Proton magnetic resonance spectroscopy of histidine residues in proteins
Author:
Publisher
Elsevier BV
Subject
Cell Biology,Molecular Biology,Biochemistry,Biophysics
Reference8 articles.
1. Structure of Hen Egg-White Lysozyme: A Three-dimensional Fourier Synthesis at 2 Å Resolution
2. Structural Studies of Ribonuclease. XXIV. The Application of Nuclear Magnetic Resonance Spectroscopy to Distinguish between the Histidine Residues of Ribonuclease1
3. USE OF GLASS ELECTRODES TO MEASURE ACIDITIES IN DEUTERIUM OXIDE1,2
4. Nuclear Magnetic Resonance Studies of Proteins
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1. LINE WIDTHS OF PROTON MAGNETIC RESONANCE SPECTRA OF PROTEINS IN SOLUTION;International Journal of Protein Research;2009-01-09
2. Pharmaceutical Applications of NMR;Annual Reports on NMR Spectroscopy;1996
3. 1H-NMR Study on the Structure of Lysozyme from Guinea Hen Egg White;The Journal of Biochemistry;1991-12
4. Heteronuclear 2D NMR studies of an engineered insulin monomer: assignment and characterization of the receptor-binding surface by selective deuterium and carbon-13 labeling with application to protein design;Biochemistry;1991-07
5. Sequence-specific 1H-NMR assignments for the aromatic region of several biologically active, monomeric insulins including native human insulin;Biochimica et Biophysica Acta (BBA) - Molecular Cell Research;1990-06
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