6oln

Controlling the Self-Assembly of Synthetic Metal-Coordinating Coiled-Coil Peptides: Orthorhombic Lattice from a Trimeric Coiled Coil

spinqualitylabelsall models 6oln, resolution 2.50Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 6oln is a 6 chain structure with sequence from Synthetic construct. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: X-ray diffraction, Resolution 2.5Å Ligands: 7WJ, ACE, CL, CU, NH2 Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Publication Abstract from PubMed Metal-binding peptides are versatile building blocks in supramolecular chemistry. We recently reported a class of crystalline materials formed through a combination of coiled-coil peptide self-association and metal coordination. Here, we probe the serendipitously discovered metal binding motif that drives the assembly and apply these insights to exert rational control over structure and morphology in the materials. Understanding and controlling the metal-directed assembly of terpyridine-functionalized coiled-coil peptides.,Scheib KA, Tavenor NA, Lawless MJ, Saxena S, Horne WS Chem Commun (Camb). 2019 Jul 2;55(54):7752-7755. doi: 10.1039/c9cc03496j. PMID:31204733 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

Proteopedia Page Contributors and Editors (what is this?)

OCA