Studies of individual carbon sites of hemoglobins in solution by natural abundance carbon 13 nuclear magnetic resonance spectroscopy
Author:
Publisher
Elsevier BV
Subject
Cell Biology,Molecular Biology,Biochemistry
Reference25 articles.
1. Natural-abundance carbon-13 nuclear magnetic resonance studies in 20-mm sample tubes. Numerous single-carbon resonances of hen egg-white lysozyme
2. Cytochrome c. Observation of Numerous Single-Carbon Sites of the Reduced and Oxidized Species by Means of Natural-Abundance 13C Nuclear Magnetic Resonance Spectroscopy
3. CARBON-13 FOURIER TRANSFORM NMR STUDIES IN 20 mm SAMPLE TUBES: OBSERVATION OF INDIVIDUAL CARBON SITES IN PROTEINS
4. Studies of individual carbon sites of proteins in solution by natural abundance carbon 13 nuclear magnetic resonance spectroscopy. Relaxation behavior
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1. Proteins and Model Systems: Spectral Analyses;Encyclopedia of Magnetic Resonance;2009-09-15
2. Protein Structure Refinement Using 13Cα Chemical Shift Tensors;Journal of the American Chemical Society;2009-01-05
3. A Solid State 13C NMR, Crystallographic, and Quantum Chemical Investigation of Phenylalanine and Tyrosine Residues in Dipeptides and Proteins;Journal of the American Chemical Society;2007-05-17
4. The Application of High Resolution Nuclear Magnetic Resonance to Biological Systems;Methods of Biochemical Analysis;2006-10-31
5. Studies of Protein Structure by NMR Spectroscopy;Annual Reports on NMR Spectroscopy;1995
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