Sökning: "Beräkningsbiologi Och Biologisk Fysik"
Visar resultat 11 - 15 av 36 avhandlingar innehållade orden Beräkningsbiologi Och Biologisk Fysik.
11. Computational Prediction Models for Proteolytic Cleavage and Epitope Identification
Sammanfattning : The biological functions of proteins depend on their physical interactions with other molecules, such as proteins and peptides. Therefore, modeling the protein-ligand interactions is important for understanding protein functions in different biological processes. LÄS MER
12. Modeling of Protein Folding and Genetic Networks
Sammanfattning : Models for potein folding are developed and applied to peptides and small proteins with both α-helix and β-sheet structure. The energy functions, in which effective hydrophobicity forces and hydrogen bonds are taken to be the two central terms, are sequence-based and deliberately kept simple. LÄS MER
13. Physical Modeling of Protein Folding
Sammanfattning : Sequence-based models for protein folding are developed and tested on peptides with both alpha- and beta-structure, and on small three-helix-bundle proteins. The interaction potentials of the models are minimalistic and based mainly on hydrogen bonding and effective hydrophobicity forces. LÄS MER
14. Thermodynamics of Protein Folding and Design
Sammanfattning : 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. LÄS MER
15. Hydrophobicity Patterns in Protein Folding
Sammanfattning : The protein folding problem is addressed focussing on the hydro- phobicity patterns in the amino acid sequences and structures. Both real and model proteins are investigated. The hydrophobicity pattern of real proteins is probed in two ways. First, it is asked which binary pattern is most conserved within groups of related proteins. LÄS MER