標題: Global and Local Structural Changes of Protein Unfolding
作者: Shiu, Ying-Jen
Jeng, U-Ser
Lin, Sheng-Hsien
應用化學系
應用化學系分子科學碩博班
Department of Applied Chemistry
Institute of Molecular science
關鍵字: cytochrome c;ising model;mean filed approximation;multi-group unfolding
公開日期: 2009
摘要: In the mean-field Ising model, the folding-unfolding behavior of a protein is regarded as an ensemble of units reduced from, presumably, peptide bonds or amino acid residues. Units of similar thermodynamic properties are further classified into groups that are related to, for instance, alpha-helices or beta-sheets. Units of the same group are assumed to unfold collectively, whereas those of different groups may undergo either sequential or coupled unfolding. The introduction of unfolding groups facilitates the description of non-collective local structural changes experimentally observed via a multi-group unfolding. We incorporate denaturants and temperature effects into the free energy expression of the protein upon dissolution in a specific environment at thermal equilibrium, and a model protein, cytochrome c, was examined. Results indicate that there are at least four unfolding groups induced unfolding of cytochrome c: two are related to the prosthetic heme group, whereas another two groups are a-helices and global nearly group, which largely account for global changes in protein morphology. The extracted thermodynamic parameters, on the basis of the Ising model, can closely predict unfolding behaviors of the proteins in compounded denaturing environments.
URI: http://hdl.handle.net/11536/15949
http://dx.doi.org/10.1002/masy.200950510
ISSN: 1022-1360
DOI: 10.1002/masy.200950510
期刊: MACROMOLECULAR SYMPOSIA
Volume: 279
起始頁: 63
結束頁: 64
Appears in Collections:Conferences Paper


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