NMR assignments as a basis for structural characterization of denatured states of globular proteins
- 31 December 1994
- journal article
- Published by Elsevier in Current Opinion in Structural Biology
- Vol. 4 (1) , 93-99
- https://doi.org/10.1016/s0959-440x(94)90065-5
Abstract
No abstract availableKeywords
This publication has 23 references indexed in Scilit:
- Peptide models of protein folding initiation sites. 1. Secondary structure formation by peptides corresponding to the G- and H-helixes of myoglobinBiochemistry, 1993
- Methodological advances in protein NMRAccounts of Chemical Research, 1993
- A general method for assigning NMR spectra of denatured proteins using 3D HC(CO)NH-TOCSY triple resonance experimentsJournal of Biomolecular NMR, 1993
- NMR Determination of Residual Structure in a Urea-Denatured Protein, the 434-RepressorScience, 1992
- Folding of peptide fragments comprising the complete sequence of proteinsJournal of Molecular Biology, 1992
- 1H,15N and13C NMR assignments of the 434 repressor fragments 1–63 and 44–63 unfolded in 7 M ureaFEBS Letters, 1992
- An N-terminal fragment of barnase has residual helical structure similar to that in a refolding intermediateJournal of Molecular Biology, 1992
- Overcoming the overlap problem in the assignment of proton NMR spectra of larger proteins by use of three-dimensional heteronuclear proton-nitrogen-15 Hartmann-Hahn-multiple quantum coherence and nuclear Overhauser-multiple quantum coherence spectroscopy: application to interleukin 1.beta.Biochemistry, 1989
- Individual assignments of the methyl resonances in the proton nuclear magnetic resonance spectrum of the basic pancreatic trypsin inhibitorBiochemistry, 1978
- Manifestations of the tertiary structures of proteins in high-frequency nuclear magnetic resonanceJournal of the American Chemical Society, 1967