Zobrazeno 1 - 10
of 287
pro vyhledávání: '"Carbonic Anhydrase B"'
Autor:
Vitaly A. Balobanov, N. S. Katina, Nelly B. Ilyina, Anatoly S. Glukhov, Victor V. Marchenkov, Natalya Ryabova
Publikováno v:
Biomolecules, Vol 11, Iss 1608, p 1608 (2021)
Biomolecules
Volume 11
Issue 11
Biomolecules
Volume 11
Issue 11
The development of many severe human diseases is associated with the formation of amyloid fibrils. Most of the available information on the process of amyloid formation has been obtained from studies of small proteins and peptides, wherein the featur
Akademický článek
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Publikováno v:
Molecular Biology. 39:438-444
High-resolution NMR spectroscopy has been used to study native carbonic anhydrase B unfolding with urea at pH 5.75 and T = 298 K. The rigidity parameter reflecting the effectiveness of spin diffusion (SD) displays a sigma-like dependence on urea conc
Refolding of denatured carbonic anhydrase B by reversed micelles formulated with nonionic surfactant
Publikováno v:
Biochemical Engineering Journal. 19:217-220
We have succeeded in the efficient refolding of denatured carbonic anhydrase B (CAB) using reversed micelles formulated with nonionic surfactant. The reversed micelles with nonionic tetraethylene glycol dodecyl ether prevented denatured CAB from aggr
Publikováno v:
FEBS Letters. 314:89-92
The Gdm-HCl-induced unfolding of bovine carbonic anhydrase B and S. aureus beta-lactamase was studied at 4 degrees C by a variety of methods. With the use of FPLC it has been shown that within the transition from the molten globule to the unfolded st
Publikováno v:
Bioconjugate Chemistry. 10:321-324
We have been studying the formation of hydrogel nanoparticles by the self-aggregation of hydrophobized polysaccharide and the effective complexation between these nanoparticles as a host and various globular soluble proteins as a guest. This paper de
Autor:
Peter Hanson, Samuel H. Gellman
Publikováno v:
Folding and Design. 3:457-468
Background: We have previously described a method for the refolding of chemically denatured proteins in which small molecules (‘artificial chaperones', a detergent and cyclodextrin) assist renaturation. In a previous analysis of lysozyme refolding
Autor:
Frank A. Gomez, Jane Kawaoka
Publikováno v:
Journal of Chromatography B: Biomedical Sciences and Applications. 715:203-210
This work evaluates the use of mobility ratios (M) to estimate binding constants of proteins to ligands using affinity capillary electrophoresis (ACE). This concept is demonstrated using two model systems: vancomycin (Van) from Streptomyces orientali
Autor:
Liujiao Bian, Xu Ji
Publikováno v:
PLoS ONE, Vol 9, Iss 3, p e91129 (2014)
PLoS ONE
PLoS ONE
Background Extensive and intensive studies on the unfolding of proteins require appropriate theoretical model and parameter to clearly illustrate the feature and characteristic of the unfolding system. Over the past several decades, four approaches h
Autor:
Jeffrey L. Cleland, Daniel I. C. Wang
Publikováno v:
Biotechnology Progress. 8:97-103
Many proteins which aggregate during refolding may form transiently populated aggregated states which do not reduce the final recovery of active species. However, the transient association of a folding intermediate will result in reduced refolding ra