TAILIEUCHUNG - Báo cáo khoa học: Searching for folded proteins in vitro and in silico

Understanding the sequence determinants of protein struc-ture, stabilityand folding is critical for understanding how natural proteins have evolved and how proteins can be engineeredtoperformnovel the protein folding problem requires the abilityto search large volumes of sequence space for proteins with specific struc-tural or functional characteristics. Here we describe our efforts to identifynovel proteins using a phage-display selection strategyfrom a mini-exon shuffling librarygener-ated from the yeast genome and from completely random sequence libraries, and compare the results to recent succes-ses in generating novel proteins usingin silicoprotein design | Eur. J. Biochem. 271 1615-1622 2004 FEBS 2004 doi MINIREVIEW Searching for folded proteins in vitro and in silico Alexander L. Watters1 and David Baker2 1 Molecular and Cellular Biology Program and department of Biochemistry and Howard Hughes Medical Institute University of Washington Seattle WA USA Understanding the sequence determinants of protein structure stability and folding is criiical lor undestlanding low natural proteins have evolved and how proteins can be engineered to perform novel functions. The complexityof the protein folding problem requires the abilityto search large volumes of sequence space for proteins with specific structural or functional characteristics. Here we describe our efforts to identify ovvel pooteins usigg a paage-disphiy selection strategy from a mini-exon shuffling library generated from the yeast genome and from completely random sequence libraries and compare the results to recent successes in generating novel proteins using in silico protein design. Keywords loop entropy mini-exon shuffling phagedisplay protein evolution random sequences simplified proteins. Introduction To probe the sequence determinants of protein folding and to investigate the selection pressures which have shaped protein evolution it is desirable to generate novel proteins in the laboratoryand to studytheir biophysical characteristics. There are two powerful approaches to generating such artificial proteins combinatorial libraryselections and computational protein design. In this paper we describe our results using both applications and present the results of an investigation of protein evolution by mini-exon shuffling. Phage-display Phage-display technology Is an excnhent modoìd for selecting functional binding mutants from large peptide or protein libraries 1 . This technology utili ss the ability to express foreign proteins on the outside of phage particles as fusions to the phage coat proteins. Phage expressing fusion .

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