Author: Uversky, Vladimir N
Title: The alphabet of intrinsic disorder: II. Various roles of glutamic acid in ordered and intrinsically disordered proteins Document date: 2013_4_1
ID: 63gh2tg4_16_1
Snippet: the membrane leads of aspartic acid, asparagine, serine and threonine form hydrogen bonds with residues located close in sequence. 74 Finally, based on the analysis of α-helical propensity of a series of dodecapeptides containing alanine, asparagine, aspartate, glutamine, glutamate and serine at the N-terminus and arginine, lysine and alanine at the C-terminus, it was concluded that the α-helix-stabilizing abilities of these residues can be ran.....
Document: the membrane leads of aspartic acid, asparagine, serine and threonine form hydrogen bonds with residues located close in sequence. 74 Finally, based on the analysis of α-helical propensity of a series of dodecapeptides containing alanine, asparagine, aspartate, glutamine, glutamate and serine at the N-terminus and arginine, lysine and alanine at the C-terminus, it was concluded that the α-helix-stabilizing abilities of these residues can be ranged as follows: aspartate > asparagine > serine > glutamate > glutamine > alanine at the N-terminus and arginine > lysine > alanine at the C-terminus. 75 Glutamic acid and protein solubility. Based on the analysis of solubility-changing substitutions in proteins it has been pointed out that together with two other hydrophilic residues (aspartic acid and serine) glutamic acid contributes significantly more favorably to protein solubility than other hydrophilic residues (asparagine, glutamine, threonine, lysine and arginine). 76 Based on this observation, an important strategy for solubility enhancement was proposed, were the hydrophilic residues that do not contribute favorably to protein solubility can be replaced with the hydrophilic residues that contribute more favorably. 76
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