The protein folding transition state: insights from kinetics and thermodynamics

Rui D M Travasso1, Patrícia F N Faísca, Antonio Rey

  • 1Departamento de Física, Centro de Física Computacional, Universidade de Coimbra, Coimbra 3004-516, Portugal. rui@lca.uc.pt

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The native conformation of a protein is formed by interactions between the side chains of its constituent amino acids. When the amino acids cannot form these interactions, the protein cannot fold by itself and needs chaperones. Notably, chaperones do not relay any additional information required for the folding of polypeptides; the native conformation of a protein is determined solely by its amino acid sequence. Chaperones catalyze protein folding without being a part of the folded protein.
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