Title : Effects of guanidinium ions on the conformational structure of glucose oxidase studied by electrochemistry, spectroscopy, and theoretical calculations: towards developing a chemical-induced protein conformation assay.

Pub. Date : 2012 Apr 28

PMID : 22415204






3 Functional Relationships(s)
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Compound Name
Protein Name
Organism
1 The interaction of GOx with the chemical denaturant resulted in a disturbance of the structure of the flavin prosthetic group (FAD moiety) that induced the moiety to become less exposed to solvent than that in the native protein molecule. Flavin-Adenine Dinucleotide hydroxyacid oxidase 1 Homo sapiens
2 MD simulations and DFT calculations revealed that Gdm(+) ions could enter the active pocket of the GOx molecule and interact with the FAD group, leading to a significant alteration in the structural characteristics and hydrogen bond networks formed between FAD and the surrounding amino acid residues. Flavin-Adenine Dinucleotide hydroxyacid oxidase 1 Homo sapiens
3 MD simulations and DFT calculations revealed that Gdm(+) ions could enter the active pocket of the GOx molecule and interact with the FAD group, leading to a significant alteration in the structural characteristics and hydrogen bond networks formed between FAD and the surrounding amino acid residues. Flavin-Adenine Dinucleotide hydroxyacid oxidase 1 Homo sapiens