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1 SAXS analysis combined with molecular modeling simulatio
2 SAXS analysis indicates the ferrihydrite particles have
3 SAXS analysis of a truncated RcRE variant revealed an "A
4 SAXS and biochemical analyses demonstrated that the "A"
5 SAXS and H/D exchange data showed that global tertiary s
6 SAXS and mutational analyses further reveal that the pre
7 SAXS data are complemented by NMR measurements and poten
8 SAXS data show that the complex retains features of the
9 SAXS data suggest structural flexibility in EF hand doma
10 SAXS data suggested a global shape of a hollow elliptica
11 SAXS measurements on bulk crystalline samples reveal tha
12 SAXS measurements show that the reaction intermediate fo
13 SAXS performed on AMP-PNP-DnaA (H136Q) indicates that th
14 SAXS results indicated that surface-modified nanoparticl
15 SAXS revealed increases in the native state radius of gy
16 SAXS showed evidence of changes in betaG but not AX in t
17 SAXS shows that interbilayer spacing (D) in the cochleat
18 SAXS solution structures of SNX20 and SNX21 show that th
19 SAXS studies further show compaction of the protein upon
20 SAXS studies indicate that, on average, three worms are
21 SAXS was used to study the interactions between the prot
22 SAXS, NMR, and ESI MS differentiate beta-NaSn13 , Sn12 ,
25 S (Fast X-Ray Scattering) rapidly computes a SAXS profile of a given atomistic model and fits it to a
26 tains normal activation by VWF D4, and has a SAXS envelope consistent with amputation of the hairpin
29 ng-state and activated forms of C29S against SAXS data with available structural data created and eva
30 eotide steps and refining the models against SAXS data, a broad array of structures can be obtained t
37 the results from earlier electrochemical and SAXS studies stating that the closed conformation, where
38 uding TEM, AFM, high-resolution cryo-EM, and SAXS/WAXS measurements, reveals that the sheet and tube
40 e tested the recent suggestion that FRET and SAXS results can be reconciled if the R(g) and R(ee) are
47 sing the program X-PLOR-NIH based on NMR and SAXS restraints agree remarkably well; even the shapes o
48 solution structural information from NMR and SAXS suggests that the structures of the cold-induced an
49 roscopic (UV-vis, CD, fluorescence, NMR, and SAXS) and microscopic studies (TEM and AFM) showed that
50 2D proton nuclear magnetic resonance and SAXS data provided constraints on the solution structure
52 he bilayer spacings (as observed by SANS and SAXS) on the ratio between amount of water and amphiphil
56 ve apparent discrepancies between smFRET and SAXS inferences, we integrated SAXS data with NMR data a
57 and unlabeled polypeptides using smFRET and SAXS, we directly assessed the contributions of dyes to
59 y using it to direct autonomous small-angle (SAXS) and grazing-incidence small-angle (GISAXS) x-ray s
61 nt conformational changes of ectoIRR in both SAXS and AFM experiments, an observation that agreed wel
62 lustrate this self-consistency, we used both SAXS and FRET data in a Bayesian procedure to refine str
67 triking conformational change as observed by SAXS, implying that altering the hetero-domain interacti
70 strates the applicability of chromatographic SAXS when studying biomolecules predisposed to aggregati
71 irst demonstration of chromatography-coupled SAXS with Evolving Factor Analysis (EFA), a powerful met
72 By combination of X-ray crystallography, SAXS and EM, together with biochemical evidences, here w
73 d invite the application of time-resolved CV-SAXS to reveal interactions that result in efficient vir
74 t variation small-angle X-ray scattering (CV-SAXS) is a powerful tool with the potential to monitor t
75 ted MS2 RNA was exclusively detected with CV-SAXS and compared with a structure derived from asymmetr
77 ely agree with the experimentally determined SAXS curves supporting the view that liraglutide forms h
78 ts indicate that as aids in tissue diagnosis SAXS is capable of distinguishing areas of invasion by d
80 s, excellent agreement with the experimental SAXS data, and a large-scale rearrangement of the signal
82 was investigated by static and stopped-flow SAXS measurements, revealing dynamic structural changes
84 le Forster resonance energy transfer (FRET), SAXS, dynamic light scattering (DLS), and two-focus fluo
85 data, such as several NMR observables, FRET, SAXS and cryo-electron microscopy data, and enables mode
87 (R(g)) and end-to-end distance (R(ee)) from SAXS profiles, we tested the recent suggestion that FRET
89 l uncertainties of the Rg data measured from SAXS experiments, which suggest no compaction, leading t
92 en smFRET and SAXS inferences, we integrated SAXS data with NMR data and reserved the smFRET data for
