Analysis of tryptophan surface accessibility in proteins by MALDI-TOF mass spectrometry.
Strohalm
Martin
M
Department of Biochemistry and Microbiology, Institute of Chemical Technology, Prague 6, 166 28, Czech Republic. martin.strohalm@vscht.cz
Santrůcek
Jirí
J
Hynek
Radovan
R
Kodícek
Milan
M
D015077:2-Hydroxy-5-nitrobenzyl Bromide / Q000737:chemistry*; D000818:Animals; D001665:Binding Sites; D002417:Cattle; D045304:Cytochromes c / Q000737:chemistry*; D006736:Horses; D006801:Humans; D009113:Muramidase / Q000737:chemistry*; D009211:Myoglobin / Q000737:chemistry*; D011485:Protein Binding; D012709:Serum Albumin / Q000737:chemistry*; D019032:Spectrometry, Mass, Matrix-Assisted Laser Desorption-Ionization / Q000379:methods*; D014364:Tryptophan / Q000737:chemistry*
D009211:Myoglobin; D012709:Serum Albumin; D015077:2-Hydroxy-5-nitrobenzyl Bromide; D014364:Tryptophan; D045304:Cytochromes c; C421864:hen egg lysozyme; D009113:Muramidase