Interaction of urea with an unfolded protein. The DNA-binding domain of the 434-repressor.
about
The free energy landscape of small molecule unbindingWater and urea interactions with the native and unfolded forms of a beta-barrel protein.Salt-stabilized globular protein structure in 7 M aqueous urea solution.Structural characterization of apomyoglobin self-associated species in aqueous buffer and urea solution.The molecular basis for the chemical denaturation of proteins by urea.Native-state hydrogen-exchange studies of a fragment complex can provide structural information about the isolated fragments.Time-dependent X-ray diffraction studies on urea/hen egg white lysozyme complexes reveal structural changes that indicate onset of denaturationMechanism of Protein Denaturation: Partial Unfolding of the P22 Coat Protein I-Domain by Urea Binding.Denaturation mechanism of BSA by urea derivatives: evidence for hydrogen-bonding mode from fluorescence tools.Structure and dynamics of a salt-bridge model system in water and DMSO.Destruction of hydrogen bonds of poly(N-isopropylacrylamide) aqueous solution by trimethylamine N-oxide
P2860
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P2860
Interaction of urea with an unfolded protein. The DNA-binding domain of the 434-repressor.
description
1995 nî lūn-bûn
@nan
1995年の論文
@ja
1995年論文
@yue
1995年論文
@zh-hant
1995年論文
@zh-hk
1995年論文
@zh-mo
1995年論文
@zh-tw
1995年论文
@wuu
1995年论文
@zh
1995年论文
@zh-cn
name
Interaction of urea with an un ...... g domain of the 434-repressor.
@ast
Interaction of urea with an un ...... g domain of the 434-repressor.
@en
type
label
Interaction of urea with an un ...... g domain of the 434-repressor.
@ast
Interaction of urea with an un ...... g domain of the 434-repressor.
@en
prefLabel
Interaction of urea with an un ...... g domain of the 434-repressor.
@ast
Interaction of urea with an un ...... g domain of the 434-repressor.
@en
P2093
P2860
P1433
P1476
Interaction of urea with an un ...... g domain of the 434-repressor.
@en
P2093
P2860
P356
10.1016/0014-5793(95)00459-M
P407
P577
1995-06-01T00:00:00Z