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@article{
 title = {Measuring protein self-association using pulsed-field-gradient NMR spectroscopy: Application to myosin light chain 2},
 type = {article},
 year = {1995},
 identifiers = {[object Object]},
 keywords = {CHAPS,Myosin light chain,Pulsed-field-gradient NMR,Self-association,Translational diffusion coefficient},
 pages = {321-328},
 volume = {6},
 websites = {http://link.springer.com/10.1007/BF00197813},
 month = {11},
 id = {07312f46-2ed1-3ece-97e7-7e8c71ba2bb5},
 created = {2020-12-17T05:29:47.718Z},
 file_attached = {false},
 profile_id = {a5a2ab6f-a8b5-3db6-97bc-618752ee4386},
 group_id = {bc1ab1d4-9e57-37e6-9fb5-435fca0ee9d2},
 last_modified = {2020-12-17T05:29:47.718Z},
 read = {false},
 starred = {false},
 authored = {false},
 confirmed = {true},
 hidden = {false},
 citation_key = {Dingley1995},
 source_type = {ARTICLE},
 notes = {cited By 118},
 private_publication = {false},
 abstract = {At the millimolar concentrations required for structural studies, NMR spectra of the calcium-binding protein myosin light chain 2 (MLC2) showed resonance line widths indicative of extensive self-association. Pulsed-field-gradient (PFG) NMR spectroscopy was used to examine whether MLC2 aggregation could be prevented by the zwitterionic bile salt derivative 3-[(3-cholamidopropyl)dimethylammonio]-1-propanesulfonate (CHAPS). PFG NMR measurements indicated that CHAPS was capable of preventing MLC2 self-association, but only at concentrations well above the critical micelle concentration of ∼7.5 mM. CHAPS was most effective at a concentration of 22.5 mM, where the apparent molecular mass of MLC2 correponded to a protein monomer plus seven molecules of bound detergent. The resolution and sensitivity of 2D 15N-1H HSQC spectra of MLC2 were markedly improved by the addition of 25 mM CHAPS, consistent with a reduction in aggregation following addition of the detergent. The average amide nitrogen T2 value for MLC2 increased from ∼30 ms in the absence of CHAPS to ∼56 ms in the presence of 25 mM CHAPS. The results of this study lead us to propose that PFG NMR spectroscopy can be used as a facile alternative to conventional techniques such as analytical ultracentrifugation for examining the self-association of biological macromolecules. © 1995 ESCOM Science Publishers B.V.},
 bibtype = {article},
 author = {Dingley, AndrewJ. and Mackay, JoelP. and Chapman, BogdanE. and Morris, MichaelB. and Kuchel, PhilipW. and Hambly, BrettD. and King, GlennF.},
 journal = {Journal of Biomolecular NMR},
 number = {3}
}