Refolding and aggregation of bovine carbonic anhydrase B: quasi-elastic light scattering analysis.
about
Structural and catalytic characterization of a thermally stable and acid-stable variant of human carbonic anhydrase II containing an engineered disulfide bondExploring local flexibility/rigidity in psychrophilic and mesophilic carbonic anhydrases.Biophysical characterization of lithostathine. Evidences for a polymeric structure at physiological pH and a proteolysis mechanism leading to the formation of fibrils.Application of dynamic laser scattering to the quality control of injectable drugs: polymer formation in ampicillin solution.Oligomerization and aggregation of bovine pancreatic ribonuclease A: characteristic events observed by FTIR spectroscopyIncreasing the net charge and decreasing the hydrophobicity of bovine carbonic anhydrase decreases the rate of denaturation with sodium dodecyl sulfate.Protein aggregation kinetics in an Escherichia coli strain overexpressing a Salmonella typhimurium CheY mutant geneMechanistic Insight into the Reactivation of BCAII Enzyme from Denatured and Molten Globule States by Eukaryotic Ribosomes and Domain V rRNAsEarly aggregated States in the folding of interleukin-1β.Proline inhibits aggregation during protein refolding.Carbonic anhydrase as a model for biophysical and physical-organic studies of proteins and protein-ligand binding.Nonspecific hydrophobic interactions stabilize an equilibrium intermediate of apomyoglobin at a key position within the AGH region.Control of aggregation in protein refolding: the temperature-leap tactic.Control of aggregation in protein refolding: a variety of surfactants promote renaturation of carbonic anhydrase II.An automated in vitro protein folding screen applied to a human dynactin subunit.Colicin E1 forms a dimer after urea-induced unfolding.Effect of operating variables on the yield of recombinant trypsinogen for a pulse-fed dilution-refolding reactor.Efficient refolding of aggregation-prone citrate synthase by polyol osmolytes: how well are protein folding and stability aspects coupled?Chaperone-assisted refolding of Escherichia coli maltodextrin glucosidase.Polyvinylpyrrolidone 40 assists the refolding of bovine carbonic anhydrase B by accelerating the refolding of the first molten globule intermediate.Folding-related dimerization of human cystatin C.The Interaction of the Molecular Chaperone, α-Crystallin, with Molten Globule States of Bovine α-Lactalbumin
P2860
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P2860
Refolding and aggregation of bovine carbonic anhydrase B: quasi-elastic light scattering analysis.
description
1990 nî lūn-bûn
@nan
1990 թուականի Դեկտեմբերին հրատարակուած գիտական յօդուած
@hyw
1990 թվականի դեկտեմբերին հրատարակված գիտական հոդված
@hy
1990年の論文
@ja
1990年論文
@yue
1990年論文
@zh-hant
1990年論文
@zh-hk
1990年論文
@zh-mo
1990年論文
@zh-tw
1990年论文
@wuu
name
Refolding and aggregation of b ...... tic light scattering analysis.
@ast
Refolding and aggregation of b ...... tic light scattering analysis.
@en
type
label
Refolding and aggregation of b ...... tic light scattering analysis.
@ast
Refolding and aggregation of b ...... tic light scattering analysis.
@en
prefLabel
Refolding and aggregation of b ...... tic light scattering analysis.
@ast
Refolding and aggregation of b ...... tic light scattering analysis.
@en
P356
P1433
P1476
Refolding and aggregation of b ...... tic light scattering analysis.
@en
P2093
P304
11072-11078
P356
10.1021/BI00502A009
P407
P577
1990-12-01T00:00:00Z