Sodium chloride enhances markedly the thermal stability of thermolysin as well as its catalytic activity.
about
Protective role of salt in catalysis and maintaining structure of halophilic proteins against denaturationSimplified protein design biased for prebiotic amino acids yields a foldable, halophilic proteinMALDI-TOF MS and CD spectral analysis for identification and structure prediction of a purified, novel, organic solvent stable, fibrinolytic metalloprotease from Bacillus cereus B80A method for screening enzyme inhibitors using size exclusion chromatography and ESI-LC-MS/MS.Structure of a partially unfolded form of Escherichia coli dihydrofolate reductase provides insight into its folding pathway.An intramolecular chaperone inserted in bacteriophage P22 coat protein mediates its chaperonin-independent folding.Functional analysis of the Burkholderia cenocepacia ZmpA metalloprotease.Investigating protein unfolding kinetics by pulse proteolysis.Ligand binding to a high-energy partially unfolded protein.Oxidant and SDS-stable alkaline protease from a halo-tolerant Bacillus clausii I-52: enhanced production and simple purification.Evaluation of the pH- and thermal stability of the recombinant green fluorescent protein (GFP) in the presence of sodium chloride.Effects of salts on the interaction of 8-anilinonaphthalene 1-sulphonate and thermolysin.Mutational effect for stability in a conserved region of thermolysin.
P2860
Q27010452-25C388D6-FA4D-44B1-85A9-AF590EA524E3Q27675962-7145432C-D248-4E18-8369-5C69E9132F42Q30372969-6B15A411-B22A-4B35-B04D-BFAD0A417EA6Q31146595-1BEF7580-68F2-4D58-AD45-E955ED6EAD10Q34621310-E5C4F678-8FFC-497F-A80E-01305BB5FF29Q37333736-179CB96A-B3DF-49D2-86FE-CE42CBC968E8Q38324668-FC012FD6-10FE-404E-B99F-7F8EEE04611AQ38357005-A3FCAD7D-5546-4818-8B3D-764F312CC390Q42552908-2F594A39-5831-4E25-B930-C502BD36694AQ45230281-68073E7D-5514-4164-9041-72F6DDEFD4E2Q46597224-0CC44125-B23D-4E32-9829-D1923A2663E0Q50222293-108FFF36-91D3-4103-A089-E84C01005341Q51499097-2A27A4B9-A5AB-4969-8241-314AEAF65C4B
P2860
Sodium chloride enhances markedly the thermal stability of thermolysin as well as its catalytic activity.
description
1998 nî lūn-bûn
@nan
1998年の論文
@ja
1998年学术文章
@wuu
1998年学术文章
@zh
1998年学术文章
@zh-cn
1998年学术文章
@zh-hans
1998年学术文章
@zh-my
1998年学术文章
@zh-sg
1998年學術文章
@yue
1998年學術文章
@zh-hant
name
Sodium chloride enhances marke ...... ell as its catalytic activity.
@en
Sodium chloride enhances marke ...... ell as its catalytic activity.
@nl
type
label
Sodium chloride enhances marke ...... ell as its catalytic activity.
@en
Sodium chloride enhances marke ...... ell as its catalytic activity.
@nl
prefLabel
Sodium chloride enhances marke ...... ell as its catalytic activity.
@en
Sodium chloride enhances marke ...... ell as its catalytic activity.
@nl
P2093
P1476
Sodium chloride enhances marke ...... ell as its catalytic activity.
@en
P2093
P304
P356
10.1016/S0167-4838(98)00189-7
P577
1998-10-01T00:00:00Z