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  2. Hydrophobicity scales - Wikipedia

    en.wikipedia.org/wiki/Hydrophobicity_scales

    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] There are clear differences between the four scales shown in the table. [11] Both the second and fourth scales place cysteine as the most hydrophobic residue, unlike the other two ...

  3. Hydrophilicity plot - Wikipedia

    en.wikipedia.org/wiki/Hydrophilicity_plot

    A hydrophilicity plot is a quantitative analysis of the degree of hydrophobicity or hydrophilicity of amino acids of a protein. It is used to characterize or identify possible structure or domains of a protein. The plot has amino acid sequence of a protein on its x-axis, and degree of hydrophobicity and hydrophilicity on its y-axis.

  4. Cystine - Wikipedia

    en.wikipedia.org/wiki/Cystine

    Cystine is the oxidized derivative of the amino acid cysteine and has the formula (SCH 2 CH(NH 2)CO 2 H) 2.It is a white solid that is poorly soluble in water. As a residue in proteins, cystine serves two functions: a site of redox reactions and a mechanical linkage that allows proteins to retain their three-dimensional structure.

  5. Cysteine - Wikipedia

    en.wikipedia.org/wiki/Cysteine

    Cysteine (/ ˈ s ɪ s t ɪ iː n /; [5] symbol Cys or C [6]) is a semiessential [7] proteinogenic amino acid with the formula HOOC−CH(−NH 2)−CH 2 −SH. The thiol side chain in cysteine enables the formation of disulfide bonds, and often participates in enzymatic reactions as a nucleophile. Cysteine is chiral, but both D and L-cysteine ...

  6. Proteinogenic amino acid - Wikipedia

    en.wikipedia.org/wiki/Proteinogenic_amino_acid

    Met is essential for humans. Always the first amino acid to be incorporated into a protein, it is sometimes removed after translation. Like cysteine, it contains sulfur, but with a methyl group instead of hydrogen. This methyl group can be activated, and is used in many reactions where a new carbon atom is being added to another molecule.

  7. Hydrophobin - Wikipedia

    en.wikipedia.org/wiki/Hydrophobin

    Hydrophobins are a group of small (~100 amino acids) cysteine-rich proteins that were discovered in filamentous fungi that are lichenized or not. Later similar proteins were also found in Bacteria. [1] Hydrophobins are known for their ability to form a hydrophobic (water-repellent) coating on the surface of an object. [2]

  8. Obesity in pets - Wikipedia

    en.wikipedia.org/wiki/Obesity_in_pets

    For dogs and cats, a 9 point body condition score (BCS) system is used to identify whether they are above their ideal weight status. [5] Scores 1-3 indicate 'too thin', 4 and 5 are 'ideal', 6 is 'above ideal', 7 is 'overweight' and 8 and 9 are 'obese'.

  9. Palmitoylation - Wikipedia

    en.wikipedia.org/wiki/Palmitoylation

    Scientists have appreciated the significance of attaching long hydrophobic chains to specific proteins in cell signaling pathways. A good example of its significance is in the clustering of proteins in the synapse. A major mediator of protein clustering in the synapse is the postsynaptic density (95kD) protein PSD-95. When this protein is ...