The tryptophan-rich domain of puroindoline is directly associated with the starch granule surface as judged by tryptic shaving and mass spectrometry

Wall, M.L., Wheeler, H.L., Huebsch, M.P., J. C. Smith (Jeffrey C.), Figeys, D. and Altosaar, I.

2010-09-01

Journal of Cereal Science , Volume 52 - Issue 2 p. 115- 120

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Keywords	ESI-MS, Isopropanol-sodium chloride solubilisation, Mass spectrometry, PIN-a, PIN-b, Puroindoline, SGAPs, Starch granule associated proteins, Starch granule surface, TRD, Trypsin, Tryptophan-rich domain, Wheat
Persistent URL	dx.doi.org/10.1016/j.jcs.2010.04.002
Journal	Journal of Cereal Science
Citation APA Style AAA Style APA Style Cell Style Chicago Style Harvard Style IEEE Style MLA Style Nature Style Vancouver Style American-Institute-of-Physics Style Council-of-Science-Editors Style BibTex Format Endnote Format RIS Format CSL Format DOIs only Format	Wall, M.L., Wheeler, H.L., Huebsch, M.P., Smith, J. C, Figeys, D., & Altosaar, I. (2010). The tryptophan-rich domain of puroindoline is directly associated with the starch granule surface as judged by tryptic shaving and mass spectrometry. Journal of Cereal Science, 52(2), 115–120. doi:10.1016/j.jcs.2010.04.002

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