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 1.05Å 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.
journal_name
FEBS Lettjournal_title
FEBS lettersauthors
Ito L,Shiraki K,Makino M,Hasegawa K,Kumasaka Tdoi
10.1016/j.febslet.2011.01.008subject
Has Abstractpub_date
2011-02-04 00:00:00pages
555-60issue
3eissn
0014-5793issn
1873-3468pii
S0014-5793(11)00029-9journal_volume
585pub_type
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