2007/12/12 by L. Cruzeiro-Hansson, Cruzeiro, Leonor
Biochemistry, Genetics and Molecular Biology · Materials Science · #Biological Physics (physics.bio-ph) #Enzyme Structure and Function #FOS: Physical sciences #Protein Structure and Dynamics #RNA and protein synthesis mechanisms
paper · pdf · doi:10.48550/arxiv.0712.2034
openalex publication_date 2007/12/12 · openalex created_date 2025/10/10 · openalex updated_date 2026/07/28
An all-atom model of proteins is used to show that the same sequence of amino acids can have many alternative structures, that are very distant from, and that can be as stable as, the corresponding native structure. Such alternative structures are not easily rationalized as belonging to the native basin and indicate instead that the free energy landscape of proteins is multi-funnel-shaped and that Anfinsen's thermodynamic hypothesis alone cannot explain protein folding. An alternative two-step process for folding is proposed and its consistency with the experimental evidence available is discussed.