Dynamics of well-folded and natively disordered proteins in solution: a time-of-flight neutron scattering study

scientific article published on 29 January 2008

Dynamics of well-folded and natively disordered proteins in solution: a time-of-flight neutron scattering study is …
instance of (P31):
scholarly articleQ13442814

External links are
P356DOI10.1007/S00249-008-0266-3
P2888exact matchhttps://scigraph.springernature.com/pub.10.1007/s00249-008-0266-3
P698PubMed publication ID18228014

P50authorSebastian BuschQ42280718
P2093author name stringW Doster
T Unruh
A M Gaspar
M-S Appavou
P2860cites workCoupled protein domain motion in Taq polymerase revealed by neutron spin-echo spectroscopyQ24537466
Why are "natively unfolded" proteins unstructured under physiologic conditions?Q29615739
Intrinsically unstructured proteins: re-assessing the protein structure-function paradigmQ29615865
Evolution of the internal dynamics of two globular proteins from dry powder to solution.Q30322770
Protein-water displacement distributions.Q30350718
What does it mean to be natively unfolded?Q34488954
Hydrodynamic changes accompanying the loss of metal ions from concanavalin AQ40346050
Structures and functionalities of milk proteinsQ41300711
Effects of the environmental factors on the casein micelle structure studied by cryo transmission electron microscopy and small-angle x-ray scattering/ultrasmall-angle x-ray scattering.Q41625015
Microscopic diffusion and hydrodynamic interactions of hemoglobin in red blood cellsQ41822625
The secondary structure of milk proteins and their biological functionQ42608675
Average protein density is a molecular-weight-dependent function.Q43104992
Molten globule structures in milk proteins: implications for potential new structure-function relationshipsQ43956757
Association behavior of beta-caseinQ44324507
Pressure-induced dissociation of casein micelles: size distribution and effect of temperatureQ47372890
Solution structure of native proteins with irregular folds from Raman optical activityQ73227985
A Raman optical activity study of rheomorphism in caseins, synucleins and tau. New insight into the structure and behaviour of natively unfolded proteinsQ77470256
Effect of self-association of alphas1-casein and its cleavage fractions alphas1-casein(136-196) and alphas1-casein(1-197),1 on aromatic circular dichroic spectra: comparison with predicted modelsQ77818141
The minimal structural requirement of concanavalin A that retains its functional aspectsQ80655740
P433issue5
P304page(s)573-582
P577publication date2008-01-29
P1433published inEuropean Biophysics JournalQ5412316
P1476titleDynamics of well-folded and natively disordered proteins in solution: a time-of-flight neutron scattering study
P478volume37

Reverse relations

cites work (P2860)
Q38965660Dynamic footprint of sequestration in the molecular fluctuations of osteopontin
Q35994848Dynamical Behavior of Human α-Synuclein Studied by Quasielastic Neutron Scattering
Q36071932Dynamical coupling of intrinsically disordered proteins and their hydration water: comparison with folded soluble and membrane proteins
Q34197530Expanding the proteome: disordered and alternatively folded proteins
Q37265336From powder to solution: hydration dependence of human hemoglobin dynamics correlated to body temperature.
Q83242647Internal motions of actin characterized by quasielastic neutron scattering
Q42701154Macromolecular dynamics in red blood cells investigated using neutron spectroscopy
Q52727763Microscopic diffusion processes measured in living planarians.
Q36038114Order out of disorder: working cycle of an intrinsically unfolded chaperone.
Q42918194Susceptibility of different proteins to flow-induced conformational changes monitored with Raman spectroscopy
Q83459778The influence of 2 kbar pressure on the global and internal dynamics of human hemoglobin observed by quasielastic neutron scattering
Q41917487Translational diffusion of hydration water correlates with functional motions in folded and intrinsically disordered proteins

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