Structure, stability and dynamics of norovirus P domain derived protein complexes studied by native mass spectrometry.

Bereszczak, Jessica Z; Barbu, Ioana M; Tan, Ming; Xia, Ming; Jiang, Xi; van Duijn, Esther; Heck, Albert J R

Bereszczak, Jessica Z; Barbu, Ioana M; Tan, Ming; Xia, Ming; Jiang, Xi; van Duijn, Esther; Heck, Albert J R.

Affiliation

Bereszczak JZ; Biomolecular Mass Spectrometry and Proteomics Group, Bijvoet Center for Biomolecular Research and Utrecht Institute of Pharmaceutical Sciences, Utrecht University, Utrecht, The Netherlands.

J Struct Biol ; 177(2): 273-82, 2012 Feb.

Article in En | MEDLINE | ID: mdl-22266117

Subject(s)

Capsid Proteins/chemistry; Norovirus/physiology; Blood Group Antigens/chemistry; Dithiothreitol/chemistry; Host-Pathogen Interactions; Humans; Hydrogen-Ion Concentration; Molecular Weight; Multiprotein Complexes/chemistry; Protein Binding; Protein Stability; Protein Structure, Quaternary; Reducing Agents/chemistry; Saliva/chemistry; Spectrometry, Mass, Electrospray Ionization; Tandem Mass Spectrometry

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Full text: 1 Database: MEDLINE Main subject: Norovirus / Capsid Proteins Type of study: Prognostic_studies Limits: Humans Language: En Journal: J Struct Biol Journal subject: BIOLOGIA MOLECULAR Year: 2012 Type: Article Affiliation country: Netherlands

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