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Journal ArticleDOI

Surface tension of amino acid solutions: A hydrophobicity scale of the amino acid residues

Henry B. Bull, +1 more
- 01 Apr 1974 - 
- Vol. 161, Iss: 2, pp 665-670
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TLDR
From the experimental results, the free energies of transfer of the amino acid residues from the solution to the surface have been calculated to yield a hydrophobicity scale of the residues, in fairly good agreement with that of Nozaki and Tanford.
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This article is published in Archives of Biochemistry and Biophysics.The article was published on 1974-04-01. It has received 449 citations till now. The article focuses on the topics: Hydrophobicity scales & Amino acid.

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Citations
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Journal ArticleDOI

A simple method for displaying the hydropathic character of a protein

TL;DR: A computer program that progressively evaluates the hydrophilicity and hydrophobicity of a protein along its amino acid sequence has been devised and its simplicity and its graphic nature make it a very useful tool for the evaluation of protein structures.
Journal ArticleDOI

New hydrophilicity scale derived from high-performance liquid chromatography peptide retention data: correlation of predicted surface residues with antigenicity and X-ray-derived accessible sites.

TL;DR: It was found that the HPLC parameters obtained in this study correlated best with antigenicity, and it was shown that a combination of the three best parameters for predicting antigenicity further improved the predictions.
Journal ArticleDOI

Bacterial osmoadaptation: the role of osmolytes in bacterial stress and virulence

TL;DR: The molecular mechanisms governing the accumulation of these compounds, both in Gram-positive and Gram-negative bacteria, are reviewed, focusing specifically on the regulation of their transport/synthesis systems and the ability of these systems to sense and respond to changes in the osmolarity of the extracellular environment.
Journal ArticleDOI

Hydrophobicity scales and computational techniques for detecting amphipathic structures in proteins

TL;DR: Although the scale is optimal only for predicting alpha-amphipathicity, it also ranks high in identifying beta-ampshipathicity and in distinguishing interior from exterior residues in a protein.
References
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Book ChapterDOI

Some factors in the interpretation of protein denaturation.

TL;DR: The chapter reviews that the denaturation is a process in which the spatial arrangement of the polypeptide chains within the molecule is changed from that typical of the native protein to a more disordered arrangement.
Journal ArticleDOI

The Solubility of Amino Acids and Two Glycine Peptides in Aqueous Ethanol and Dioxane Solutions ESTABLISHMENT OF A HYDROPHOBICITY SCALE

TL;DR: In this article, the free energies of transfer of amino acid side chains and backbone peptide units from water to ethanol and dioxane solutions have been calculated from these data and the results show the similarity between the effects of ethanol and Dioxane on the stability of those side chains.
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