Since the initial reports showing the ability of electrospray ionization mass spectrometry (ESI-MS) to study intact noncovalent biomolecular complexes, an increasing number of uses for this technique in studying biochemical systems is emerging. We have investigated the ability of ESI-MS to character
Metal-Binding Properties of Human Centrin-2 Determined by Micro-Electrospray Ionization Mass Spectrometry and UV Spectroscopy
β Scribed by Theodore A. Craig; Linda M. Benson; H. Robert Bergen III; Sergei Y. Venyaminov; Jeffrey L. Salisbury; Zachary C. Ryan; James R. Thompson; Justin Sperry; Michael L. Gross; Rajiv Kumar
- Book ID
- 108158334
- Publisher
- Elsevier Science
- Year
- 2006
- Tongue
- English
- Weight
- 528 KB
- Volume
- 17
- Category
- Article
- ISSN
- 1044-0305
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2Ψ -binding loops bind 0 or 1 Ca 2Ψ ion per protein molecule, depending on the degree of inactivation. These findings fully agree with previously reported results obtained by flow dialysis experiments. The RP-HPLC desalted metal-free proteins were analyzed in 10 mM ammonium acetate at pH 7.0. The ex
## Abstract Electrospray ionization Fourier transform ion cyclotron resonance mass spectrometry (ESIβFTICRMS) was used to investigate metal ion interactions of the 18 amino acid peptide fragment B18 (LGLLLRHLRHHSNLLANI), derived from the membraneβassociated protein bindin. The peptide sequence B18