title: A novel procedure for identification of the folding/unfolding patterns of dimeric proteins.
abstract: The unfolding of proteins has been widely used for investigating the thermodynamic properties of monomeric proteins but has been used infrequently for dimeric (or oligomeric) proteins, because of the inherent cooperation of denaturation and dissociation of the dimers (oligomers). Here, we introduce a thermodynamic parameter K(obs) to discriminate the diverse folding patterns of dimeric proteins. K(obs) remains constant as the protein concentration increases for the true one-step curve of unfolding pattern (A), increases and reaches a plateau for one-step curves with monomeric intermediate pattern (B), and increases steadily with no plateau for one-step curves with dimeric intermediate pattern (C).
authors.affiliation: The Key Laboratory of Bioinformatics, Ministry of Education, Department of Biological Sciences and Biotechnology, Tsinghua University, Beijing 100084, China.
authors.forename: Yun
authors.initials: Y
authors.lastname: He
authors.forename: Sanbo
authors.initials: S
authors.lastname: Qin
authors.forename: Xian-Ming
authors.initials: XM
authors.lastname: Pan
mesh_terms: D019281:Dimerization; D008956:Models, Chemical; D011489:Protein Denaturation; D017510:Protein Folding; D011506:Proteins / Q000032:analysis; D013816:Thermodynamics
chemical_list: D011506:Proteins