97 g partner protein Brn1(Cnd2) The analysis of SAXS and dynamic and static multiangle light scattering
99 are addressed, as well as the combination of SAXS with other X-ray and non-X-ray characterization too
103 studied several back-calculation software of SAXS scattering intensity and optimized the adjustable p
111 ll and wide-angle X-ray scattering patterns (SAXS/WAXS) over 10 decades of time spanning from 100 ps
113 teractions are sufficient to reconcile prior SAXS and FRET studies, thus providing a unified picture
115 w is synchronized with synchrotron radiation SAXS measurements to probe protein interactions while mi
119 n at small angles and in situ rheology (rheo-SAXS) experiments using the high X-ray flux of a synchro
121 roscopy, small-angle X-ray light scattering (SAXS), and molecular dynamics simulations, we provide he
122 hese proteins, small-angle X-ray scattering (SAXS) allows for a quantitative assessment and modeling
124 llographic and small-angle X-ray scattering (SAXS) analyses indicate that lattice symmetries and dime
125 (cryo-EM) and small-angle X-ray scattering (SAXS) analyses of recombinant disulfide-linked dimeric M
133 combined with small angle X-ray scattering (SAXS) and confocal laser scanning microscopy (CLSM) stud
134 We determined small-angle X-ray scattering (SAXS) and crystal structures of the main ERQC enzyme, ER
136 s detailed via small-angle X-ray scattering (SAXS) and electrospray ionization mass spectrometry (ESI
137 in solution by small-angle X-ray scattering (SAXS) and exploited the scattering profile in modeling o
138 combination of small-angle X-ray scattering (SAXS) and high throughput, droplet based microfluidics a
139 solution-based small-angle x-ray scattering (SAXS) and molecular constrained data modeling, we show t
140 s suggested by small-angle x-ray scattering (SAXS) and multiangle static light scattering (MALS) resu
142 reparation for Small-Angle X-Ray Scattering (SAXS) and Small-Angle Neutron Scattering (SANS) characte
143 as verified by Small angle X-ray scattering (SAXS) and Transmission electron microscopy (TEM) and hol
144 combined with small-angle X-ray scattering (SAXS) and viscosity measurements for three proteins, alp
149 agments to the small angle X-ray scattering (SAXS) data revealed that the protein's C-terminal domain
150 MR spectra and small-angle X-ray scattering (SAXS) data show that this beta-strand-rich conformation
152 we use NMR and small-angle x-ray scattering (SAXS) data with multiple molecular dynamics (MD) simulat
156 fer (FRET) and small-angle X-ray scattering (SAXS) experiments disagree on whether Protein L collapse
158 microscopy and small-angle X-ray scattering (SAXS) experiments reveal the formation of four classes o
159 ation curve in small-angle X-ray scattering (SAXS) experiments using isolated GluA2 ligand-binding do
161 (XPCS) in the small-angle X-ray scattering (SAXS) geometry to probe both the structural and dynamica
163 studies using small-angle X-ray scattering (SAXS) have reported no such increase of the radius of gy
171 llography, and small-angle X-ray scattering (SAXS) methodologies to demonstrate that adenine/guanine
172 FRET data with small-angle X-ray scattering (SAXS) models and published crystal structures of isolate
175 procedure for small-angle X-ray scattering (SAXS) profiles and used it to demonstrate that even rela
176 low-resolution small angle X-ray scattering (SAXS) results show that the N-terminal extensions protru
181 he crystal and small-angle X-ray scattering (SAXS) structures of Bcl-xL treated with the mild deterge
182 Mutational and small-angle X-ray scattering (SAXS) studies confirm the structural similarities of TAP
185 -based in-situ small angle X-ray scattering (SAXS) suggests that the sizes of the two samples and the
186 roteolysis and small-angle X-ray scattering (SAXS) support the proper folding of both the 14-3-3 and
187 ng synchrotron small angle x-ray scattering (SAXS) techniques, determining nanometer scale structural
188 demonstrate by small-angle X-ray scattering (SAXS) that HMBPP binding to the internal domain of BTN3A
190 mbination with small angle X-ray scattering (SAXS) to determine the structure of the main immunoreact
191 llography with small angle x-ray scattering (SAXS) to elucidate the structure of the plakin domain of
192 Here, we used Small Angle X-ray Scattering (SAXS) to investigate oligomerization of DnaA in solution
194 We combine small angle X-ray scattering (SAXS) with ensemble-optimization methods (EOM) to dynami
197 combined with small-angle X-ray scattering (SAXS), also allowed us to predict the general position o
199 on scattering, small-angle X-ray scattering (SAXS), and Forster resonance energy transfer (FRET), we
