A chromatographic approach to the determination of relative free energies of interaction between hydrophobic and amphiphilic amino acid side chains.
about
Folding protein models with a simple hydrophobic energy function: the fundamental importance of monomer inside/outside segregation.Thermodynamics of interactions between amino acid side chains: experimental differentiation of aromatic-aromatic, aromatic-aliphatic, and aliphatic-aliphatic side-chain interactions in water.Self-interaction chromatography: a tool for the study of protein-protein interactions in bioprocessing environments.
P2860
A chromatographic approach to the determination of relative free energies of interaction between hydrophobic and amphiphilic amino acid side chains.
description
1992 nî lūn-bûn
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1992年の論文
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1992年学术文章
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1992年学术文章
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1992年学术文章
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name
A chromatographic approach to ...... philic amino acid side chains.
@ast
A chromatographic approach to ...... philic amino acid side chains.
@en
type
label
A chromatographic approach to ...... philic amino acid side chains.
@ast
A chromatographic approach to ...... philic amino acid side chains.
@en
prefLabel
A chromatographic approach to ...... philic amino acid side chains.
@ast
A chromatographic approach to ...... philic amino acid side chains.
@en
P2860
P356
P1433
P1476
A chromatographic approach to ...... philic amino acid side chains.
@en
P2093
T C Pochapsky
P2860
P304
P356
10.1002/PRO.5560010610
P577
1992-06-01T00:00:00Z