Thermodynamics of Protein Folding and Design
Author
Summary, in English
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.
Publishing year
2000
Language
English
Document type
Dissertation
Publisher
Theoretical Physics, Lund University, Sölvegatan 14A, 223 62 Lund, Sweden
Topic
- 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
Status
Published
Supervisor
- [unknown] [unknown]
ISBN/ISSN/Other
- ISBN: 91-628-4305-2
Defence date
20 October 2000
Defence time
10:15
Defence place
Sal F, Theoretical Physics
Opponent
- Hue Sun Chan