November 1, 2001
Journal Article

On the Nature of Conformational Openings: Native and Unfolded-State Hydrogen and Thiol-Disulfide Exchange Studies of Ferric Aquomyoglobin

Abstract

Determining the structures of partially folded protein forms, and their order in a kinetic folding Present address: Z. Feng, University of Califomia San mechanism, is a major goal of protein folding stu- Diego, Section of Neurobiology, 9500 Gilman Drive, La dies. To this end, native-state amide hydrogen Jolla, CA 92093, USA. exchange (HX) has ~roven to be a particularly Abbreviations used: HX, hydrogen exchange; SX, powerful approach.I- I It has provided a detailed thiol-disu1fi~e exchange; AMb, ~erric myoglobin with. and unprecedented view of the structures and free w~ter coordinated to the heme lYon; apoMb, myoglobm energies of sparsely populated intermediates that WIth the .hem~ group removed;. MbCO, ferrous is not obtainable by other techniques. Despite its myoglobm WIth carbon monoXIde bound to the heme.1

Revised: November 20, 2003 | Published: November 1, 2001

Citation

Feng X., M.C. Butler, S.L. Alam, and S.N. Loh. 2001. On the Nature of Conformational Openings: Native and Unfolded-State Hydrogen and Thiol-Disulfide Exchange Studies of Ferric Aquomyoglobin. Journal of Molecular Biology 314, no. 1:153-166.