H. Bayley, F.E. Romesberg, Curr. Opin. Chem. Biol., (2006) 10:598-600.
Editorial comment on the special biopolymers issue of Curr. Opin. Chem. Biol.
A.M. Leconte, F.E Romesberg, Nature, (2006) 444:553-555.
We review the report of the structure of xDNA from the Kool lab.
L.B. Sagle, J. Zimmermann, P.E. Dawson, F.E. Romesberg, J. Am. Chem. Soc. (Comm.) (2006) 128:14232-14233.
We report the use of a recently developed technique to study the folding of cyt c that is based on the site-selective incorporation of carbon−deuterium (C−D) bonds and their characterization by IR spectroscopy.
Y. Kim, A.M. Leconte, Y. Hari, F.E. Romesberg, Angew. Chem. Int. Ed. (2006) 45:7809-7812.
Pyridyl 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.
C.S. Kinnaman, M.E. Cremeens, F.E. Romesberg, S.A. Corcelli, J. Am. Chem. Soc. (Comm.) (2006) 128(41):13334-13335.
We explore the viability of α-carbon deuterated bonds (Cα−D) as infrared (IR) probes of protein backbone dynamics.
A.M. Leconte and F.E. Romesberg, Nat. Meth. (2006) 3:667-668.
Wereview a report by Hirao et al. demonstrating that DNA containing an unnatural base pair is both efficiently PCR amplified and transcribed.
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.
We 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.