Denaturation of Proteins: Single or Multiple Step Process?

摘要: WE have reported the nuclear magnetic resonance (NMR) spectra of eleven proteins covering a wide range molecular weights in five denaturing solvents1. With some exceptions (with disulphide bonds intact) appeared to behave solution as random coils, devoid non-covalent interactions. We thus defined by NMR spectroscopy particular denatured state (the unfolded state) and next step is study denaturation process brought about progressive addition denaturant native protein. At 60 MHz we can examine simultaneously six parameters (proton resonances) protein1. 220 many more resonances be observed, because much greater resolving power spectrometer2. Here direct attention whether single or multiple process; satisfactory answer has often been difficult obtain past3, but it prerequisite any meaningful thermodynamic denaturation.