201 roscopy (NMR), small-angle X-ray scattering (SAXS), and single-molecule Forster resonance energy tran
202 spectroscopy, Small-angle X-ray Scattering (SAXS), and single-molecule Forster Resonance Energy Tran
203 time-resolved small angle X-ray scattering (SAXS), and time-resolved negative stain electron microsc
204 combination of small-angle x-ray scattering (SAXS), atomistic molecular dynamic simulations, single-m
205 iques, such as small-angle X-ray scattering (SAXS), can be applied at larger scale, but they miss ato
206 combination of small-angle X-ray scattering (SAXS), computational studies, mutagenesis and microbial
208 asurements and small-angle X-ray scattering (SAXS), coupled with biochemical and functional analyses
210 e strengths of small-angle X-ray scattering (SAXS), crystallography, and cryo-electron microscopy (cr
211 ility by using small-angle X-ray scattering (SAXS), dynamic light scattering (DLS), and NMR relaxatio
215 so revealed by small-angle X-ray scattering (SAXS), especially the closed pore effects on lithium-ion
216 combination of small angle X-ray scattering (SAXS), low-pressure N2 and CO2 adsorption (LPGA) and hig
217 ned X-ray crystallography, X-ray scattering (SAXS), modeling and biophysical approaches, with in vivo
218 entrifugation, small-angle X-ray scattering (SAXS), molecular dynamics (MD) simulations, and ligand-b
219 e described by small-angle X-ray scattering (SAXS), pair distribution function (PDF), and electrospra
220 modeling with small-angle X-ray scattering (SAXS), pair distribution function (PDF), and X-ray powde
221 using combined small angle X-ray scattering (SAXS), small angle neutron scattering (SANS) and low-pre
222 hermore, using small-angle X-ray scattering (SAXS), the positions of the flanking acyl carrier protei
223 try (ITC), and small angle x-ray scattering (SAXS), we dissect binding and catalysis on multiple phos
225 ing assays and small-angle X-ray scattering (SAXS), we find that the SVM metric sigma correlates not
226 utagenesis and small-angle X-ray scattering (SAXS), we show that these states involve aromatic residu
227 ansfer (FRET), small-angle x-ray scattering (SAXS), x-ray crystallography, electron microscopy, and t
228 combination of small angle X-ray scattering (SAXS), X-ray hydroxyl radical footprinting, circular dic
229 of Pcore with small angle x-ray scattering (SAXS)-based ensemble modeling of the full-length P prote
245 of small- and wide- angle X-ray scattering (SAXS/WAXS) during in situ repeated tensile loading to el
246 situ small- and wide-angle X-ray scattering (SAXS/WAXS), atomic force and cryogenic transmission elec
248 upled with small-angle X-ray scattering (SEC-SAXS) analysis, we investigated the ACMSD tetramer struc
249 coupled to small-angle X-ray scattering (SEC-SAXS) of this hybrid module bound to 1D10 provided furth
250 line with small-angle X-ray scattering (SEC-SAXS) to analyze the full-length hPAH solution structure
251 tially regulates ACMSD activity and that SEC-SAXS coupled with X-ray crystallography is a powerful to
252 udy the phase separation process via in situ SAXS experiments as well as ex situ electron microscopy,
254 However, conducting the analogous in situ SAXS studies during RAFT aqueous emulsion polymerization
257 hy, nuclear magnetic resonance spectroscopy, SAXS and molecular dynamics calculations, we show that t
258 endent of age, disease and treatment status, SAXS revealed reduced fibril plasticity at high strain r
261 rties on the hydration shell by a systematic SAXS/SANS study using three mutants of a single protein,
262 Biophysical evidence from TEM, cryo-TEM, SAXS, AFM, and STEM measurements on the 3FD-IL nanosheet
271 ess favorable lens shape required to fit the SAXS data from the N-terminal truncated nanodisc system
272 In a cutting-edge approach, we fitted the SAXS data to full MD simulations from the same condition
273 he ACMSD tetramer structure, and fitting the SAXS data with X-ray crystal structures of the monomeric
276 the dynamics in momentum space, which in the SAXS geometry reflects structural relaxation on the nano
278 gh-resolution KIX domain structures into the SAXS-derived envelopes suggested that the G-region emerg
281 model provides satisfactory data fits to the SAXS patterns and allows the mean silica volume fraction
292 ort factor RanBP5 that can be modelled using SAXS and we show that the PA-PB1-RanPB5 complex is no lo
294 mbranes are produced for x = 200-1000, while SAXS indicates a gradual reduction in mean aggregation n
295 h four had a size median below 100 nm, while SAXS showed a size median below 100 nm for six evaluated
297 t protein liquid chromatography coupled with SAXS minimized data artifacts caused by a non-monodisper
299 mic-scale characterization techniques (XAFS, SAXS, XRF, and electron microscopy) to follow the proces