NMR Determination of Residual Structure in a Urea-Denatured Protein, the 434-Repressor
- 11 September 1992
- journal article
- Published by American Association for the Advancement of Science (AAAS) in Science
- Vol. 257 (5076) , 1559-1563
- https://doi.org/10.1126/science.1523410
Abstract
A nuclear magnetic resonance (NMR) structure determination is reported for the polypeptide chain of a globular protein in strongly denaturing solution. Nuclear Overhauser effect (NOE) measurements with a 7 molar urea solution of the amino-terminal 63-residue domain of the 434-repressor and distance geometry calculations showed that the polypeptide segment 54 to 59 forms a hydrophobic cluster containing the side chains of Val 54 , Val 56 , Trp 58 , and Leu 59 . This residual structure in the urea-unfolded protein is related to the corresponding region of the native, folded protein by simple rearrangements of the residues 58 to 60. Based on these observations a model for the early phase of refolding of the 434-repressor(1-63) is proposed.Keywords
This publication has 23 references indexed in Scilit:
- 1H,15N and13C NMR assignments of the 434 repressor fragments 1–63 and 44–63 unfolded in 7 M ureaFEBS Letters, 1992
- Determination of the nuclear magnetic resonance solution structure of the DNA-binding domain (residues 1 to 69) of the 434 repressor and comparison with the X-ray crystal structureJournal of Molecular Biology, 1992
- Proton-proton Overhauser effects of receptor-bound cyclosporin A observed with the use of a heteronuclear-resolved half-filter experimentJournal of the American Chemical Society, 1991
- Characterization of protein folding intermediates: Current Opinion in Structural Biology 1991, 1:22–27Current Opinion in Structural Biology, 1991
- Efficient computation of three-dimensional protein structures in solution from nuclear magnetic resonance data using the program DIANA and the supporting programs CALIBA, HABAS and GLOMSAJournal of Molecular Biology, 1991
- Restrained energy refinement with two different algorithms and force fields of the structure of the α‐amylase inhibitor tendamistat determined by nmr in solutionBiopolymers, 1990
- Stereospecific assignment of the methyl 1H NMR lines of valine and leucine in polypeptides by nonrandom 13C labellingFEBS Letters, 1989
- Structure of the amino-terminal domain of phage 434 represser at 2.0 Å resolutionJournal of Molecular Biology, 1989
- Pseudo-structures for the 20 common amino acids for use in studies of protein conformations by measurements of intramolecular proton-proton distance constraints with nuclear magnetic resonanceJournal of Molecular Biology, 1983
- 1H‐nmr parameters of the common amino acid residues measured in aqueous solutions of the linear tetrapeptides H‐Gly‐Gly‐X‐L‐Ala‐OHBiopolymers, 1979