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Design of a novel globular protein fold with atomic-level accuracy
Author(s): Kuhlman B, Dantas G, Ireton GC, Varani G, Stoddard BL, Baker D
Source: SCIENCE    Volume: 302    Issue: 5649    Pages: 1364-1368    Published: NOV 21 2003  
Times Cited: 365     References: 36     
Abstract: A major challenge of computational protein design is the creation of novel proteins with arbitrarily chosen three-dimensional structures. Here, we used a general computational strategy that iterates between sequence design and structure prediction to design a 93-residue alpha/beta protein called Top7 with a novel sequence and topology. Top7 was found experimentally to be folded and extremely stable, and the x-ray crystal structure of Top7 is similar (root mean square deviation equals 1.2 angstroms) to the design model. The ability to design a new protein fold makes possible the exploration of the large regions of the protein universe not yet observed in nature.
Document Type: Article
Language: English
Reprint Address: Baker, D (reprint author), Univ Washington, Dept Biochem, Seattle, WA 98195 USA
Addresses:
1. Univ Washington, Dept Biochem, Seattle, WA 98195 USA
2. Univ Washington, Dept Chem, Seattle, WA 98195 USA
3. Univ Washington, Howard Hughes Med Inst, Seattle, WA 98195 USA
4. Fred Hutchinson Canc Res Ctr, Div Basic Sci, Seattle, WA 98109 USA
Publisher: AMER ASSOC ADVANCEMENT SCIENCE, 1200 NEW YORK AVE, NW, WASHINGTON, DC 20005 USA
Subject Category: Multidisciplinary Sciences
IDS Number: 745HP
ISSN: 0036-8075
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