Microcalorimetric studies on the interaction mechanism between proteins and hydrophobic solid surfaces in hydrophobic interaction chromatography: effects of salts, hydrophobicity of the sorbent, and structure of the protein.
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Online Hydrophobic Interaction Chromatography-Mass Spectrometry for Top-Down ProteomicsA new thermodynamic model describes the effects of ligand density and type, salt concentration and protein species in hydrophobic interaction chromatography.Isothermal microcalorimetry to investigate non specific interactions in biophysical chemistry.Thermodynamic analysis of the interaction between proteins and solid surfaces: application to liquid chromatography.On-line determination by small angle X-ray scattering of the shape of hen egg white lysozyme immediately following elution from a hydrophobic interaction chromatography column.Studies on the binding sites of IgG2 monoclonal antibodies recognized by terpyridine-based affinity ligands.Thermodynamic assessment of the stability of thrombin receptor antagonistic peptides in hydrophobic environments.Role of interfacial hydrophobic residues in the stabilization of the leucine zipper structures of the transcription factors c-Fos and c-Jun.Extended DLVO calculations expose the role of the structural nature of the adsorbent beads during chromatography.The influence of mixed salts on the capacity of HIC adsorbers: A predictive correlation to the surface tension and the aggregation temperature.Optimal design of microarray immunoassays to compensate for kinetic limitations: theory and experiment.
P2860
Q30383142-78B6DDDD-E029-427D-90B1-3AAB1E5B6F35Q30415320-51F51BEE-970F-4CC4-BC66-05272D1E26D1Q33616419-5A68C5D8-54F2-4469-9A36-DB43DF465E9CQ34601784-38C3D0C8-1F62-4C7D-976E-7B3CF3DFC657Q39513578-50C62890-4F8E-446E-AA1C-6873B5531052Q40026405-11499B6B-BA2E-42CC-B37C-A983FF5AF022Q40205531-4028A009-CEAF-474A-9310-6BE082FE8580Q43767916-CCC94E71-E874-4CFD-A898-50CD3EE15D2FQ47634246-C9AC944E-1FE7-47A4-8185-3146C98F38DCQ48010295-79F7F727-F5A5-4DE7-9347-BA9DAC6BC05BQ53620498-90F12AE7-1841-44D4-BBCE-0C994B4E792E
P2860
Microcalorimetric studies on the interaction mechanism between proteins and hydrophobic solid surfaces in hydrophobic interaction chromatography: effects of salts, hydrophobicity of the sorbent, and structure of the protein.
description
2001 nî lūn-bûn
@nan
2001年の論文
@ja
2001年学术文章
@wuu
2001年学术文章
@zh-cn
2001年学术文章
@zh-hans
2001年学术文章
@zh-my
2001年学术文章
@zh-sg
2001年學術文章
@yue
2001年學術文章
@zh
2001年學術文章
@zh-hant
name
Microcalorimetric studies on t ...... and structure of the protein.
@en
Microcalorimetric studies on t ...... and structure of the protein.
@nl
type
label
Microcalorimetric studies on t ...... and structure of the protein.
@en
Microcalorimetric studies on t ...... and structure of the protein.
@nl
prefLabel
Microcalorimetric studies on t ...... and structure of the protein.
@en
Microcalorimetric studies on t ...... and structure of the protein.
@nl
P2093
P356
P1433
P1476
Microcalorimetric studies on t ...... and structure of the protein.
@en
P2093
P304
P356
10.1021/AC0102056
P407
P577
2001-08-01T00:00:00Z