Probing receptor-ligand interactions by sedimentation equilibrium

Proceedings of SPIE - The International Society for Optical Engineering

Volumn 2985, Issue , 1997, Pages 170-177

  Philo, John S ^a  

^a AMGEN INC   (United States)

Author keywords

Analytical ultracentrifugation; Protein protein interactions; Receptors; Sedimentation equilibrium

Indexed keywords

CENTRIFUGATION; CONCENTRATION (PROCESS); DIMERIZATION; DISSOCIATION; MOLECULAR WEIGHT; PROTEINS; STOICHIOMETRY;

ANALYTICAL ULTRACENTRIFUGATION;

BIOTECHNOLOGY;

EID: 0031389742     PISSN: 0277786X     EISSN: None     Source Type: Conference Proceeding    
DOI: 10.1117/12.274348     Document Type: Conference Paper

References (13)

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4. Human growth hormone and extracellular domain of its receptor: Crystal structure of the complex
5. Dimerization and activation of the Kit receptor by monovalent and bivalent binding of the stem cell factor
6. Interactions of neurotrophin-3 (NT-3), brain-derived neurotrophic factor (BDNF), and the NT-3/BDNF heterodimer with the extracellular domains of the TrkB and TrkC receptors
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10. Dimerization of the extracellular domain of granulocyte-colony stimulating factor receptor by ligand binding: A monovalent ligand induces 2:2 complexes
11. New developments in the study of biomolecular association via sedimentation equilibrium
12. Analysis of data from the analytical ultracentrifuge by nonlinear least-squares techniques
13. Parameter estimation by least-squares methods