title: Residual structure in unfolded proteins.
abstract: The denatured state ensemble (DSE) of unfolded proteins, once considered to be well-modeled by an energetically featureless random coil, is now well-known to contain flickering elements of residual structure. The position and nature of DSE residual structure may provide clues toward deciphering the protein folding code. This review focuses on recent advances in our understanding of the nature of DSE collapse under folding conditions, the quantification of the stability of residual structure in the DSE, the determination of the location and types of residues involved in thermodynamically significant residual structure and advances in detection of long-range interactions in the DSE.
authors: Department of Chemistry and Biochemistry and Center for Biomolecular Structure and Dynamics, The University of Montana, Missoula, MT 59812, USA. bruce.bowler@umontana.edu
authors: Bruce E
authors: BE
authors: Bowler
mesh_terms: D006801:Humans; D010455:Peptides / Q000737:chemistry; D011489:Protein Denaturation; D017510:Protein Folding; D011506:Proteins / Q000737:chemistry* / Q000378:metabolism; D012997:Solvents; D013816:Thermodynamics
chemical_list: D010455:Peptides; D011506:Proteins; D012997:Solvents