Direct energy transfer to study the 3D structure of non-native proteins: AGH complex in molten globule state of apomyoglobin

The direct energy transfer technique was modified and appliedto probe the relative localization of apomyoglobin A-, G- andH-helixes, which are partly protected from deuterium exchangein the equilibrium molten globule state and in the molten globule-likekinetic intermediate. The non-radiative transfer of tryptophanelectronic energy to 3-nitrotyrosine was studied in differentconformational states of apomyoglobin (native, molten globule,unfolded) and interpreted in terms of average distances betweengroups of the protein chain. The experimental data show thatthe distance between the middle of A-helix and the N-terminusof G-helix as well as the distance between the middle of theA-helix and the C-terminus of the H-helix in the molten globulestate are close to those in the native state. This is a strongargument in favor of similarity of the overall architectureof the molten globule and native states.