Structure and properties of a complex of α-synuclein and a single-domain camelid antibody

Journal of Molecular Biology

Volumn 402, Issue 2, 2010, Pages 326-343

  De Genst, Erwin J ^a,b   Guilliams, Tim ^a   Wellens, Joke ^b,c   Day, Elizabeth M ^a,b   Waudby, Christopher A ^a,b   Meehan, Sarah ^a   Dumoulin, Mireille ^a,b   Hsu, Shang Te Danny ^a   Cremades, Nunilo ^a   Verschueren, Koen H G ^b,c   Pardon, Els ^b,c   Wyns, Lode ^b,c   Steyaert, Jan ^b,c   Christodoulou, John ^a,b   Dobson, Christopher M ^a  

^a UNIVERSITY OF CAMBRIDGE   (United Kingdom)

^b VRIJE UNIVERSITEIT BRUSSEL   (Belgium)

^c DEPARTMENT OF PLANT SYSTEMS BIOLOGY   (Belgium)

Author keywords

Amyloid; Nanobody; Nuclear magnetic resonance; X ray crystallography; synuclein

Indexed keywords

ALPHA SYNUCLEIN; MONOMER; NBSYN2 ANTIBODY; PROTEIN ANTIBODY; UNCLASSIFIED DRUG; ANTIBODY; PEPTIDE LIBRARY; PROTEIN BINDING;

ARTICLE; ARTIODACTYLA; BINDING AFFINITY; CALORIMETRY; CARBOXY TERMINAL SEQUENCE; CONTROLLED STUDY; CROSS LINKING; CRYSTAL STRUCTURE; IN VITRO STUDY; IN VIVO STUDY; MORPHOLOGY; NONHUMAN; NUCLEAR MAGNETIC RESONANCE SPECTROSCOPY; PH; PHAGE DISPLAY; PRIORITY JOURNAL; PROTEIN AGGREGATION; PROTEIN BINDING; PROTEIN DOMAIN; PROTEIN INTERACTION; PROTEIN SECONDARY STRUCTURE; PROTEIN STRUCTURE; THERMODYNAMICS; THERMOSTABILITY; X RAY CRYSTALLOGRAPHY; ANIMAL; ANTIBODY AFFINITY; CHEMICAL STRUCTURE; CHEMISTRY; KINETICS; METABOLISM; NUCLEAR MAGNETIC RESONANCE; PEPTIDE LIBRARY; PROTEIN ANALYSIS; PROTEIN DENATURATION; PROTEIN MULTIMERIZATION; PROTEIN QUATERNARY STRUCTURE; TRANSMISSION ELECTRON MICROSCOPY;

CAMELIDAE;

ALPHA-SYNUCLEIN; ANIMALS; ANTIBODIES; ANTIBODY AFFINITY; CALORIMETRY; CAMELIDS, NEW WORLD; CRYSTALLOGRAPHY, X-RAY; KINETICS; MICROSCOPY, ELECTRON, TRANSMISSION; MODELS, MOLECULAR; NUCLEAR MAGNETIC RESONANCE, BIOMOLECULAR; PEPTIDE LIBRARY; PROTEIN BINDING; PROTEIN DENATURATION; PROTEIN INTERACTION MAPPING; PROTEIN MULTIMERIZATION; PROTEIN STRUCTURE, QUATERNARY;

EID: 77956885443     PISSN: 00222836     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.jmb.2010.07.001     Document Type: Article

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