Natively unfolded proteins: A point where biology waits for physics

By Vladimir N Uversky. Protein Science, 2002

1,773 citations recorded by the source corpus.

Subfields: Materials Chemistry, Molecular Biology

View Paper: https://www.semanticscholar.org/paper/31429fdedd10844e95dc6de1945b6ef72b2441da

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Citations in the corpus

DisProt: the Database of Disordered Proteins (2006, background): “One more extended disordered conformation, the pre-molten globule state, was added to complete the ‘The Protein Quartet’ model ( 26 ).”
Intrinsically unstructured proteins and their functions (2005, background): “jpg" NDATA ITEM> ]> The occurrence of unstructured regions of significant size (>50 residues) is surprisingly common in functional protein”
Improved Disorder Prediction by Combination of Orthogonal Approaches (2009, methodology): “Thus, there is no single gold standard for order/disorder assignment; instead, we need to use several experimental methods in concert [5,12,13,14,15,16,17].”
CIDER: Resources to Analyze Sequence-Ensemble Relationships of Intrinsically Disordered Proteins (2017, background): “Amino acid compositions of IDPs play central roles in determining their conformational properties (7,11– 16, 28, 31 ). localCIDER enables rapid, proteome-wide proteome-wide investigations of compositional biases and the evolutionary preferences within IDPs.”
Protein flexibility and intrinsic disorder (2004, background): “Given the strong association of disorder with function (Dunker et al. 2002a), disordered proteins are becoming the subject of increased interest (Wright and Dyson 1999; Dunker et al. 2002a; Dyson and Wright 2002; Uversky 2002b).”
The interplay between structure and function in intrinsically unstructured proteins (2005, background): “shown to fall into coil-like and a premolten-globule-like classes, with significant residual structure in the latter [8].”
Sampling bottlenecks in de novo protein structure prediction (2009, neutral): “(a) Correlation between the Rh values for CTPRs of different lengths (CTPR2, CTPR3, CTPR4, CTPR6, CTPR8, and CTPR20) measured by FCS and the Rh values calculated from the crystal structures of the CTPRs using the program Hydropro,20 (filled circles) or the Rh values calculated using a model that des”
Flexible-meccano: a tool for the generation of explicit ensemble descriptions of intrinsically disordered proteins and their associated experimental observables (2012, background): “disordered in their from https://academic.oup.com/bioinformatics/article-abstract/28/11/1463/ functional state has revolutionized our understanding of structural and molecular biology (Babu, 2012; Uversky, 2002).”
Assessing protein disorder and induced folding (2005, background): “temperature-induced formation of secondary structure.(3,16,42) This was observed for such natively disordered proteins as -synuclein,(86) phosphodiesterase -subunit,(87) 636–771 fragment of caldesmon,(20) extracellular domain of the nerve growth factor receptor,(88) and -casein.”
Comprehensive comparative assessment of in-silico predictors of disordered regions. (2012, background): “, partially folded or molten/pre-molten globule-like, domains with poorly packed side chains [[2],[3]].”
Analysis of molecular recognition features (MoRFs). (2006, background): “20 12, 16, 19 Protein phosphorylation represents an important regulatory regulatory mechanism in”
Conformational constraints for amyloid fibrillation: the importance of being unfolded. (2004, background): “[11] for a list of these proteins) may easily form fibrils.”
Natural protein sequences are more intrinsically disordered than random sequences (2016, background): “It should be noted, however, that SPINE-D [26] likely over-predicts structured regions because it cannot distinguish proteins in molten globule states (compact with some secondary structures [30]) from proteins in unique three-dimensional structures.”
Intrinsically Disordered Proteins and Their “Mysterious” (Meta)Physics (2019, background): “From a physical viewpoint, the lack of compact structure in a protein with low hydrophobicity and high net charge makes perfect sense, since strong charge-charge repulsion in such a polypeptide is not compensated by strong enough hydrophobic attraction [4, 35, 40, 63, 64].”
Intrinsically disordered proteins and structured proteins with intrinsically disordered regions have different functional roles in the cell (2019, background): “In 88 this context, the lack of a well-defined 3D-structure represents a major functional advantage for 89 IDPs, allowing them to interact with a broad range of substrates with relatively high-specificity and 90 low-affinity, often undergoing a disorder-to-order transition upon binding [2,8,26,37,38”