scholarly journals X-ray-scattering of turkey skeletal-muscle troponin C in solution at low pH

1989 ◽  
Vol 261 (3) ◽  
pp. 1043-1046 ◽  
Author(s):  
E J Wachtel ◽  
T Sverbilova ◽  
W D McCubbin ◽  
C M Kay
Keyword(s):  
Skeletal Muscle ◽  
Small Angle ◽  
Solution Structure ◽  
Low Ph ◽  
Troponin C ◽  
Radius Of Gyration ◽  
Maximum Dimension ◽  
X Ray ◽  
X Ray Scattering ◽  
Ray Scattering

The solution structure of troponin C from turkey skeletal muscle was studied at low pH by small-angle X-ray-scattering. We find that troponin C at pH 5.3 in the presence of Mg2+ has a triaxial radius of gyration and maximum dimension comparable with those of the crystallized protein. However, the relative disposition of domains is more similar to that found for the highly homologous rabbit protein in solution at pH 7.4.

Calcium-induced increase in the radius of gyration and maximum dimension of calmodulin measured by small-angle x-ray scattering

Biochemistry ◽  
1985 ◽  
Vol 24 (24) ◽  
pp. 6740-6743 ◽  
Author(s):  
B. A. Seaton ◽  
J. F. Head ◽  
D. M. Engelman ◽  
F. M. Richards
Keyword(s):  
Small Angle ◽  
Radius Of Gyration ◽  
Maximum Dimension ◽  
X Ray ◽  
X Ray Scattering ◽  
Ray Scattering

Solution Structure of the Chicken Skeletal Muscle Troponin Complex Via Small-angle Neutron and X-ray Scattering

2005 ◽  
Vol 345 (4) ◽  
pp. 797-815 ◽  
Author(s):  
William A. King ◽  
Deborah B. Stone ◽  
Peter A. Timmins ◽  
Theyencheri Narayanan ◽  
Alex A.M. von Brasch ◽  
...  
Keyword(s):  
Skeletal Muscle ◽  
Small Angle ◽  
Solution Structure ◽  
X Ray ◽  
X Ray Scattering ◽  
Troponin Complex ◽  
Chicken Skeletal Muscle ◽  
Ray Scattering

scholarly journals Small-Angle X-Ray Scattering Analysis of the Bifunctional Antibiotic Resistance Enzyme Aminoglycoside (6′) Acetyltransferase-Ie/Aminoglycoside (2″) Phosphotransferase-Ia Reveals a Rigid Solution Structure

2012 ◽  
Vol 56 (4) ◽  
pp. 1899-1906 ◽  
Author(s):  
Shane J. Caldwell ◽  
Albert M. Berghuis
Keyword(s):  
Small Angle ◽  
Active Sites ◽  
Solution Structure ◽  
Coenzyme A ◽  
Radius Of Gyration ◽  
Bifunctional Enzyme ◽  
X Ray ◽  
X Ray Scattering ◽  
The Impact ◽  
Ray Scattering

ABSTRACTAminoglycoside (6′) acetyltransferase-Ie/aminoglycoside (2″) phosphotransferase-Ia [AAC(6′)-Ie/APH(2″)-Ia] is one of the most problematic aminoglycoside resistance factors in clinical pathogens, conferring resistance to almost every aminoglycoside antibiotic available to modern medicine. Despite 3 decades of research, our understanding of the structure of this bifunctional enzyme remains limited. We used small-angle X-ray scattering (SAXS) to model the structure of this bifunctional enzyme in solution and to study the impact of substrate binding on the enzyme. It was observed that the enzyme adopts a rigid conformation in solution, where the N-terminal AAC domain is fixed to the C-terminal APH domain and not loosely tethered. The addition of acetyl-coenzyme A, coenzyme A, GDP, guanosine 5′-[β,γ-imido]triphosphate (GMPPNP), and combinations thereof to the protein resulted in only modest changes to the radius of gyration (RG) of the enzyme, which were not consistent with any large changes in enzyme structure upon binding. These results imply some selective advantage to the bifunctional enzyme beyond coexpression as a single polypeptide, likely linked to an improvement in enzymatic properties. We propose that the rigid structure contributes to improved electrostatic steering of aminoglycoside substrates toward the two active sites, which may provide such an advantage.

scholarly journals A model of the solution structure of human Pex5p obtained by small angle X-ray scattering

2006 ◽  
Vol 62 (a1) ◽  
pp. s264-s264
Author(s):  
K. Shiozawa ◽  
P. Konarev ◽  
C. Neufeld ◽  
W. A. Stanley ◽  
M. Wilmanns ◽  
...  
Keyword(s):  
Small Angle ◽  
Solution Structure ◽  
X Ray ◽  
X Ray Scattering ◽  
Ray Scattering

