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prot pi – protein isoelectric point — an online program for calculating pI of proteins (include multiple subunits and posttranslational modifications) CurTiPot — a suite of spreadsheets for computing acid-base equilibria (charge versus pH plot of amphoteric molecules e.g., amino acids)
The amino acids in a standard π-helix are arranged in a right-handed helical structure. Each amino acid corresponds to an 87° turn in the helix (i.e., the helix has 4.1 residues per turn), and a translation of 1.15 Å (0.115 nm) along the helical axis.
2-, alpha-, or α-amino acids [21] have the generic formula H 2 NCHRCOOH in most cases, [b] where R is an organic substituent known as a "side chain". [22] Of the many hundreds of described amino acids, 22 are proteinogenic ("protein-building").
[69] [70] Buffering is an essential part of acid base physiology including acid–base homeostasis, [71] and is key to understanding disorders such as acid–base disorder. [ 72 ] [ 73 ] [ 74 ] The isoelectric point of a given molecule is a function of its p K values, so different molecules have different isoelectric points.
The digits of pi extend into infinity, and pi is itself an irrational number, meaning it can’t be truly represented by an integer fraction (the one we often learn in school, 22/7, is not very ...
Short pieces of left-handed helix sometimes occur with a large content of achiral glycine amino acids, but are unfavorable for the other normal, biological L-amino acids. The pitch of the alpha-helix (the vertical distance between consecutive turns of the helix) is 5.4 Å (0.54 nm), which is the product of 1.5 and 3.6.
Histidine (symbol His or H) [2] is an essential amino acid that is used in the biosynthesis of proteins.It contains an α-amino group (which is in the protonated –NH 3 + form under biological conditions), a carboxylic acid group (which is in the deprotonated –COO − form under biological conditions), and an imidazole side chain (which is partially protonated), classifying it as a ...
Also, amino acid side chain affinity for water was measured using vapor phases. [14] Vapor phases represent the simplest non polar phases, because it has no interaction with the solute. [18] The hydration potential and its correlation to the appearance of amino acids on the surface of proteins was studied by Wolfenden.