Fluorescence spectra study the perturbations of CopC native fold by 2-p-toluidinynaphthalene-6-sulfonate.
2-p-Toluidinynaphthalene-6-sulfonate (TNS) was discovered to perturb native fold of CopC protein and to induce loss of biological activity to some extent which was dependent on TNS concentration. Hydrophobic and electrostatic interactions were revealed to account for the perturbation by comparison with some analogy. TNS, with far low concentration of 10(-5) to 10(-4)M, is presented as a denaturant. So TNS should be deliberated in detecting macromolecular conformation change as single evidence at higher concentration.
Li
Huiqing
H
Institute of Molecular Science, Key Laboratory of Chemical Biology and Molecular Engineering of Ministry of Education, Shanxi University, Taiyuan, Shanxi 030006, PR China.
Zhao
Yaqin
Y
Zhen
Xiaoyan
X
Yang
Binsheng
B
D001426:Bacterial Proteins / Q000737:chemistry*; D003300:Copper / Q000737:chemistry; D006863:Hydrogen-Ion Concentration; D057927:Hydrophobic and Hydrophilic Interactions; D009282:Naphthalenesulfonates / Q000737:chemistry*; D017433:Protein Structure, Secondary; D012967:Sodium Dodecyl Sulfate / Q000737:chemistry; D013050:Spectrometry, Fluorescence; D055672:Static Electricity; D017186:Titrimetry
D001426:Bacterial Proteins; C071265:CopC protein, Bacteria; D009282:Naphthalenesulfonates; D012967:Sodium Dodecyl Sulfate; C009497:2-(4-toluidino)-6-naphthalenesulfonic acid; D003300:Copper