Size and shape trump charge in interactions of oxovanadates with self-assembled interfaces: application of continuous shape measure analysis to the decavanadate anion

2016 ◽  
Vol 40 (2) ◽  
pp. 962-975 ◽  
Author(s):  
Irma Sánchez-Lombardo ◽  
Bharat Baruah ◽  
Santiago Alvarez ◽  
Katarina R. Werst ◽  
Nicole A. Segaline ◽  
...  
Keyword(s):  
Light Scattering ◽  
Nmr Spectroscopy ◽  
Dynamic Light Scattering ◽  
Shape Analysis ◽  
Reverse Micelles ◽  
Size And Shape ◽  
Measure Analysis ◽  
Self Assembled

Using 51V NMR spectroscopy, dynamic light scattering and continuous shape analysis to characterize two polyoxometalate-encapsulation in reverse micelles.

scholarly journals Size and Shape of Human Fibrinogen in Solution

1977 ◽  
Author(s):  
V. Hofmann ◽  
P.W. Straub ◽  
T. Binkert ◽  
E. Serrallach ◽  
W. Känzig ◽  
...  
Keyword(s):  
Light Scattering ◽  
Dynamic Light Scattering ◽  
Analytical Ultracentrifugation ◽  
Rotational Diffusion ◽  
Axial Ratio ◽  
Major Axis ◽  
Fluorescence Depolarization ◽  
Human Fibrinogen ◽  
Size And Shape ◽  
Rotational Diffusion Coefficients

In order to obtain information on size and shape of the fibrinogen molecule in solution the translational diffusion coefficient (DT), the rotational diffusion coefficients (DR⊥ and DR//) and the sedimentation coefficients (S) have been measured on human fibrinogen with a clottaoility above 95%. The methods used were dynamic light scattering, nanosecond fluorescence depolarization and analytical ultracentrifugation. Dynamic light scattering yields DT = 2.0 ± 3% x 10-7 cm2sec–1 at a concentration of 7 mg/ml in 0.15 M Tris-NaCl, pH 7.4. DT is strongly dependent on concentration, being 3.4 ± 10% × 10-7 cm2 sec-1 at 0.1 mg/ml. The rotation along the minor axis as measured with the same method is DR = // 1.5 × 106 sec-1 at 0.1 mg/ml. The rotation along the major axis as measured on fibrinogen labeled with dansylchloride is DR// = 1.5 x106 sec–1. S is also strongly dependent on concentration, being 7.9 S at 0.1 mg/ml, 8.1 S at 1 mg/ml and 6.6 S at 10 mg/ml.These results fit with an elongated molecule having an axial ratio of 7. They are compatible with a MW of 340’000 only for concentrations above 2 mg/ml, while at lower concentrations (0.1 mg/ml) they agree with a MW of approximately half the accepted value.

Dynamic Light Scattering and FTIR Spectroscopic Investigations on the Reverse Micelles Produced During the Extraction of Nd(III) and Nitric Acid in Tetra Ethylhexyl Diglycolamide

2017 ◽  
Vol 2 (34) ◽  
pp. 11177-11186 ◽  
Author(s):  
Kantamani Rama Swami ◽  
Asokan Sudha Suneesh ◽  
Radhakrishnan Kumaresan ◽  
Konda Athmaram Venkatesan ◽  
Malpan Pailo Antony
Keyword(s):  
Light Scattering ◽  
Nitric Acid ◽  
Dynamic Light Scattering ◽  
Reverse Micelles ◽  
Spectroscopic Investigations

Characterizing the Brownian Diffusion of Nanocolloids and Molecular Solutions: Diffusion-Ordered NMR Spectroscopy vs Dynamic Light Scattering

2020 ◽  
Vol 124 (22) ◽  
pp. 4631-4650 ◽  
Author(s):  
Chengqi Zhang ◽  
Zhicheng Jin ◽  
Birong Zeng ◽  
Wentao Wang ◽  
Goutam Palui ◽  
...  
Keyword(s):  
Light Scattering ◽  
Nmr Spectroscopy ◽  
Dynamic Light Scattering ◽  
Brownian Diffusion

scholarly journals AHSP (α-haemoglobin-stabilizing protein) stabilizes apo-α-haemoglobin in a partially folded state

2010 ◽  
Vol 432 (2) ◽  
pp. 275-282 ◽  
Author(s):  
Kaavya Krishna Kumar ◽  
Claire F. Dickson ◽  
Mitchell J. Weiss ◽  
Joel P. Mackay ◽  
David A. Gell
Keyword(s):  
Light Scattering ◽  
Nmr Spectroscopy ◽  
Dynamic Light Scattering ◽  
Redox Activity ◽  
Heterodimeric Complex ◽  
Self Association ◽  
Partially Folded State ◽  
Haem Iron

To produce functional Hb (haemoglobin), nascent α-globin (αo) and β-globin (βo) chains must each bind a single haem molecule (to form αh and βh) and interact together to form heterodimers. The precise sequence of binding events is unknown, and it has been suggested that additional factors might enhance the efficiency of Hb folding. AHSP (α-haemoglobin-stabilizing protein) has been shown previously to bind αh and regulate redox activity of the haem iron. In the present study, we used a combination of classical and dynamic light scattering and NMR spectroscopy to demonstrate that AHSP forms a heterodimeric complex with αo that inhibits αo aggregation and promotes αo folding in the absence of haem. These findings indicate that AHSP may function as an αo-specific chaperone, and suggest an important role for αo in guiding Hb assembly by stabilizing βo and inhibiting off-pathway self-association of βh.

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