Sequence and structural duality: designing peptides to adopt two stable conformations.

@article{Pandya2004, abstract = {To improve our understanding of conformational transitions in proteins, we are attempting the de novo design of peptides that switch structural state. Here, we describe coiled-coil peptides with sequence and structural duality; that is, features compatible with two different coiled-coil motifs superimposed within the same sequence. Specifically, we promoted a parallel leucine-zipper dimer under reducing conditions, and a monomeric helical hairpin in an intramolecularly disulfide bridged state. Using an iterative process, we engineered peptides that formed stable structures consistent with both targets under the different conditions. Finally, for one of the designs, we demonstrated a one-way switch from the helical hairpin to the coiled-coil dimer upon addition of disulfide-reducing agents.}, address = {Department of Biochemistry, John Maynard-Smith Building, School of Life Sciences, University of Sussex, Falmer, Brighton, BN1 9QG, United Kingdom.}, author = {Pandya, M. J. and Cerasoli, E. and Joseph, A. and Stoneman, R. G. and Waite, E. and Woolfson, D. N. }, citeulike-article-id = {2395428}, doi = {10.1021/ja045568c}, issn = {0002-7863}, journal = {J Am Chem Soc}, keywords = {coiled-coil, hairpin, switch}, month = {December}, number = {51}, pages = {17016--17024}, posted-at = {2008-05-27 14:06:14}, priority = {2}, title = {Sequence and structural duality: designing peptides to adopt two stable conformations.}, url = {http://dx.doi.org/10.1021/ja045568c}, volume = {126}, year = {2004} }

TY - JOUR ID - Pandya2004 L3 - citeulike-article-id:2395428 TI - Sequence and structural duality: designing peptides to adopt two stable conformations. JF - J Am Chem Soc VL - 126 IS - 51 SP - 17016 EP - 17024 AD - Department of Biochemistry, John Maynard-Smith Building, School of Life Sciences, University of Sussex, Falmer, Brighton, BN1 9QG, United Kingdom. SN - 0002-7863 N2 - To improve our understanding of conformational transitions in proteins, we are attempting the de novo design of peptides that switch structural state. Here, we describe coiled-coil peptides with sequence and structural duality; that is, features compatible with two different coiled-coil motifs superimposed within the same sequence. Specifically, we promoted a parallel leucine-zipper dimer under reducing conditions, and a monomeric helical hairpin in an intramolecularly disulfide bridged state. Using an iterative process, we engineered peptides that formed stable structures consistent with both targets under the different conditions. Finally, for one of the designs, we demonstrated a one-way switch from the helical hairpin to the coiled-coil dimer upon addition of disulfide-reducing agents. KW - coiled-coil KW - hairpin KW - switch AU - Pandya, MJ AU - Cerasoli, E AU - Joseph, A AU - Stoneman, RG AU - Waite, E AU - Woolfson, DN PY - 2004/12/29/ UR - http://dx.doi.org/10.1021/ja045568c ER -