title: Structural and dynamical insights into the molten-globule form of ovalbumin.
abstract: Ovalbumin is a 45 kDa egg-white glycoprotein which belongs to the class of serpin superfamily. We have studied the structural properties of both native and partially unfolded molten-globule forms of ovalbumin using a diverse array of spectroscopic tools. Time-resolved fluorescence measurements provided important structural and dynamical insights into the native and molten-globule states. Fluorescence anisotropy decay analysis indicated that there is a conformational swelling from the native to the molten-globule form of ovalbumin. We have also carried out red-edge excitation shift measurements to probe the dipolar relaxation dynamics around the intrinsic tryptophan residues. Additionally, stopped-flow fluorescence experiments revealed that the conformational transition from the native to the molten-globule form proceeds in a stepwise manner involving a burst-phase with a submillisecond conformational change followed by biphasic slower conformational reorganizations on the millisecond time scale leading to the final molten-globule state.
authors.affiliation: Indian Institute of Science Education and Research (IISER), Knowledge City, SAS Nagar, Mohali, India. mily@iisermohali.ac.in
authors.forename: Mily
authors.initials: M
authors.lastname: Bhattacharya
authors.forename: Samrat
authors.initials: S
authors.lastname: Mukhopadhyay
mesh_terms: D002942:Circular Dichroism; D006863:Hydrogen-Ion Concentration; D007700:Kinetics; D010047:Ovalbumin / Q000737:chemistry*; D011489:Protein Denaturation; D017433:Protein Structure, Secondary; D017434:Protein Structure, Tertiary; D013050:Spectrometry, Fluorescence
chemical_list: D010047:Ovalbumin