about
Determining biophysical protein stability in lysates by a fast proteolysis assay, FASTppStructural Basis for Protein Antiaggregation Activity of the Trigger Factor ChaperoneMaltose/maltodextrin system of Escherichia coli: transport, metabolism, and regulationIn vitro recombination of non-homologous genes can result in gene fusions that confer a switching phenotype to cellsRescue of glaucoma-causing mutant myocilin thermal stability by chemical chaperones.Exploration of multi-state conformational dynamics and underlying global functional landscape of maltose binding protein.Amyloid fibril formation by the glaucoma-associated olfactomedin domain of myocilin.Molecular Probing of the HPV-16 E6 Protein Alpha Helix Binding Groove with Small Molecule Inhibitors.Loss of function in phenylketonuria is caused by impaired molecular motions and conformational instabilityAn evaluation tool for FKBP12-dependent and -independent mTOR inhibitors using a combination of FKBP-mTOR fusion protein, DSC and NMR.Ligand binding specificity of the Escherichia coli periplasmic histidine binding protein, HisJ.A fusion tag to fold on: the S-layer protein SgsE confers improved folding kinetics to translationally fused enhanced green fluorescent protein.Maltodextrin-binding proteins from diverse bacteria and archaea are potent solubility enhancers.Thermodynamics and dynamics of histidine-binding protein, the water-soluble receptor of histidine permease. Implications for the transport of high and low affinity ligands.Prediction of the maximal stability temperature of monomeric globular proteins solely from amino acid sequence.Protein fusion tags for efficient expression and purification of recombinant proteins in the periplasmic space of E. coli.
P2860
Q21030644-0E9AC526-F012-4E20-BAEC-C1FE6D4D2C39Q27683688-F8F795BA-15A4-49BD-B49A-E89D52877535Q28266679-4253E928-FAC4-4296-BCD3-1D9359C9A9ABQ28742847-87CDF7AE-6B9C-43C1-9BF8-08C119B4EE91Q33869299-840E598C-6AB8-456D-B7A8-3CA79113D103Q34244861-4EC12158-4CAA-40B4-B985-CB81E62E4DB6Q35881767-0F054DAA-B7ED-44AE-8E9C-01FEAD98E50BQ35935872-16BA4F2D-4735-4F40-B706-0E365DF1347CQ36744649-4E244152-0A32-4790-B02E-7453FBD29CE9Q38755521-EFF6D1E0-56DE-4C84-B33D-5B9DFDABA685Q39172539-DF4A2333-FB4C-4CE6-8435-B207235A3781Q39543733-69229908-AD1A-47DF-8D6C-3126DC448E5AQ41468687-95C6D46A-74A5-46A6-B5A0-5FC5FE1A6954Q41743298-E942E001-37BD-44D2-A822-EC612E455125Q52209059-A2E7966F-5294-494A-B4C0-9B3C74386C5DQ53230714-AD7B1627-F158-419A-A3D1-EFFAA6ACF46B
P2860
description
1997 nî lūn-bûn
@nan
1997年の論文
@ja
1997年学术文章
@wuu
1997年学术文章
@zh-cn
1997年学术文章
@zh-hans
1997年学术文章
@zh-my
1997年学术文章
@zh-sg
1997年學術文章
@yue
1997年學術文章
@zh
1997年學術文章
@zh-hant
name
Thermodynamics of maltose binding protein unfolding.
@ast
Thermodynamics of maltose binding protein unfolding.
@en
type
label
Thermodynamics of maltose binding protein unfolding.
@ast
Thermodynamics of maltose binding protein unfolding.
@en
prefLabel
Thermodynamics of maltose binding protein unfolding.
@ast
Thermodynamics of maltose binding protein unfolding.
@en
P2860
P356
P1433
P1476
Thermodynamics of maltose binding protein unfolding.
@en
P2093
V Novokhatny
P2860
P304
P356
10.1002/PRO.5560060116
P577
1997-01-01T00:00:00Z