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| beta sheet | |
|---|---|
| Name | Beta sheet |
| Caption | Schematic of beta sheet arrangement |
| Type | Secondary structure |
| Discovered | 1951 |
| Discoverer | Pauling and Corey |
beta sheet
Beta sheet structures are common protein secondary elements characterized by extended peptide strands aligned to form hydrogen-bonded sheets. The discovery and description involved researchers such as Linus Pauling, Robert Corey, Max Perutz, John Kendrew, and institutions like the California Institute of Technology and the Medical Research Council in studies related to hemoglobin and myoglobin. Experimental determination uses methods developed at places like the Royal Institution, including techniques from X-ray crystallography and nuclear magnetic resonance that were advanced at institutions such as the University of Cambridge and the Massachusetts Institute of Technology.
Beta sheets are arrays of beta strands found in proteins studied by laboratories including the Laboratory of Molecular Biology and published in journals affiliated with the Royal Society and the National Academy of Sciences. Early models arose in the context of structural work on macromolecules at institutions such as the Scripps Research Institute and the Max Planck Society. Structural biology efforts from groups at the European Molecular Biology Laboratory and the Howard Hughes Medical Institute clarified sheet occurrence in enzymes, antibodies, and viral capsids, with implications noted by researchers at the Wellcome Trust and the Cold Spring Harbor Laboratory.
Geometrically, beta strands adopt an extended conformation whose backbone dihedral angles were first analyzed by investigators like Robert Corey and Linus Pauling and later refined by computational groups at the University of California, San Diego and the University of Oxford. Strand packing and twist are quantified using parameters developed by teams at the Weizmann Institute of Science and the European Bioinformatics Institute, and visualized by software from the RCSB Protein Data Bank and the Protein Data Bank in Europe. Models of strand registry and pleating were evaluated in collaboration with structural efforts at the Max Planck Institute for Biophysical Chemistry and the Institut Pasteur.
Stability of sheets depends on backbone hydrogen bonds characterized in foundational studies by Linus Pauling and later thermodynamic measurements by groups at the National Institutes of Health and the Pasteur Institute. Hydrogen-bond patterns are interpreted through data from experiments at the Brookhaven National Laboratory and theoretical work from researchers at the California Institute of Technology and Princeton University. Solvent exposure and side-chain interactions were probed in studies affiliated with the Swiss Federal Institute of Technology and the University of Tokyo, showing contributions from intramolecular forces measured using techniques developed at the Max Delbrück Center.
Sheets occur in antiparallel and parallel arrangements described in reviews by authors affiliated with the Johns Hopkins University and the University of Chicago. Topological classification schemes were proposed by groups at the European Molecular Biology Laboratory and databases curated by the Protein Data Bank and the SCOP and CATH projects, with examples drawn from proteins studied at the Institut Pasteur, the Karolinska Institute, and the Kavli Institute for Theoretical Physics.
Folding pathways involving sheet formation were explored in kinetic experiments from laboratories at the University of California, San Francisco and the University of Pennsylvania, and simulated by computational teams at the Oak Ridge National Laboratory and Microsoft Research. Chaperone-mediated assistance for sheet-containing proteins was characterized by groups at the National Institute of Diabetes and Digestive and Kidney Diseases and the European Molecular Biology Laboratory, while single-molecule studies from the Max Planck Institute and the University of Basel provided real-time insights into nucleation and propagation.
Beta sheets provide structural scaffolds in enzymes and binding proteins investigated at the Salk Institute and the Fred Hutchinson Cancer Research Center, and form cores of antibodies characterized at the Centers for Disease Control and Prevention and vaccine research at the Bill & Melinda Gates Foundation. Sheets contribute to ligand recognition in receptors studied by researchers at the Rockefeller University and the Broad Institute, and form structural motifs in viral proteins examined at the Centers for Disease Control and Prevention and the World Health Organization.
Misfolding of beta-rich proteins underlies pathologies studied by consortia at the Alzheimer's Association, the National Institute on Aging, and the Michael J. Fox Foundation, with amyloid assemblies characterized by investigators at the Scripps Research Institute and the Gladstone Institutes. Prion diseases and systemic amyloidoses have been examined in clinical and structural programs at the Mayo Clinic, the Cleveland Clinic, and university centers such as the University of Oxford and the University of Cambridge, highlighting therapeutic research supported by the Wellcome Trust and the European Commission.
Category:Protein structure