title: Structural characterization of pollen allergens.
abstract: The molecular characterization of allergens has accelerated significantly since the widespread implementation of modern analytical methods. The combination of gene cloning and heterologous protein expression has generated an extensive array of allergens that is available for comparative analysis, as well as clinical applications. Several internet-accessible allergen databases integrate the accumulated information from biomedical research and clinical practice. Innovations in classical biophysical methods, such as mass spectrometry, X-ray crystallography, and nuclear magnetic resonance spectroscopy, have rendered complex biological macromolecules amenable to detailed structural analysis. The modern scientific era has realized the synthesis of bioinformatics, molecular biology, biochemistry, biophysics, and immunology, and given us the means needed to decipher the remaining mysteries of allergies. This article addresses how the synergism of modern scientific techniques has hastened our understanding of allergies, how these techniques are applied in the identification and characterization of allergens, and how these methods assist the rational development of clinical tools for allergy diagnosis and treatment.
authors.affiliation: Department of Structural Biology, Institute of Chemistry, University of Graz, Austria. verdino@scripps.edu
authors.forename: Petra
authors.initials: P
authors.lastname: Verdino
mesh_terms: D000485:Allergens / Q000737:chemistry*; D000595:Amino Acid Sequence; D002942:Circular Dichroism / Q000379:methods; D019295:Computational Biology / Q000379:methods; D018360:Crystallography, X-Ray / Q000379:methods; D006801:Humans; D019906:Nuclear Magnetic Resonance, Biomolecular / Q000379:methods; D011058:Pollen / Q000737:chemistry / Q000276:immunology*; D011487:Protein Conformation; D020836:Protein Structure, Quaternary; D017433:Protein Structure, Secondary; D017434:Protein Structure, Tertiary
chemical_list: D000485:Allergens