Toward β-Amino Acid Proteins: A Cooperatively Folded β-Peptide Quaternary Structure Export

@article{Qiu2006, abstract = {Abstract: Folded polymers in nature are assembled from simple monomers and adopt complex folded structures through networks of stabilizing noncovalent interactions. These interactions define secondary and tertiary structure and in most cases specify a unique three-dimensional architecture. Individual secondary or tertiary structures can also associate with one another to form multi-subunit quaternary structures. Nonnatural folded polymers have potential for similar structural versatility. Here we describe a pair of 3-peptides whose sequences were designed to promote a 14-helix structure in water, favor hetero-oligomer formation, and disfavor nonspecific aggregation. These 3-peptides assemble noncovalently into a well-defined hetero-oligomer characterized by a defined stoichiometry, a highly stabilized secondary structure, and a cooperative melting transition (TM > 55 C). This work demonstrates that 3-peptides can assemble into defined, cooperatively folded quaternary structures and constitutes an important step toward designing protein-like assemblies from nonnatural polymers.}, author = {Qiu, J. X. and Petersson, E. J. and Matthews, E. E. and Schepartz, A.}, citeulike-article-id = {2522118}, citeulike-linkout-0 = {http://pubs3.acs.org/acs/journals/doilookup?in_doi=10.1021/ja063164+}, journal = {Journal of the American Chemical Society}, keywords = {foldamer}, number = {35}, pages = {11338--11339}, posted-at = {2008-03-12 18:14:51}, priority = {0}, title = {Toward \&\#x03B2;-Amino Acid Proteins: A Cooperatively Folded \&\#x03B2;-Peptide Quaternary Structure}, url = {http://pubs3.acs.org/acs/journals/doilookup?in_doi=10.1021/ja063164+}, volume = {128}, year = {2006} }

TY - JOUR ID - Qiu2006 L3 - citeulike-article-id:2522118 N2 - Abstract: Folded polymers in nature are assembled from simple monomers and adopt complex folded structures through networks of stabilizing noncovalent interactions. These interactions define secondary and tertiary structure and in most cases specify a unique three-dimensional architecture. Individual secondary or tertiary structures can also associate with one another to form multi-subunit quaternary structures. Nonnatural folded polymers have potential for similar structural versatility. Here we describe a pair of 3-peptides whose sequences were designed to promote a 14-helix structure in water, favor hetero-oligomer formation, and disfavor nonspecific aggregation. These 3-peptides assemble noncovalently into a well-defined hetero-oligomer characterized by a defined stoichiometry, a highly stabilized secondary structure, and a cooperative melting transition (TM > 55 C). This work demonstrates that 3-peptides can assemble into defined, cooperatively folded quaternary structures and constitutes an important step toward designing protein-like assemblies from nonnatural polymers. IS - 35 JF - Journal of the American Chemical Society EP - 11339 TI - Toward β-Amino Acid Proteins: A Cooperatively Folded β-Peptide Quaternary Structure VL - 128 SP - 11338 KW - foldamer AU - Qiu, JX AU - Petersson, EJ AU - Matthews, EE AU - Schepartz, A PY - 2006/// UR - http://pubs3.acs.org/acs/journals/doilookup?in_doi=10.1021/ja063164+ ER -