Journal of the American Chemical Society · 2007 · 205 citations · 16 references
Life SciencesBiochemistryBiophysicsProtein FoldingStructural BiochemistryStructural BiologyMacromolecular AssemblyMacromolecular StructureProtein ConformationProtein OligomerizationProtein StructureSecondary StructureAqueous SolvationBeta SheetsOligomerization MechanismsPeptide Self-assemblyProtein CrystallographyProtein Self-assemblyX-ray Crystallography Of Folded Proteins
We recently reported that β-peptides can form discrete hetero-oligomers in aqueous solution. Here we describe the structure of such an oligomer as determined by X-ray crystallography. The structure of Zwit-1F reveals a homo-octamer of two cupped “hands” composed of both parallel and antiparallel 3 14 -helices. The core of the assembly is composed entirely of solvent-excluded β 3 -homoleucine residues. The Zwit-1F assembly shares many of the physical characteristics of natural proteins.
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X-Ray Structure of the GCN4 Leucine Zipper, a Two-Stranded, Parallel Coiled Coil
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Heat capacity and conformation of proteins in the denatured state
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