Topic
Hydrophobicity scales
About: Hydrophobicity scales is a research topic. Over the lifetime, 413 publications have been published within this topic receiving 53333 citations.
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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.
21,921 citations
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TL;DR: An algorithm has been developed which identifies alpha-helices involved in the interactions of membrane proteins with lipid bilayers and which distinguishes them from helices in soluble proteins, and suggests four transmembrane helices and a surface-seeking helix in fragment B, the moiety known to have trans Membrane function.
2,157 citations
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TL;DR: A complete interfacial hydrophobicity scale that includes the contribution of the peptide bond was determined from the partitioning of two series of small model peptides into the interfaces of neutral (zwitterionic) phospholipid membranes.
Abstract: The partitioning of membrane-active oligopeptides into membrane interfaces promotes the formation of secondary structure. A quantitative description of the coupling of structure formation to partitioning, which may provide a basis for understanding membrane protein folding and insertion, requires an appropriate free energy scale for partitioning. A complete interfacial hydrophobicity scale that includes the contribution of the peptide bond was therefore determined from the partitioning of two series of small model peptides into the interfaces of neutral (zwitterionic) phospholipid membranes. Aromatic residues are found to be especially favoured at the interface while charged residues, and the peptide bond, are disfavoured about equally. Reduction of the high cost of partitioning the peptide bond through hydrogen bonding may be important in the promotion of structure formation in the membrane interface.
1,531 citations
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01 Jan 1986
TL;DR: The next generation of autonomous vehicles will be able to communicate with each other in a much more efficient and efficient manner than the current generation of vehicles that can communicate solely with the human eye.
Abstract: PERSPECTIVES AND OVERVIEW ............................................................................................................. 32
1,498 citations
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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.
1,290 citations