| Summary: | 碩士 === 國立東華大學 === 應用物理研究所 === 92 ===
Proteins are important biological macromolecules which are composed of 20 kinds of amino acids. They have important biological functions for life, and these functions depend highly on their three dimensional structures. Because the processes of protein folding are too complex, until now there has no good theory to explain protein folding precisely.
In this thesis we first review relevant theories of protein folding. Then we study the properties of HP chains on the square lattice by exact enumeration and other methods in equilibrium statistical mechanics. Our goal is to distinguish protein-like sequences, which are capable of folding to an unique ground state both kinetically and thermodynamically, from random sequences. We find that among all HP chains, protein-like chains own native states of high designability, and their sequences only contain short sections of H monomers and alternate HP patterns.
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