Conformation and stability of thiol-modified bovine beta-lactoglobulin.
about
Salt-dependent monomer-dimer equilibrium of bovine beta-lactoglobulin at pH 3The loss of the hemoglobin H2S-binding function in annelids from sulfide-free habitats reveals molecular adaptation driven by Darwinian positive selection.Principal component analysis of the pH-dependent conformational transitions of bovine beta-lactoglobulin monitored by heteronuclear NMRCa(II)- and Tb(III)-induced stabilization and refolding of anticoagulation factor I from the venom of Agkistrodon acutus.A thiol probe for measuring unfolded protein load and proteostasis in cells.Bovine β-lactoglobulin is dimeric under imitative physiological conditions: dissociation equilibrium and rate constants over the pH range of 2.5-7.5.New Trends for the Evaluation of Heat Treatments of Milk.
P2860
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P2860
Conformation and stability of thiol-modified bovine beta-lactoglobulin.
description
2000 nî lūn-bûn
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2000 թուականի Սեպտեմբերին հրատարակուած գիտական յօդուած
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2000 թվականի սեպտեմբերին հրատարակված գիտական հոդված
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2000年の論文
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2000年論文
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2000年論文
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2000年論文
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2000年論文
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2000年論文
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2000年论文
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name
Conformation and stability of thiol-modified bovine beta-lactoglobulin.
@ast
Conformation and stability of thiol-modified bovine beta-lactoglobulin.
@en
type
label
Conformation and stability of thiol-modified bovine beta-lactoglobulin.
@ast
Conformation and stability of thiol-modified bovine beta-lactoglobulin.
@en
prefLabel
Conformation and stability of thiol-modified bovine beta-lactoglobulin.
@ast
Conformation and stability of thiol-modified bovine beta-lactoglobulin.
@en
P2093
P2860
P1433
P1476
Conformation and stability of thiol-modified bovine beta-lactoglobulin
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P2093
P2860
P304
P577
2000-09-01T00:00:00Z