Glycine amide shielding on the aromatic surfaces of lysozyme: implication for suppression of protein aggregation |
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Authors: | Ito Len Shiraki Kentaro Makino Masatomo Hasegawa Kazuya Kumasaka Takashi |
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Affiliation: | aJapan Synchrotron Radiation Research Institute (SPring-8), 1-1-1 Kouto, Sayo, Hyogo 679-5198, Japan;bInstitute of Applied Physics, University of Tsukuba, 1-1-1 Tennodai, Tsukuba, Ibaraki 305-8573, Japan |
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Abstract: | 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. |
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Keywords: | Glycine amide Crystal structure Lysozyme Protein aggregation Accessible surface area |
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