Sequential assignment of the proton nuclear magnetic resonance spectrum of barnase
- 14 August 1990
- journal article
- research article
- Published by American Chemical Society (ACS) in Biochemistry
- Vol. 29 (32), 7425-7432
- https://doi.org/10.1021/bi00484a011
Abstract
Two-dimensional nuclear magnetic resonance spectroscopy has been used to study the bacterial ribonuclease barnase (MW 12382). Resonance assignments have been made for protons in all of the 110 residues. Analysis of medium- and long-range contracts in NOESY spectra has demonstrated that the major elements of secondary structure in barnase in solution are essentially identical with those found in the crystal structure.This publication has 7 references indexed in Scilit:
- Kinetic characterization of the recombinant ribonuclease from Bacillus amyloliquefaciens (barnase) and investigation of key residues in catalysis by site-directed mutagenesisBiochemistry, 1989
- Energetics of complementary side chain packing in a protein hydrophobic coreBiochemistry, 1989
- A proton nuclear magnetic resonance study of the antihypertensive and antiviral protein BDS-I from the sea anemone Anemonia sulcata: sequential and stereospecific resonance assignment and secondary structureBiochemistry, 1989
- Properties of a 19‐kDa Zn2+‐binding protein and sequence of the Zn2+‐binding domainsEuropean Journal of Biochemistry, 1988
- Expression of Bacillus amyloliquefaciens extracellular ribonuclease (barnase) in Escherichia coli following an inactivating mutationGene, 1987
- Improved spectral resolution in COSY 1H NMR spectra of proteins via double quantum filteringBiochemical and Biophysical Research Communications, 1983
- A two-dimensional nuclear Overhauser enhancement (2D NOE) experiment for the elucidation of complete proton-proton cross-relaxation networks in biological macromoleculesBiochemical and Biophysical Research Communications, 1980