Expressed protein ligation for metalloprotein design and engineering.
作者： Kevin M. Clark , Wilfred A. van der Donk , Yi Lu
DOI: 10.1016/S0076-6879(09)62005-X
关键词: Metalloprotein 、 Selenocysteine 、 Azurin 、 Cysteine 、 Protein splicing 、 Biochemistry 、 Protein engineering 、 Amino acid 、 Binding site 、 Chemistry
摘要: Abstract Metalloproteins contain highly specialized metal‐binding sites that are designed to accept specific metal ions maintain correct function. Although many of the have been modified with success, relative paucity functional group availability within proteinogenic amino acids can sometimes leave open questions about functions binding ligands. Attaining a more thorough analysis individual acid function metalloproteins has realized using expressed protein ligation (EPL). Here we describe our recent efforts EPL incorporate nonproteinogenic cysteine and methionine analogues into type 1 copper site found in Pseudomonas aeruginosa azurin.
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