Results 1 - 10 of 1,977

COEVOLVED RESIDUES AND THE FUNCTIONAL ASSOCIATION FOR INTRINSICALLY DISORDERED PROTEINS

by Chan-seok Jeong, Dongsup Kim
"... The evolution of intrinsically disordered proteins has been studied primarily by focusing on evolutionary changes at an individual position such as substitution and conservation, but the evolutionary association between disordered residues has not been comprehensively investigated. Here, we analyze ..."
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The evolution of intrinsically disordered proteins has been studied primarily by focusing on evolutionary changes at an individual position such as substitution and conservation, but the evolutionary association between disordered residues has not been comprehensively investigated. Here, we analyze

H (2006) Disordered domains and high surface charge confer hubs with the ability to interact with multiple proteins in interaction networks

by Ashwini Patil , Haruki Nakamura - FEBS Lett
"... Abstract We investigate the structural properties of hubs that enable them to interact with several partners in protein-protein interaction networks. We find that hubs have more observed and predicted disordered residues with fewer loops/coils, and more charged residues on the surface as compared t ..."
Abstract - Cited by 48 (3 self) - Add to MetaCart
Abstract We investigate the structural properties of hubs that enable them to interact with several partners in protein-protein interaction networks. We find that hubs have more observed and predicted disordered residues with fewer loops/coils, and more charged residues on the surface as compared

Predicting intrinsic disorder from amino acid sequence

by Zoran Obradovic, Kang Peng, Slobodan Vucetic, Predrag Radivojac, Celeste J. Brown, A. Keith Dunker - Proteins , 2003
"... ABSTRACT Blind predictions of intrinsic order and disorder were made on 42 proteins subsequently revealed to contain 9,044 ordered residues, 284 disordered residues in 26 segments of length 30 residues or less, and 281 disordered residues in 2 disordered segments of length greater than 30 residues. ..."
Abstract - Cited by 51 (14 self) - Add to MetaCart
ABSTRACT Blind predictions of intrinsic order and disorder were made on 42 proteins subsequently revealed to contain 9,044 ordered residues, 284 disordered residues in 26 segments of length 30 residues or less, and 281 disordered residues in 2 disordered segments of length greater than 30 residues

Molecular dynamics simulations of biomolecules,”

by Martin Karplus , J Andrew Mccammon - Nat Struct Biol, , 2002
"... It has been 25 years since the first molecular dynamics simulation of a macromolecule of biological interest was published 1 . The simulation concerned the bovine pancreatic trypsin inhibitor (BPTI), which has served as the 'hydrogen molecule' of protein dynamics because of its small size ..."
Abstract - Cited by 143 (3 self) - Add to MetaCart
mean-square fluctuations versus residue number (introduced in ref. 1) became a standard part of the analysis of high-resolution structures, even though the contribution to the B-factors from overall translation and rotation as well as crystal disorder continues to be a concern in their interpretation

Evaluation of disorder predictions in CASP5

by Eugene Melamud, John Moult - Suppl 6 , 2003
"... ABSTRACT This paper reports an analysis of the accuracy of predictions of structural disorder received as part of the CASP5 experiment. Six groups made predictions of disorder. The predictions of the fourmost active groups have been comparedwith the experimental results, in terms of the sensitivity ..."
Abstract - Cited by 1 (0 self) - Add to MetaCart
and specificity of themethods. All fourmethods succeed in detecting over half the disordered residues in the targets, with a generally low rate of over-prediction. Twoof themethods perform significantly betterwhen the structure of a related protein is available. There is a trade-off between the fraction

Residual disorder and diffusion in thin Heusler alloy films

by unknown authors , 2014
"... ar ..."
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Abstract not found

Library of disordered patterns in 3D protein structures

by Michail Yu. Lobanov, Eugeniya I. Furletova, Natalya S. Bogatyreva, Michail A. Roytberg, Oxana V - PLoS Comput. Biol , 2010
"... Intrinsically disordered regions serve as molecular recognition elements, which play an important role in the control of many cellular processes and signaling pathways. It is useful to be able to predict positions of disordered regions in protein chains. The statistical analysis of disordered residu ..."
Abstract - Cited by 3 (1 self) - Add to MetaCart
residues was done considering 34,464 unique protein chains taken from the PDB database. In this database, 4.95 % of residues are disordered (i.e. invisible in X-ray structures). The statistics were obtained separately for the N- and C-termini as well as for the central part of the protein chain. It has

Intrinsic disorder is a common feature of hub proteins from four eukaryotic interactomes. PLoS Comput Biol 2: e100

by Chad Haynes, Christopher J. Oldfield, Fei Ji, Niels Klitgord, Michael E. Cusick, Predrag Radivojac, Vladimir N. Uversky, Marc Vidal, Lilia M. Iakoucheva , 2006
"... Recent proteome-wide screening approaches have provided a wealth of information about interacting proteins in various organisms. To test for a potential association between protein connectivity and the amount of predicted structural disorder, the disorder propensities of proteins with various number ..."
Abstract - Cited by 52 (5 self) - Add to MetaCart
that interact with 10 partners, are significantly more disordered than end proteins, defined here as those that interact with just one partner. The proportion of predicted disordered residues, the average disorder score, and the number of predicted disordered regions of various lengths were higher overall

QuasiExperimentation

by Tanmay M, A Sampak Samanta, A Grant A. Broker, Cong-gui Zhao A, Edward R. T. Tiekink B , 1979
"... disorder in main residue; R factor = 0.049; wR factor = 0.117; data-to-parameter ratio = 16.1. ..."
Abstract - Cited by 77 (0 self) - Add to MetaCart
disorder in main residue; R factor = 0.049; wR factor = 0.117; data-to-parameter ratio = 16.1.

Inferring function using patterns of native disorder in proteins

by Anna Lobley, Mark B. Swindells, Christine A. Orengo, David T. Jones - PLoS Comput. Biol , 2007
"... Natively unstructured regions are a common feature of eukaryotic proteomes. Between 30 % and 60 % of proteins are predicted to contain long stretches of disordered residues, and not only have many of these regions been confirmed experimentally, but they have also been found to be essential for prote ..."
Abstract - Cited by 19 (0 self) - Add to MetaCart
Natively unstructured regions are a common feature of eukaryotic proteomes. Between 30 % and 60 % of proteins are predicted to contain long stretches of disordered residues, and not only have many of these regions been confirmed experimentally, but they have also been found to be essential
Results 1 - 10 of 1,977