91-628-4305-2
Publication statusPublished - 2000
Publication categoryResearch

Bibliographic note

Defence details Date: 2000-10-20 Time: 10:15 Place: Sal F, Theoretical Physics External reviewer(s) Name: Chan, Hue Sun Title: [unknown] Affiliation: [unknown] ---