Role of hydrophobicity in protein structure is overestimated

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

*Corresponding author for this work

Research output: Contribution to journalArticlepeer-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 languageEnglish
Pages (from-to)405-408
Number of pages4
JournalInternational Journal of Peptide and Protein Research
Volume34
Issue number5
DOIs
StatePublished - Nov 1989

Keywords

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

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