Real-time NMR kinetic studies provide global and residue-specific information on the non-cooperative unfolding of the beta-trefoil protein, interleukin-1beta.
The interleukin-1beta (IL-1beta) structural motif is a beta-trefoil super fold created by six two-stranded beta-hairpins. Turns are thus particularly important in creating the topology and the arrangement of beta-strands in this structural motif. In contrast to the signals observed in optical studies, real-time NMR kinetic investigations of the denaturant-induced unfolding of interleukin-1beta provide direct, global, and residue-specific information on the structural nature of the unfolding reaction. Heterogeneity in the individual amino acid residue kinetics reveals a rugged unfolding landscape. The relative kinetic stability of native-like turns supports low temperature molecular dynamics predictions of turn-controlled unfolding.
Roy
Melinda
M
Department of Chemistry and Biochemistry, University of California-San Diego, La Jolla, CA 92093-0359, USA.
Jennings
Patricia A
PA
D000596:Amino Acids / Q000032:analysis; D007375:Interleukin-1 / Q000737:chemistry*; D007700:Kinetics; D008958:Models, Molecular; D019906:Nuclear Magnetic Resonance, Biomolecular; D011489:Protein Denaturation; D017510:Protein Folding; D017433:Protein Structure, Secondary; D014508:Urea / Q000737:chemistry
D000596:Amino Acids; D007375:Interleukin-1; D014508:Urea