Literature summary for 3.2.1.17 extracted from

Deshpande, A.; Nimsadkar, S.; Mande, S.C.
Effect of alcohols on protein hydration: crystallographic analysis of hen egg-white lysozyme in the presence of alcohols (2005), Acta Crystallogr. Sect. D, 61, 1005-1008.

Crystallization (Commentary)

Crystallization (Comment)	Organism
hanging drop method, crystals of native enzyme and enzyme in complex with various alcohols (ethanol, 1-butanol, 1-pentanol, 2-propanol or TFE). Although the alcohols have very little effect on the conformation of the overall protein structure, they profoundly affect protein hydration and disorder of the bound water. Increasing order of hydrophobicity of alcohols is directly proportional to the higher number of weakly bound waters in the protein	Gallus gallus

Crystallization (Comment)

Organism

hanging drop method, crystals of native enzyme and enzyme in complex with various alcohols (ethanol, 1-butanol, 1-pentanol, 2-propanol or TFE). Although the alcohols have very little effect on the conformation of the overall protein structure, they profoundly affect protein hydration and disorder of the bound water. Increasing order of hydrophobicity of alcohols is directly proportional to the higher number of weakly bound waters in the protein

Gallus gallus

Organism

Organism	UniProt	Comment	Textmining
Gallus gallus	P00698	-	-

Source Tissue

Source Tissue	Comment	Organism	Textmining
egg white	-	Gallus gallus	-

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Release 2023.1 (January 2023)