polar amino acid

po·lar a·mi·no ac·id

an α-amino acid in which the functional group attached to the α-carbon (that is, R in RCH(NH3+)COO-) has hydrophilic properties, for example, serine, cysteine, homocysteine.
References in periodicals archive ?
For each ith polar amino acid, all free lattice points that are common neighbours of lattice points occupied by (i - 1)th and (i + 1)th amino acids are listed.
These amino acids are broadly divided into two categories based on their hydrophobicity (a) hydrophobic amino acids (Gly, Ala, Pro, Val, Leu, Ile, Met, Phe, Tyr, Trp) denoted by H; and (b) hydrophilic or polar amino acids (Ser, Thr, Cys, Asn, Gln, Lys, His, Arg, Asp, Glu) denoted by P.
The Arg114Pro amino acid substitution would produce a change from a hydrophilic positively charged, polar amino acid on the amino-terminal domain (residues 1-164) to a hydrophobic nonpolar amino acid.
Higher water absorption capacity of spirulina protein isolates (2.96 [+ or -] 0.17 mL/g) may have been due to presence of more polar amino acids at primary cites of protein-water interface (Table 2).
The replacement of P92S and A277T were conversion of non-polar to polar amino acids whereas the change of T156A T191A and T239M were from polar to nonpolar amino acids.
A percentage of polar amino acids were higher while nonpolar were lesser in mesophilic [beta]-galactosidase as compared to psychrophilic and thermophilic [beta]-galactosidases (Figure 1).
Samples of Day 1, 5 and 6 are observed to be undesirable in formulation of foods like pancakes, soups and other baked foods as these cannot bind fats to create tenderness or smoothness probably because the hydrophobic non- polar amino acids residues are not exposed enough to bind fats.
Substitution with the charged or polar amino acids Asp and Cys resulted in loss of transporter function while Met319 retained partial activity.
purpuratus); it also exhibits a high Gly/Ala ratio, a high percentage of polar amino acids without charge, and a slightly higher Ile/Leu ratio compared with other AIF sequences.
The second jump occurs when the group of predominantly small polar amino acids (DSNTHC) is joined with the group containing large polar amino acids (EKRQ).
NFPA yielded good retention (retention time, 6-8 min) and peak shape for the polar amino acids CML and CEL.