1btd

Theoretical Model: The protein structure described on this page was determined theoretically, and hence should be interpreted with caution.

BETADOUBLET: DE NOVO DESIGN, SYNTHESIS, AND CHARACTERIZATION OF A MODEL BETASANDWICH PROTEIN

spinqualitylabelsall models 1btd Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights For a guided tour on the structure components use FirstGlance. Resources: FirstGlance, PDBsum, ProSAT Publication Abstract from PubMed How an amino acid sequence encodes the information necessary for a protein to adopt a unique tertiary structure remains unresolved. We are addressing this problem by designing "from scratch" protein molecules that will adopt predetermined three-dimensional structures. Based on this strategy, two identical four-stranded beta-sheets were designed to dimerize and form a beta-sandwich protein, called betadoublet. A synthetic gene encoding half the beta-sandwich protein was expressed in Escherichia coli, and the protein was purified to homogeneity. Biophysical characterization of betadoublet in aqueous solution demonstrated that the disulfide formed between the two sheets and that the dimer was a compact unaggregated globular protein, consisting predominantly of beta-sheet and stable to thermal denaturation. It has some backbone amide protons whose exchange is slow enough to be measured by NMR but binds more of the dye 1-anilinonaphthalene-8-sulfonate than a well-folded protein. Betadoublet: de novo design, synthesis, and characterization of a beta-sandwich protein.,Quinn TP, Tweedy NB, Williams RW, Richardson JS, Richardson DC Proc Natl Acad Sci U S A. 1994 Sep 13;91(19):8747-51. PMID:8090717 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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