Hydrophilicity of polar amino acid side-chains is markedly reduced by flanking peptide bonds
- 1 April 1988
- journal article
- research article
- Published by Elsevier in Journal of Molecular Biology
- Vol. 200 (3), 513-522
- https://doi.org/10.1016/0022-2836(88)90540-2
Abstract
No abstract availableThis publication has 13 references indexed in Scilit:
- Hydrophobicity of Amino Acid Residues in Globular ProteinsScience, 1985
- Turns in Peptides and ProteinsAdvances in protein chemistry, 1985
- Intrahelical hydrogen bonding of serine, threonine and cysteine residues within α-helices and its relevance to membrane-bound proteinsJournal of Molecular Biology, 1984
- A simple method for displaying the hydropathic character of a proteinJournal of Molecular Biology, 1982
- On the Hydrophobic Nature of Signal SequencesEuropean Journal of Biochemistry, 1981
- Affinities of amino acid side chains for solvent waterBiochemistry, 1981
- Trans‐membrane Translocation of ProteinsEuropean Journal of Biochemistry, 1979
- Shape of the hydrophobic barrier of phospholipid bilayers (Evidence for water penetration in biological membranes)The Journal of Membrane Biology, 1974
- Partition coefficients and their usesChemical Reviews, 1971
- Thermodynamics of transfer of amides from an apolar to an aqueous solutionBiochemistry, 1969