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
