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  2. Hydrophobicity scales - Wikipedia

    en.wikipedia.org/wiki/Hydrophobicity_scales

    A table comparing four different scales for the hydrophobicity of an amino acid residue in a protein with the most hydrophobic amino acids on the top. A number of different hydrophobicity scales have been developed. [3] [1] [7] [8] [9] The Expasy Protscale website lists a total of 22 hydrophobicity scales. [10]

  3. Hopp–Woods scale - Wikipedia

    en.wikipedia.org/wiki/Hopp–Woods_scale

    The Hopp–Woods hydrophilicity scale of amino acids is a method of ranking the amino acids in a protein according to their water solubility in order to search for surface locations on proteins, and especially those locations that tend to form strong interactions with other macromolecules such as proteins, DNA, and RNA.

  4. Hydrophilicity plot - Wikipedia

    en.wikipedia.org/wiki/Hydrophilicity_plot

    Analyzing the shape of the plot gives information about partial structure of the protein. For instance, if a stretch of about 20 amino acids shows positive for hydrophobicity, these amino acids may be part of alpha-helix spanning across a lipid bilayer, which is composed of hydrophobic fatty acids. On the converse, amino acids with high ...

  5. List of chemistry mnemonics - Wikipedia

    en.wikipedia.org/wiki/List_of_chemistry_mnemonics

    A mnemonic is a memory aid used to improve long-term memory and make the process of consolidation easier. Many chemistry aspects, rules, names of compounds, sequences of elements, their reactivity, etc., can be easily and efficiently memorized with the help of mnemonics. This article contains the list of certain mnemonics in chemistry.

  6. Amino acid - Wikipedia

    en.wikipedia.org/wiki/Amino_acid

    Structure of a typical L-alpha-amino acid in the "neutral" form. Amino acids are organic compounds that contain both amino and carboxylic acid functional groups. [1] Although over 500 amino acids exist in nature, by far the most important are the 22 α-amino acids incorporated into proteins. [2]

  7. Hydrophobic-polar protein folding model - Wikipedia

    en.wikipedia.org/wiki/Hydrophobic-polar_protein...

    The hydrophobic-polar protein folding model is a highly simplified model for examining protein folds in space. First proposed by Ken Dill in 1985, it is the most known type of lattice protein: it stems from the observation that hydrophobic interactions between amino acid residues are the driving force for proteins folding into their native state. [1]

  8. Fantasy football Start 'Em, Sit 'Em: 40 players to start or ...

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    Week 12 marks the first "Byemageddon” of the NFL season in fantasy football. A season-high six teams have their bye this week: the New York Jets, Atlanta Falcons, Buffalo Bills, Cincinnati ...

  9. Protein folding - Wikipedia

    en.wikipedia.org/wiki/Protein_folding

    The hydrophobic effect is the phenomenon in which the hydrophobic chains of a protein collapse into the core of the protein (away from the hydrophilic environment). [12] In an aqueous environment, the water molecules tend to aggregate around the hydrophobic regions or side chains of the protein, creating water shells of ordered water molecules ...

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