Mass spectrometry of intact V-type ATPases reveals bound lipids and the effects of nucleotide binding.

Zhou M, Morgner N, Barrera NP, Politis A, Isaacson SC, Matak-Vinkovic D, Murata T, Bernal RA, Stock D, Robinson CV. Mass spectrometry of intact V-type ATPases reveals bound lipids and the effects of nucleotide binding. Science. 2011 Oct 21; 334(6054):380-385.

View in: PubMed

subject areas

Adenosine Triphosphatases
Adenosine Triphosphate
Bacterial Proteins
Binding Sites
Cardiolipins
Enterococcus
Hydrolysis
Mass Spectrometry
Membrane Lipids
Models, Molecular
Phosphatidylethanolamines
Protein Conformation
Protein Multimerization
Protein Structure, Tertiary
Protein Subunits
Spectrometry, Mass, Electrospray Ionization
Thermus thermophilus
Vacuolar Proton-Translocating ATPases

authors with profiles

Ricardo Bernal

RCMI CC is supported by the National Institute on Minority Health and Health Disparities, National Institutes of Health (NIH), through Grant Number U24MD015970. The contents of this site are solely the responsibility of the authors and do not necessarily represent the official views of the NIH

For technical support please contact support