Tryptic proteol ysis of coupling factor-latent ATPase from Mycobacterium phlei. Theoretical modeling of structure-function relationships
Author:
Publisher
Elsevier BV
Subject
Cell Biology,Biochemistry,Biophysics
Reference22 articles.
1. Oxidative phosphorylation in fractionated bacterial systems XLIII. Coupling factors associated with the NAD+-linked electron transport pathway
2. Energy-transducing membrane-bound coupling factor-ATPase from Mycobacterium phlei. I. Purification, homogeneity, and properties
3. Effects of trypsin treatment on the structure and function of solubilized coupling factor-latent ATPase from Mycobacterium phlei
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1. The Proton-Translocating Membrane ATPase (F1F0) in Streptococcus faecalis (faecium);The Enzymes of Biological Membranes;1985
2. Electron microscopy of beef heart F1-ATPase crystals.;Journal of Biological Chemistry;1983-03
3. Polymorphism and conformational dynamics of F1-ATPases from bacterial membranes a model for the regulation of these enzymes on the basis of molecular plasticity;Biochimica et Biophysica Acta (BBA) - Reviews on Biomembranes;1982-05
4. Effect of proteolytic digestion on the Ca2+-ATPase activity and subunits of latent and thiol-activated chloroplast coupling factor 1.;Journal of Biological Chemistry;1982-05
5. Energy-Transducing Coupling Factor F0F1 from Mycobacterium phlei;Membranes and Transport;1982
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