title: Subunit exchange rates in Hepatitis B virus capsids are geometry- and temperature-dependent.
abstract: Native tandem mass spectrometry reveals marked differences in the rates at which the two polymorphic forms of the HBV capsid exchange dimeric subunits with the soluble pool.
authors.affiliation: Biomolecular Mass Spectrometry and Proteomics Group, Bijvoet Center for Biomolecular Research and Utrecht Institute for Pharmaceutical Sciences, University of Utrecht, Padualaan 8, 3584 CH Utrecht, The Netherlands.
authors.forename: Charlotte
authors.initials: C
authors.lastname: Uetrecht
authors.forename: Norman R
authors.initials: NR
authors.lastname: Watts
authors.forename: Stephen J
authors.initials: SJ
authors.lastname: Stahl
authors.forename: Paul T
authors.initials: PT
authors.lastname: Wingfield
authors.forename: Alasdair C
authors.initials: AC
authors.lastname: Steven
authors.forename: Albert J R
authors.initials: AJ
authors.lastname: Heck
mesh_terms: D036022:Capsid Proteins / Q000737:chemistry*; D019281:Dimerization; D006515:Hepatitis B virus / Q000378:metabolism*; D006863:Hydrogen-Ion Concentration; D013058:Mass Spectrometry; D021122:Protein Subunits / Q000737:chemistry; D013696:Temperature
chemical_list: D036022:Capsid Proteins; D021122:Protein Subunits