Beyond de novo protein design--de novo design of non-natural folded oligomers.
The mystery of how a protein sequence specifies a unique structure has intrigued chemists, leading to the design and study of foldamers, non-natural oligomeric molecules that adopt well-defined structures. Recently, the sequence specificity of the various regular repeating structures has been revealed for bioinspired foldamers and such foldamers have been created to adopt helical bundle tertiary structures. One major strategy for the generation of abiotic foldamers has involved molecular design of the monomer geometry. These advances in foldamer research may lead to future applications in biomedical and materials science.
Department of Chemistry, University at Buffalo, The State University of New York, Buffalo, New York 14260-3000, USA. chengr@buffalo.edu
Richard P
RP
Cheng
D000596:Amino Acids / Q000737:chemistry / Q000378:metabolism; D008958:Models, Molecular; D010455:Peptides / Q000737:chemistry / Q000378:metabolism; D034444:Peptoids / Q000737:chemistry / Q000378:metabolism; D011487:Protein Conformation; D015202:Protein Engineering / Q000379:methods* / Q000639:trends; D017510:Protein Folding; D011506:Proteins / Q000737:chemistry* / Q000378:metabolism; D013329:Structure-Activity Relationship
D000596:Amino Acids; D010455:Peptides; D034444:Peptoids; D011506:Proteins