Intrinsically unstructured proteins.
The recent suggestion that the classical structure-function paradigm should be extended to proteins and protein domains whose native and functional state is intrinsically unstructured has received a great deal of support. There is ample evidence that the unstructured state, common to all living organisms, is essential for basic cellular functions; thus it deserves to be recognized as a separate functional and structural category within the protein kingdom. In this review, recent findings are surveyed to illustrate that this novel but rapidly advancing field has reached a point where these proteins can be comprehensively classified on the basis of structure and function.
D000595:Amino Acid Sequence; D000596:Amino Acids / Q000737:chemistry; D019277:Entropy; D057927:Hydrophobic and Hydrophilic Interactions; D008958:Models, Molecular; D011485:Protein Binding; D011487:Protein Conformation; D011489:Protein Denaturation; D017510:Protein Folding; D011506:Proteins / Q000737:chemistry* / Q000145:classification* / Q000378:metabolism; D055672:Static Electricity; D013329:Structure-Activity Relationship
D000596:Amino Acids; D011506:Proteins