Selective detection of mobile amino acid resonances of chloroplast ATP synthase by proton spin-echo NMR
Author:
Publisher
American Chemical Society (ACS)
Subject
Biochemistry
Link
https://pubs.acs.org/doi/pdf/10.1021/bi00341a025
Reference26 articles.
1. Abragam, A. (1961) The Principles of Nuclear Magnetism, pp58-63, Oxford University Press, Oxford.
2. Adenosine triphosphatase from rat liver mitochondria. Crystallization and x-ray diffraction studies of the F1-component of the enzyme.
3. Structure of the mitochondrial F1 ATPase at 9-A resolution.
4. Modification of essential carboxyl residues in chloroplast coupling factor 1
5. Two different types of essential carboxyl groups in chloroplast coupling factor
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1. Lack of Effect of the Length of Oligoglycine- and Oligo(ethylene glycol)-Derived para-Substituents on the Affinity of Benzenesulfonamides for Carbonic Anhydrase II in Solution;Journal of the American Chemical Society;1994-06
2. High Mobility of N-Terminal Parts of A and B Subunits of Ricin;Journal of Biomolecular Structure and Dynamics;1989-06
3. Biochemical and proton NMR characterization of the isolated functional beta-subunit of coupling factor one from spinach chloroplasts;Biochemical and Biophysical Research Communications;1987-04
4. Proton Spin-Echo Spectra of the Isolated Beta Subunit of the CF0-CF1 ATP Synthase;Progress in Photosynthesis Research;1987
5. Interaction of a spin-labeled phenylalanine analog with normal and sickle hemoglobins: detection of site-specific interactions through spin-label-induced proton NMR relaxation;Biochemistry;1986-09-23
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