From therapeutic nucleic acids to redox hydrogels: the diverse world of biopolymers

H. Bayley, F.E. Romesberg, Curr. Opin. Chem. Biol., (2006) 10:598-600.
pubpic2006bayleyEditorial comment on the special biopolymers issue of Curr. Opin. Chem. Biol.


Stability and polymerase recognition of pyridine nucleobase analogues: role of minor-groove H-bond acceptors

Y. Kim, A.M. Leconte, Y. Hari, F.E. Romesberg, Angew. Chem. Int. Ed. (2006) 45:7809-7812.
pubpic2006kimPyridyl nucleoside analogues are synthesized and characterized. An α-glycosidic nitrogen atom provides an H-bond acceptor that does not significantly facilitate pairing with natural nucleobases. However, it forms minor-groove H-bonds with water molecules and DNA polymerases that optimize the stability and replication, respectively, of the UBP.

Antibody evolution constrains conformational heterogeneity by tailoring protein dynamics

J. Zimmermann, E.L. Oakman, I.F. Thorpe, X. Shi, P. Abbyad, C.L. Brooks, III, S.G. Boxer, F.E. Romesberg, Proc. Natl. Acad. Sci. USA (2006) 103:13722-13727.
pubpic2006zimmermannWe report the characterization of protein heterogeneity and dynamics as a function of evolution for the antifluorescein antibody 4-4-20. Using nonlinear laser spectroscopy, surface plasmon resonance, and molecular dynamics simulations, we demonstrate that evolution localized the Ab-combining site from a heterogeneous ensemble of conformations to a single conformation by introducing mutations that act cooperatively and over significant distances to rigidify the protein.