Premium
Glycine amide shielding on the aromatic surfaces of lysozyme: Implication for suppression of protein aggregation
Author(s) -
Ito Len,
Shiraki Kentaro,
Makino Masatomo,
Hasegawa Kazuya,
Kumasaka Takashi
Publication year - 2011
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/j.febslet.2011.01.008
Subject(s) - lysozyme , chemistry , crystallization , protein aggregation , amide , glycine , protein crystallization , biophysics , protein structure , resolution (logic) , molecule , amino acid , stereochemistry , crystallography , biochemistry , organic chemistry , biology , artificial intelligence , computer science
Glycine amide (GlyAd), a typically amidated amino acid, is a versatile additive that suppresses protein aggregation during refolding, heat treatment, and crystallization. In spite of its effectiveness, the exact mechanism by which GlyAd suppresses protein aggregation remains to be elucidated. Here, we show the crystal structure of the GlyAd–lysozyme complex by high resolution X‐ray crystallographic analysis at a 1.05 Å resolution. GlyAd bound to the lysozyme surface near aromatic residues and decreased the amount of bound waters and increased the mobility of protein. Arg and GlyAd molecules are different in binding sites and patterns from glycerol and related compounds, indicating that decreasing hydrophobic patches might be involved in suppression of protein aggregation.