Surface-induced dissociation of homotetramers with D2 symmetry yields their assembly pathways and characterizes the effect of ligand binding

Chemistry and Biology

Volumn 22, Issue 5, 2015, Pages 583-592

  Quintyn, Royston S ^a   Yan, Jing ^a   Wysocki, Vicki H ^a  

^a OHIO STATE UNIVERSITY   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

DIMER; LIGAND; MONOMER; STREPTAVIDIN; TETRAMER; AVIDIN; NEUTRAVIDIN; PREALBUMIN; PROTEIN; PROTEIN BINDING;

ARTICLE; BINDING SITE; COLLISIONALLY ACTIVATED DISSOCIATION; CRYSTAL STRUCTURE; DENATURATION; DIMERIZATION; DISSOCIATION; ENERGY; GAS; ION MOBILITY SPECTROMETRY; LIGAND BINDING; MASS SPECTROMETRY; PRIORITY JOURNAL; PROTEIN QUATERNARY STRUCTURE; SURFACE PROPERTY; TEMPERATURE; THERMOSTABILITY; CHEMICAL STRUCTURE; CHEMISTRY; ELECTROSPRAY MASS SPECTROMETRY; HIGH PERFORMANCE LIQUID CHROMATOGRAPHY; METABOLISM; PROTEIN DATABASE; PROTEIN MULTIMERIZATION;

AVIDIN; CHROMATOGRAPHY, HIGH PRESSURE LIQUID; DATABASES, PROTEIN; LIGANDS; MODELS, MOLECULAR; PREALBUMIN; PROTEIN BINDING; PROTEIN MULTIMERIZATION; PROTEIN STRUCTURE, QUATERNARY; PROTEINS; SPECTROMETRY, MASS, ELECTROSPRAY IONIZATION; STREPTAVIDIN;

EID: 84930090440     PISSN: 10745521     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.chembiol.2015.03.019     Document Type: Article

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