scholarly article | Q13442814 |
P356 | DOI | 10.1007/S00249-008-0266-3 |
P2888 | exact match | https://scigraph.springernature.com/pub.10.1007/s00249-008-0266-3 |
P698 | PubMed publication ID | 18228014 |
P50 | author | Sebastian Busch | Q42280718 |
P2093 | author name string | W Doster | |
T Unruh | |||
A M Gaspar | |||
M-S Appavou | |||
P2860 | cites work | Coupled protein domain motion in Taq polymerase revealed by neutron spin-echo spectroscopy | Q24537466 |
Why are "natively unfolded" proteins unstructured under physiologic conditions? | Q29615739 | ||
Intrinsically unstructured proteins: re-assessing the protein structure-function paradigm | Q29615865 | ||
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 A | Q40346050 | ||
Structures and functionalities of milk proteins | Q41300711 | ||
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 cells | Q41822625 | ||
The secondary structure of milk proteins and their biological function | Q42608675 | ||
Average protein density is a molecular-weight-dependent function. | Q43104992 | ||
Molten globule structures in milk proteins: implications for potential new structure-function relationships | Q43956757 | ||
Association behavior of beta-casein | Q44324507 | ||
Pressure-induced dissociation of casein micelles: size distribution and effect of temperature | Q47372890 | ||
Solution structure of native proteins with irregular folds from Raman optical activity | Q73227985 | ||
A Raman optical activity study of rheomorphism in caseins, synucleins and tau. New insight into the structure and behaviour of natively unfolded proteins | Q77470256 | ||
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 models | Q77818141 | ||
The minimal structural requirement of concanavalin A that retains its functional aspects | Q80655740 | ||
P433 | issue | 5 | |
P304 | page(s) | 573-582 | |
P577 | publication date | 2008-01-29 | |
P1433 | published in | European Biophysics Journal | Q5412316 |
P1476 | title | Dynamics of well-folded and natively disordered proteins in solution: a time-of-flight neutron scattering study | |
P478 | volume | 37 |
Q38965660 | Dynamic footprint of sequestration in the molecular fluctuations of osteopontin |
Q35994848 | Dynamical Behavior of Human α-Synuclein Studied by Quasielastic Neutron Scattering |
Q36071932 | Dynamical coupling of intrinsically disordered proteins and their hydration water: comparison with folded soluble and membrane proteins |
Q34197530 | Expanding the proteome: disordered and alternatively folded proteins |
Q37265336 | From powder to solution: hydration dependence of human hemoglobin dynamics correlated to body temperature. |
Q83242647 | Internal motions of actin characterized by quasielastic neutron scattering |
Q42701154 | Macromolecular dynamics in red blood cells investigated using neutron spectroscopy |
Q52727763 | Microscopic diffusion processes measured in living planarians. |
Q36038114 | Order out of disorder: working cycle of an intrinsically unfolded chaperone. |
Q42918194 | Susceptibility of different proteins to flow-induced conformational changes monitored with Raman spectroscopy |
Q83459778 | The influence of 2 kbar pressure on the global and internal dynamics of human hemoglobin observed by quasielastic neutron scattering |
Q41917487 | Translational diffusion of hydration water correlates with functional motions in folded and intrinsically disordered proteins |
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