Role of hydrophobicity in protein structure is overestimated

MICHAEL BLOEMENDAL; YIZHAK MARCUS; ANDRE H. SIJPKES; GUS SOMSEN

doi:10.1111/j.1399-3011.1989.tb00709.x

Role of hydrophobicity in protein structure is overestimated

MICHAEL BLOEMENDAL^*
, YIZHAK MARCUS
, ANDRE H. SIJPKES
, GUS SOMSEN

^*Corresponding author for this work

Institute of Chemistry

Research output: Contribution to journal › Article › peer-review

13 Scopus citations

Abstract

Some microcalorimetrically measured and theoretically calculated thermodynamic interaction coefficients of amino acid compounds in aqueous and peptidic systems have been collected, and are reported here. They indicate that although hydrophobicity contributes to the stability of the native structure of proteins, its influence on their exact configuration is limited.

Original language	English
Pages (from-to)	405-408
Number of pages	4
Journal	International Journal of Peptide and Protein Research
Volume	34
Issue number	5
DOIs	https://doi.org/10.1111/j.1399-3011.1989.tb00709.x
State	Published - Nov 1989

Keywords

N,N‐dimethylformamide
amino acid compounds
hydrophobic interaction
protein structure
thermodynamic interaction coefficients

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10.1111/j.1399-3011.1989.tb00709.x

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abstract = "Some microcalorimetrically measured and theoretically calculated thermodynamic interaction coefficients of amino acid compounds in aqueous and peptidic systems have been collected, and are reported here. They indicate that although hydrophobicity contributes to the stability of the native structure of proteins, its influence on their exact configuration is limited.",

keywords = "N,N‐dimethylformamide, amino acid compounds, hydrophobic interaction, protein structure, thermodynamic interaction coefficients",

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AU - MARCUS, YIZHAK

AU - SIJPKES, ANDRE H.

AU - SOMSEN, GUS

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KW - N,N‐dimethylformamide

KW - amino acid compounds

KW - hydrophobic interaction

KW - protein structure

KW - thermodynamic interaction coefficients

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ER -

Role of hydrophobicity in protein structure is overestimated

Abstract

Keywords

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