User:Just granpa
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Side-chain properties
class="wikitable sortable" style="text-align: center"
! scope="col" | Amino acid ! scope="col" | Short ! scope="col" | {{abbr|Abbrev.|Abbreviation}} ! scope="col" | Side chain ! scope="col" | Hydro- ! scope="col" | {{abbr|pKa§|Acid dissociation constant}} ! scope="col" | Polar ! scope="col" | pH ! scope="col" | Small ! scope="col" | Tiny ! scope="col" | Aromatic ! scope="col" | van der Waals |
scope="row" {{rh2|align=right}} | Alanine
| A | Ala | -CH3 | {{ya}} | - | {{na}} | - | {{ya}} | {{ya}} | Aliphatic | 67 |
---|
scope="row" {{rh2|align=right}} | Glycine
| G | Gly | -H | {{ya}} | - | {{na}} | - | {{ya}} | {{ya}} | - | 48 |
scope="row" {{rh2|align=right}} | Methionine
| M | Met | -CH2CH2SCH3 | {{ya}} | - | {{na}} | - | {{na}} | {{na}} | Aliphatic | 124 |
scope="row" {{rh2|align=right}} | Proline
| P | Pro | -CH2CH2CH2- | {{ya}} | - | {{na}} | - | {{ya}} | {{na}} | - | 90 |
scope="row" {{rh2|align=right}} | Arginine
| R | Arg | -(CH2)3NH-C(NH)NH2 | {{na}} | 12.3 | {{ya}} | strongly basic | {{na}} | {{na}} | - | 148 |
§: Values for Asp, Cys, Glu, His, Lys & Tyr were determined using the amino acid residue placed centrally in an alanine pentapeptide.{{cite journal | vauthors = Thurlkill RL, Grimsley GR, Scholtz JM, Pace CN | title = pK values of the ionizable groups of proteins | journal = Protein Science | volume = 15 | issue = 5 | pages = 1214–8 | date = May 2006 | pmid = 16597822 | pmc = 2242523 | doi = 10.1110/ps.051840806 }} The value for Arg is from Pace et al. (2009).{{cite journal | vauthors = Pace CN, Grimsley GR, Scholtz JM | title = Protein ionizable groups: pK values and their contribution to protein stability and solubility | journal = The Journal of Biological Chemistry | volume = 284 | issue = 20 | pages = 13285–9 | date = May 2009 | pmid = 19164280 | pmc = 2679426 | doi = 10.1074/jbc.R800080200 | doi-access = free }} The value for Sec is from Byun & Kang (2011).{{cite journal | vauthors = Byun BJ, Kang YK | title = Conformational preferences and pK(a) value of selenocysteine residue | journal = Biopolymers | volume = 95 | issue = 5 | pages = 345–53 | date = May 2011 | pmid = 21213257 | doi = 10.1002/bip.21581 | s2cid = 11002236 }}
N.D.: The pKa value of Pyrrolysine has not been reported.
Note: The pKa value of an amino-acid residue in a small peptide is typically slightly different when it is inside a protein. Protein pKa calculations are sometimes used to calculate the change in the pKa value of an amino-acid residue in this situation.
hieroglyphics
see also: Egyptian Hieroglyphs