Title of article :
Acyl-coenzyme A binding protein (ACBP)
Author/Authors :
Birthe B. Kragelund، نويسنده , , Jens Knudsen، نويسنده , , Flemming M. Poulsen، نويسنده ,
Pages :
12
From page :
150
To page :
161
Abstract :
Acyl-coenzyme A binding proteins are known from a large group of eukaryote species and to bind a long chain length acyl-CoA ester with very high affinity. Detailed biochemical mapping of ligand binding properties has been obtained as well as in-depth structural studies on the bovine apo-protein and of the complex with palmitoyl-CoA using NMR spectroscopy. In the four α-helix bundle structure, a set of 21 highly conserved residues present in more that 90% of all known sequences of acyl-coenzyme A binding proteins constitutes three separate mini-cores. These residues are predominantly located at the helix-helix interfaces. From studies of a large set of mutant proteins the role of the conserved residues has been related to structure, function, folding and stability.
Keywords :
Two-state folding , Four-helix bundle , nuclear magnetic resonance
Journal title :
Astroparticle Physics
Record number :
568307
Link To Document :
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