title: The native-state ensemble of proteins provides clues for folding, misfolding and function.
abstract: The predominant equilibrium in proteins is not between native and unfolded states, it is between the native and multiple partially unfolded forms. Some of these partially unfolded forms can be energetically close to the native state and, therefore, have the potential to become appreciably populated. This could have an important role in protein function or misfolding diseases. The recent identification and characterization of the partially unfolded forms of apoflavodoxin furthers our understanding of their formation.
authors.affiliation: Department of Biochemistry and BIFI, University of Zaragoza, Zaragoza 50009, Spain.
authors.forename: Nunilo
authors.initials: N
authors.lastname: Cremades
authors.forename: Javier
authors.initials: J
authors.lastname: Sancho
authors.forename: Ernesto
authors.initials: E
authors.lastname: Freire
mesh_terms: D001059:Apoproteins / Q000737:chemistry* / Q000502:physiology; D016948:Azotobacter vinelandii / Q000737:chemistry; D005418:Flavodoxin / Q000737:chemistry*; D008958:Models, Molecular; D011487:Protein Conformation; D017510:Protein Folding; D013816:Thermodynamics
chemical_list: D001059:Apoproteins; D005418:Flavodoxin; C026932:apoflavodoxin