2kib | pdb_00002kib
From Proteopedia
Protein Fibril
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Structural highlights
Publication Abstract from PubMedThe fibril structure formed by the amyloidogenic fragment SNNFGAILSS of the human islet amyloid polypeptide (hIAPP) is determined with 0.52 A resolution. Symmetry information contained in the easily obtainable resonance assignments from solid-state NMR spectra (see picture), along with long-range constraints, can be applied to uniquely identify the supramolecular organization of fibrils. Unique identification of supramolecular structures in amyloid fibrils by solid-state NMR spectroscopy.,Nielsen JT, Bjerring M, Jeppesen MD, Pedersen RO, Pedersen JM, Hein KL, Vosegaard T, Skrydstrup T, Otzen DE, Nielsen NC Angew Chem Int Ed Engl. 2009;48(12):2118-21. PMID:19130518[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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This page was last modified 07:05, 1 December 2021.