Thermodynamic assessment of the stability of thrombin receptor antagonistic peptides in hydrophobic environments.
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Salts employed in hydrophobic interaction chromatography can change protein structure - insights from protein-ligand interaction thermodynamics, circular dichroism spectroscopy and small angle X-ray scattering.Thermodynamic analysis of the interaction between proteins and solid surfaces: application to liquid chromatography.
P2860
Thermodynamic assessment of the stability of thrombin receptor antagonistic peptides in hydrophobic environments.
description
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2002年の論文
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2002年論文
@yue
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@zh-hant
2002年論文
@zh-hk
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@zh-mo
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@zh-tw
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name
Thermodynamic assessment of th ...... s in hydrophobic environments.
@en
type
label
Thermodynamic assessment of th ...... s in hydrophobic environments.
@en
prefLabel
Thermodynamic assessment of th ...... s in hydrophobic environments.
@en
P2860
P1433
P1476
Thermodynamic assessment of th ...... es in hydrophobic environments
@en
P2093
Agnes J O Jong
Milton T W Hearn
P2860
P304
P356
10.1016/S0006-3495(02)75574-4
P407
P577
2002-05-01T00:00:00Z