Measuring protein self-association using pulsed-field-gradient NMR spectroscopy: Application to myosin light chain 2. Dingley, A., Mackay, J., Chapman, B., Morris, M., Kuchel, P., Hambly, B., & King, G. Journal of Biomolecular NMR, 6(3):321-328, 11, 1995. ![Measuring protein self-association using pulsed-field-gradient NMR spectroscopy: Application to myosin light chain 2 [link]](https://bibbase.org/img/filetypes/link.svg "link")
Website abstract bibtex 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.
@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 = {256d67a2-fff2-3bc9-904b-268fe2078087},
created = {2020-10-01T06:20:40.962Z},
file_attached = {false},
profile_id = {45e2f77d-7a48-31e0-99de-4a07a154b051},
group_id = {c2dc1a38-fc29-3f20-8d91-e4e1a13d85ae},
last_modified = {2020-10-29T21:44:45.426Z},
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}
}
Downloads: 0
{"_id":"6oc2qjuPCZCRhRkDW","bibbaseid":"dingley-mackay-chapman-morris-kuchel-hambly-king-measuringproteinselfassociationusingpulsedfieldgradientnmrspectroscopyapplicationtomyosinlightchain2-1995","authorIDs":["ZTncL5PqZZ6RafCsL"],"author_short":["Dingley, A.","Mackay, J.","Chapman, B.","Morris, M.","Kuchel, P.","Hambly, B.","King, G."],"bibdata":{"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":"256d67a2-fff2-3bc9-904b-268fe2078087","created":"2020-10-01T06:20:40.962Z","file_attached":false,"profile_id":"45e2f77d-7a48-31e0-99de-4a07a154b051","group_id":"c2dc1a38-fc29-3f20-8d91-e4e1a13d85ae","last_modified":"2020-10-29T21:44:45.426Z","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","bibtex":"@article{\n title = {Measuring protein self-association using pulsed-field-gradient NMR spectroscopy: Application to myosin light chain 2},\n type = {article},\n year = {1995},\n identifiers = {[object Object]},\n keywords = {CHAPS,Myosin light chain,Pulsed-field-gradient NMR,Self-association,Translational diffusion coefficient},\n pages = {321-328},\n volume = {6},\n websites = {http://link.springer.com/10.1007/BF00197813},\n month = {11},\n id = {256d67a2-fff2-3bc9-904b-268fe2078087},\n created = {2020-10-01T06:20:40.962Z},\n file_attached = {false},\n profile_id = {45e2f77d-7a48-31e0-99de-4a07a154b051},\n group_id = {c2dc1a38-fc29-3f20-8d91-e4e1a13d85ae},\n last_modified = {2020-10-29T21:44:45.426Z},\n read = {false},\n starred = {false},\n authored = {false},\n confirmed = {true},\n hidden = {false},\n citation_key = {Dingley1995},\n source_type = {ARTICLE},\n notes = {cited By 118},\n private_publication = {false},\n 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.},\n bibtype = {article},\n author = {Dingley, AndrewJ. and Mackay, JoelP. and Chapman, BogdanE. and Morris, MichaelB. and Kuchel, PhilipW. and Hambly, BrettD. and King, GlennF.},\n journal = {Journal of Biomolecular NMR},\n number = {3}\n}","author_short":["Dingley, A.","Mackay, J.","Chapman, B.","Morris, M.","Kuchel, P.","Hambly, B.","King, G."],"urls":{"Website":"http://link.springer.com/10.1007/BF00197813"},"biburl":"https://bibbase.org/service/mendeley/a5a2ab6f-a8b5-3db6-97bc-618752ee4386","bibbaseid":"dingley-mackay-chapman-morris-kuchel-hambly-king-measuringproteinselfassociationusingpulsedfieldgradientnmrspectroscopyapplicationtomyosinlightchain2-1995","role":"author","keyword":["CHAPS","Myosin light chain","Pulsed-field-gradient NMR","Self-association","Translational diffusion coefficient"],"metadata":{"authorlinks":{"mackay, j":"https://mackaymatthewslab.org/"}}},"bibtype":"article","creationDate":"2020-08-19T06:33:00.916Z","downloads":0,"keywords":["chaps","myosin light chain","pulsed-field-gradient nmr","self-association","translational diffusion coefficient"],"search_terms":["measuring","protein","self","association","using","pulsed","field","gradient","nmr","spectroscopy","application","myosin","light","chain","dingley","mackay","chapman","morris","kuchel","hambly","king"],"title":"Measuring protein self-association using pulsed-field-gradient NMR spectroscopy: Application to myosin light chain 2","year":1995,"biburl":"https://bibbase.org/service/mendeley/a5a2ab6f-a8b5-3db6-97bc-618752ee4386","dataSources":["QNo3CKhtog6c3sh7Y","ya2CyA73rpZseyrZ8"]}