Solution structure of a human cystatin A variant, cystatin A2-98 M65L by NMR spectroscopy. A possible role of the interactions between the N- and C-termini to maintain the inhibitory active form of cystatin A

Biochemistry ◽  
1995 ◽  
Vol 34 (45) ◽  
pp. 14637-14648 ◽  
Author(s):  
Shin-ichi Tate ◽  
Toshio Ushioda ◽  
Naoko Utsunomiya-Tate ◽  
Kazunori Shibuya ◽  
Yukihito Ohyama ◽  
...  
Keyword(s):  
Nmr Spectroscopy ◽  
Solution Structure ◽  
Active Form ◽  
Cystatin A ◽  
Human Cystatin

scholarly journals Structure of Nanobody Nb23

Molecules ◽  
2021 ◽  
Vol 26 (12) ◽  
pp. 3567
Author(s):  
Mathias Percipalle ◽  
Yamanappa Hunashal ◽  
Jan Steyaert ◽  
Federico Fogolari ◽  
Gennaro Esposito
Keyword(s):  
Nmr Spectroscopy ◽  
Chemical Shift ◽  
Solution Structure ◽  
Chemical Shifts ◽  
Molecular Size ◽  
Side Chain ◽  
3D Nmr ◽  
Target Antigen ◽  
Internuclear Distances ◽  
2D And 3D

Background: Nanobodies, or VHHs, are derived from heavy chain-only antibodies (hcAbs) found in camelids. They overcome some of the inherent limitations of monoclonal antibodies (mAbs) and derivatives thereof, due to their smaller molecular size and higher stability, and thus present an alternative to mAbs for therapeutic use. Two nanobodies, Nb23 and Nb24, have been shown to similarly inhibit the self-aggregation of very amyloidogenic variants of β2-microglobulin. Here, the structure of Nb23 was modeled with the Chemical-Shift (CS)-Rosetta server using chemical shift assignments from nuclear magnetic resonance (NMR) spectroscopy experiments, and used as prior knowledge in PONDEROSA restrained modeling based on experimentally assessed internuclear distances. Further validation was comparatively obtained with the results of molecular dynamics trajectories calculated from the resulting best energy-minimized Nb23 conformers. Methods: 2D and 3D NMR spectroscopy experiments were carried out to determine the assignment of the backbone and side chain hydrogen, nitrogen and carbon resonances to extract chemical shifts and interproton separations for restrained modeling. Results: The solution structure of isolated Nb23 nanobody was determined. Conclusions: The structural analysis indicated that isolated Nb23 has a dynamic CDR3 loop distributed over different orientations with respect to Nb24, which could determine differences in target antigen affinity or complex lability.

Solution Structure of [Me-L-Leu7]Didemnin B Determined by NMR Spectroscopy and Refined by MD Calculation

1990 ◽  
Vol 73 (1) ◽  
pp. 25-47 ◽  
Author(s):  
Horst Kessler ◽  
Siggi Mronga ◽  
Martin Will ◽  
Ulrich Schmidt
Keyword(s):  
Nmr Spectroscopy ◽  
Solution Structure ◽  
Didemnin B

Role of Barium(II) in the Determination of the Absolute Configuration of Chiral Amines by1H NMR Spectroscopy

2006 ◽  
Vol 71 (3) ◽  
pp. 1119-1130 ◽  
Author(s):  
Rosa García ◽  
José M. Seco ◽  
Saulo A. Vázquez ◽  
Emilio Quiñoá ◽  
Ricardo Riguera
Keyword(s):  
Nmr Spectroscopy ◽  
Absolute Configuration ◽  
Chiral Amines ◽  
The Absolute

scholarly journals Rab3D regulates amylase levels, not agonist-induced amylase release, in AR42J cells

2012 ◽  
Vol 17 (2) ◽  
Author(s):  
Saima Limi ◽  
George Ojakian ◽  
Robert Raffaniello
Keyword(s):  
Secretory Granules ◽  
Active Form ◽  
Subcellular Fractionation ◽  
Amylase Release ◽  
Ar42j Cells ◽  
Granule Density ◽  
Granule Morphology ◽  
Pancreatic Exocrine

AbstractRab3D is a low molecular weight GTP-binding protein that associates with secretory granules in exocrine cells. AR42J cells are derived from rat pancreatic exocrine tumor cells and develop an acinar cell-like phenotype when treated with dexamethasone (Dex). In the present study, we examined the role of Rab3D in Dex-treated AR42J cells. Rab3D expression and localization were analyzed by subcellular fractionation and immunoblotting. The role of Rab3D was examined by overexpressing myc-labeled wild-type-Rab3D and a constitutively active form of Rab3D (Rab3D-Q81L) in AR42J cells. We found that Rab3D is predominantly membrane-associated in AR42J cells and co-localizes with zymogen granules (ZG). Following CCK-8-induced exocytosis, amylase-positive ZGs appeared to move towards the periphery of the cell and co-localization between Rab3D and amylase was less complete when compared to basal conditions. Overexpression of WT, but not mutant Rab3D, resulted in an increase in cellular amylase levels. Overexpression of mutant and WT Rab3D did not affect granule morphology, CCK-8-induced secretion, long-term (48 hr) basal amylase release or granule density. We conclude that Rab3D is not involved in agonist-induced exocytosis in AR42J cells. Instead, Rab3D may regulate amylase content in these cells.

Solution structure of branched U3′p5′A2′p5′G3′p5′C and its comparison with A2′p5′G3′p5′U by 500 MHz NMR spectroscopy

Tetrahedron ◽  
1991 ◽  
Vol 47 (20-21) ◽  
pp. 3417-3430 ◽  
Author(s):  
C. Glemarec ◽  
M. Jaseja ◽  
A. Sandström ◽  
L. Koole ◽  
P. Agback ◽  
...  
Keyword(s):  
Nmr Spectroscopy ◽  
Solution Structure

CERAMICS BASED ON ORGANOSILICON POLYMERS-PRECURSORS: MICROSTRUCTURE AND PROPERTIES (review). Part 2

2021 ◽  
pp. 22-32
Author(s):  
A.M. Shestakov ◽  
Keyword(s):  
Electron Microscopy ◽  
Nmr Spectroscopy ◽  
Material Properties ◽  
Structural Organization ◽  
Ceramic Materials ◽  
Special Role ◽  
Correct Interpretation ◽  
Instrumental Methods ◽  
Organosilicon Polymers

Shows the scientific approaches of various authors to the study of the microstructure of ceramics, the purpose of which is to elucidate its structural organization at the micro- and nanoscale, as well as the influence of the microstructure on the complex of material properties. Various instrumental methods for studying ceramics (NMR spectroscopy, electron microscopy, х-ray structural analysis, etc.) are considered, the permissible capabilities of research methods and analysis of the results obtained with their correct interpretation are shown. The special role of theoretical modeling in understanding the structure of the considered ceramic materials is noted.

Solution Structure of a DNA Complex with the Fluorescent Bis-Intercalator TOTO Determined by NMR Spectroscopy

Biochemistry ◽  
1995 ◽  
Vol 34 (27) ◽  
pp. 8542-8553 ◽  
Author(s):  
H. Peter Spielmann ◽  
David E. Wemmer ◽  
Jens Peter Jacobsen
Keyword(s):  
Nmr Spectroscopy ◽  
Solution Structure ◽  
Dna Complex
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