title: Expanding the Range of Protein Function at the Far End of the Order-Structure Continuum.
abstract: The traditional view of the structure-function paradigm is that a protein's function is inextricably linked to a well defined, three-dimensional structure, which is determined by the protein's primary amino acid sequence. However, it is now accepted that a number of proteins do not adopt a unique tertiary structure in solution and that some degree of disorder is required for many proteins to perform their prescribed functions. In this review, we highlight how a number of protein functions are facilitated by intrinsic disorder and introduce a new protein structure taxonomy that is based on quantifiable metrics of a protein's disorder.
authors: From the Research Laboratory for Electronics, Department of Electrical Engineering & Computer Science, and.
authors: Virginia M
authors: VM
authors: Burger
authors: From the Research Laboratory for Electronics, Department of Electrical Engineering & Computer Science, and.
authors: Diego O
authors: DO
authors: Nolasco
authors: From the Research Laboratory for Electronics, Department of Electrical Engineering & Computer Science, and the Institute for Medical Engineering and Science, Massachusetts Institute of Technology, Cambridge, Massachusetts 02138 cmstultz@mit.edu.
authors: Collin M
authors: CM
authors: Stultz
mesh_terms: D000595:Amino Acid Sequence; D000596:Amino Acids / Q000737:chemistry* / Q000378:metabolism; D050882:CREB-Binding Protein / Q000737:chemistry* / Q000235:genetics / Q000378:metabolism; D003087:Colicins / Q000737:chemistry* / Q000235:genetics / Q000378:metabolism; D004926:Escherichia coli / Q000235:genetics / Q000378:metabolism; D039642:Eukaryotic Initiation Factors / Q000737:chemistry* / Q000235:genetics / Q000378:metabolism; D006801:Humans; D064267:Intrinsically Disordered Proteins / Q000737:chemistry* / Q000235:genetics / Q000378:metabolism; D011485:Protein Binding; D017510:Protein Folding; D054730:Protein Interaction Domains and Motifs; D017433:Protein Structure, Secondary; D013329:Structure-Activity Relationship; D013816:Thermodynamics
chemical_list: D000596:Amino Acids; D003087:Colicins; C104151:EIF4EBP2 protein, human; D039642:Eukaryotic Initiation Factors; D064267:Intrinsically Disordered Proteins; C488859:immE9 protein, E coli; D050882:CREB-Binding Protein; C494363:CREBBP protein, human
keywords: biophysics; conformational change; intrinsically disordered protein; protein folding; protein structure