Computational De Novo Design and Characterization of a Four-Helix Bundle Protein that Selectively Binds a Nonbiological Cofactor [J.Am. Chem. Soc.2005,127, 1346−1347].
نویسندگان
چکیده
منابع مشابه
Computational de novo design and characterization of a protein that selectively binds a highly hyperpolarizable abiological chromophore.
This work reports the first example of a single-chain protein computationally designed to contain four α-helical segments and fold to form a four-helix bundle encapsulating a supramolecular abiological chromophore that possesses exceptional nonlinear optical properties. The 109-residue protein, designated SCRPZ-1, binds and disperses an insoluble hyperpolarizable chromophore, ruthenium(II) [5-(...
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The protein Felix was designed de novo to fold into an antiparallel four-helix bundle of specific topology. Its sequence of 79 amino acid residues is not homologous to any known protein sequence, but is "native-like" in that it is nonrepetitive and contains 19 of the 20 naturally occurring amino acids. Felix has been expressed from a synthetic gene cloned in Escherichia coli, and the protein ha...
متن کاملDomain-swapped dimeric structure of a stable and functional de novo four-helix bundle protein, WA20.
To probe the potential for activity in unevolved amino acid sequence space, we created a third generation combinatorial library of de novo four-helix bundle proteins. The "artificial superfamily" of helical bundles was designed using binary patterning of polar and nonpolar residues, and expressed in Escherichia coli from a library of synthetic genes. WA20, picked from the library, is one of the...
متن کاملDe novo design of a transmembrane Zn²⁺-transporting four-helix bundle.
The design of functional membrane proteins from first principles represents a grand challenge in chemistry and structural biology. Here, we report the design of a membrane-spanning, four-helical bundle that transports first-row transition metal ions Zn(2+) and Co(2+), but not Ca(2+), across membranes. The conduction path was designed to contain two di-metal binding sites that bind with negative...
متن کاملThe design of a four-helix bundle protein.
The design of proteins with predetermined structural properties is a necessary first step in the de novo design of novel enzymes and receptors. A major problem associated with the design of proteins is the high flexibility inherent in polypeptide chains. It has been estimated that a protein of 100 residues can adopt up to 101~176 different conformations, a number that is as large as the number ...
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ژورنال
عنوان ژورنال: Journal of the American Chemical Society
سال: 2006
ISSN: 0002-7863,1520-5126
DOI: 10.1021/ja059923q