期刊
FEBS LETTERS
卷 585, 期 3, 页码 555-560出版社
WILEY
DOI: 10.1016/j.febslet.2011.01.008
关键词
Glycine amide; Crystal structure; Lysozyme; Protein aggregation; Accessible surface area
资金
- Japan Science Society
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 angstrom 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. (C) 2011 Federation of European Biochemical Societies. Published by Elsevier B.V. All rights reserved.
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