Intrinsically disordered proteins and their environment: effects of strong denaturants, temperature, pH, counter ions, membranes, binding partners, osmolytes, and macromolecular crowding.
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Systematic analysis of compositional order of proteins reveals new characteristics of biological functions and a universal correlate of macroevolutionStructure and expression of a novel compact myelin protein - small VCP-interacting protein (SVIP)NS3 protease from hepatitis C virus: biophysical studies on an intrinsically disordered protein domainSolution structure of Rv2377c-founding member of the MbtH-like protein familyThe influence of chemical chaperones on enzymatic activity under thermal and chemical stresses: common features and variation among diverse chemical familiesIntrinsically disordered and pliable Starmaker-like protein from medaka (Oryzias latipes) controls the formation of calcium carbonate crystalsBiophysical properties of intrinsically disordered p130Cas substrate domain--implication in mechanosensingA decade and a half of protein intrinsic disorder: biology still waits for physicsAdvantages of proteins being disordered.A group 6 late embryogenesis abundant protein from common bean is a disordered protein with extended helical structure and oligomer-forming properties.Understanding protein non-folding.Involvement of C-Terminal Histidines in Soybean PM1 Protein Oligomerization and Cu2+ Binding.High-throughput characterization of intrinsic disorder in proteins from the Protein Structure Initiative.Thermostability in endoglucanases is fold-specificBioinformatics analysis of disordered proteins in prokaryotes.Multi-scaled explorations of binding-induced folding of intrinsically disordered protein inhibitor IA3 to its target enzyme.The relationship between folding and activity in UreG, an intrinsically disordered enzyme.The protein kingdom extended: ordered and intrinsically disordered proteins, their folding, supramolecular complex formation, and aggregation.From the Cover: Charge interactions can dominate the dimensions of intrinsically disordered proteins.Expanding the proteome: disordered and alternatively folded proteins.Calcium-induced folding and stabilization of the intrinsically disordered RTX domain of the CyaA toxinPerturbed amelogenin secondary structure leads to uncontrolled aggregation in amelogenesis imperfecta mutant proteins.Effects of molecular crowding on the dynamics of intrinsically disordered proteins.Disorder in cholesterol-binding functionality of CRAC peptides: a molecular dynamics study.A multi-pronged search for a common structural motif in the secretion signal of Salmonella enterica serovar Typhimurium type III effector proteins.Targeting intrinsically disordered proteins in neurodegenerative and protein dysfunction diseases: another illustration of the D(2) concept.Intrinsic Disorder of the C-Terminal Domain of Drosophila Methoprene-Tolerant Protein.Nucleocytoplasmic transport: a role for nonspecific competition in karyopherin-nucleoporin interactionsThe molecular mechanism of nuclear transport revealed by atomic-scale measurements.Identification of minimally interacting modules in an intrinsically disordered protein.Restored mutant receptor:Corticoid binding in chaperone complexes by trimethylamine N-oxideProtein Composition Determines the Effect of Crowding on the Properties of Disordered Proteins.Cyclic N-terminal loop of amylin forms non amyloid fibers.Deducing conformational variability of intrinsically disordered proteins from infrared spectroscopy with Bayesian statistics.The mysterious unfoldome: structureless, underappreciated, yet vital part of any given proteome.Single-molecule spectroscopy reveals polymer effects of disordered proteins in crowded environments.Cell volume homeostatic mechanisms: effectors and signalling pathways.Amyloid structure--one but not the same: the many levels of fibrillar polymorphism.Novel strategies for drug discovery based on Intrinsically Disordered Proteins (IDPs)From water and ions to crowded biomacromolecules: in vivo structuring of a prokaryotic cell.
P2860
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P2860
Intrinsically disordered proteins and their environment: effects of strong denaturants, temperature, pH, counter ions, membranes, binding partners, osmolytes, and macromolecular crowding.
description
article científic
@ca
article scientifique
@fr
articolo scientifico
@it
artigo científico
@pt
bilimsel makale
@tr
scientific article published on October 2009
@en
vedecký článok
@sk
vetenskaplig artikel
@sv
videnskabelig artikel
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vědecký článek
@cs
name
Intrinsically disordered prote ...... , and macromolecular crowding.
@en
Intrinsically disordered prote ...... , and macromolecular crowding.
@nl
type
label
Intrinsically disordered prote ...... , and macromolecular crowding.
@en
Intrinsically disordered prote ...... , and macromolecular crowding.
@nl
prefLabel
Intrinsically disordered prote ...... , and macromolecular crowding.
@en
Intrinsically disordered prote ...... , and macromolecular crowding.
@nl
P2860
P1433
P1476
Intrinsically disordered prote ...... , and macromolecular crowding.
@en
P2860
P2888
P304
P356
10.1007/S10930-009-9201-4
P577
2009-10-01T00:00:00Z