ULTRA SMALL-ANGLE X-RAY SCATTERING STUDY OF FLOCCULATION IN SILICA-FILLED RUBBER

2014 ◽  
Vol 87 (2) ◽  
pp. 348-359 ◽  
Author(s):  
Satoshi Mihara ◽  
Rabin N. Datta ◽  
Wilma K. Dierkes ◽  
Jacques W. M. Noordermeer ◽  
Naoya Amino ◽  
...  
Keyword(s):  
Fractal Dimension ◽  
Small Angle ◽  
Radius Of Gyration ◽  
X Ray ◽  
X Ray Scattering ◽  
Mass Fractal ◽  
Mass Fractal Dimension ◽  
Lower Mobility ◽  
Low Mass ◽  
Ray Scattering

ABSTRACT The flocculation of silica during vulcanization is monitored using the ultra small-angle X-ray scattering technique for two different types of silica: a highly dispersible silica (HD) and a conventional silica (CV), mixed into a blend of S-SBR and BR rubbers. The cutoff length of the silica aggregate Rss and the mass fractal dimension Dm, which indicate the degree of flocculation of aggregates, are estimated according to the modified unified equation. The aggregate radius Ra is estimated to be related to the lower cutoff length Rss, indicating the radius of gyration of the mass-fractal structure. For both silicas, Ra increases during vulcanization. For the CV silica, an increase of Dm is observed, whereas no significant increase of Dm can be seen for the HD silica. The Ra of CV is relatively high compared with that of HD. On the other hand, the CV silica shows a relatively lower Dm compared with that of HD. These results indicate that CV has a larger size of aggregates and lower degree of agglomeration of its aggregates. The presence of di(tri-ethoxy-silyl-propyl)tetrasulfide (TESPT) as coupling agent between the silica and rubber decreases the aggregate radius of silica. However, in the absence of TESPT, a low mass-fractal dimension, which means a low degree of agglomeration of aggregates, is observed. This results from a lower mobility of silica aggregates, depending on the size of the aggregates. The silica loading also has an influence on the flocculation process. The aggregate radius increases as the silica loading is increased. At the same time, a higher mass-fractal dimension, and therefore also a higher degree of agglomeration, can be seen at higher silica loading.

Investigation of Ribulose-1,5-bisphosphate Carboxylase-Oxygenase from Tobacco by Small Angle X-Ray Scattering: A Structural Model for the Enzyme in Solution

1988 ◽  
Vol 43 (5-6) ◽  
pp. 373-376 ◽  
Author(s):  
P. M. Abuja ◽  
I. Pilz
Keyword(s):  
Small Angle ◽  
Quaternary Structure ◽  
Higher Plants ◽  
Maximum Diameter ◽  
Radius Of Gyration ◽  
Bisphosphate Carboxylase ◽  
X Ray ◽  
X Ray Scattering ◽  
Inactive Form ◽  
Ray Scattering

The quaternary structure of ribulose-1,5-bisphosphate carboxylase/oxygenase from tobacco (Nicotiana tabacum) was investigated in solution by means of small angle X-ray scattering. The most important molecular parameters as the radius of gyration (Rg) and the maximum diameter (Dmax) were determined. Both the active and the inactive form of the enzyme were measured at 5 °C and at 20 °C. A more distinct difference in size could be detected between the inactive forms at these two temperatures (Rg = 4.80 nm (5 °C) and 4.68 nm (20 °C)) than between the active forms (Rg = 4.73 nm and 4.69 nm). The maximum diameters were determined to be 13.1 nm for the inactive form at 5 °C and 12.8 nm for the other forms. A model is proposed consisting of eight large and eight small subunits arranged in the way that seems to be typical for this enzyme in higher plants.

Solution Structure of Myosin-ADP-MgFn Ternary Complex by Fluorescent Probes and Small-Angle Synchrotron X-Ray Scattering

2000 ◽  
Vol 128 (4) ◽  
pp. 687-694 ◽  
Author(s):  
S. Manita ◽  
T. Aihara ◽  
Y. Uyehara ◽  
K. Homma ◽  
Y. Sugimoto ◽  
...  
Keyword(s):  
Fluorescent Probes ◽  
Small Angle ◽  
Solution Structure ◽  
Ternary Complex ◽  
X Ray ◽  
X Ray Scattering ◽  
Ray Scattering

scholarly journals The solution structure and activation of visual arrestin studied by small-angle X-ray scattering

2002 ◽  
Vol 269 (15) ◽  
pp. 3801-3809 ◽  
Author(s):  
Brian H. Shilton ◽  
J. Hugh McDowell ◽  
W. Clay Smith ◽  
Paul A. Hargrave
Keyword(s):  
Small Angle ◽  
Solution Structure ◽  
X Ray ◽  
X Ray Scattering ◽  
Ray Scattering
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