Biochemistry Faculty
Jennifer J. Ottesen
Research Interests:
Research in the Ottesen laboratory utilizes peptide and protein chemistry
to address biological problems. The Ottesen group is developing improved
techniques for solid phase chemical ligation, which allows the rapid
recombination of peptide elements into larger macromolecules. They also
employ expressed protein ligation, in which synthetic polypeptides and
recombinant protein elements can be chemoselectively linked together.
This allows the power of synthetic techniques to be applied to large
proteins.
Publications
Selected publications from the last several years:
Ottesen, J.J., Bar-Dagan, M., Giovani, B., Muir, T.W. (2008) "An amalgamation of solid phase peptide synthesis and ribosomal peptide synthesis." Biopolymers 90(3):406-14.
Ottesen, J.J., Huse, M., Sekedat, M.D., Muir, T.W. (2004) "Semisynthesis
of phosphovariants of Smad2 reveals a substrate preference of the activated
T beta RI kinase." Biochemistry 43(19), 5698-706.
Cowburn, D., Shekhtman, A., Xu, R., Ottesen,
J.J., Muir, T.W. (2004) "Segmental
isotopic labeling for structural biological applications of NMR." Methods
Mol Biol. 278, 47-56.
Wilson, K.A., Kalkum, M., Ottesen, J.J., Yuzenkova, J., Chait, B.T.,
Landick, R., Muir, T., Severinov, K. and Darst, S.A. (2004) "Structure
of microcin J25, a peptide inhibitor of bacterial RNA polymerase, is
a lassoed tail." J. Am Chem. Soc. 125(41), 12475-83.
Ottesen, J.J., Blaschke, U.K. Cowburn, D. and Muir, T.W. (2003) "Segmental
isotopic labeling: Prospects for a new tool to study the structure-function
relationships in multi-domain proteins." Biol. Mag. Res. 20, 35-51.
Mezo, A.R., Ottesen, J.J., and Imperiali B. (2001) " Discovery
and characterization of a discretely folded homotrimeric betabetaalpha
peptide." J. Am. Chem. Soc. 123(5), 1002-3.
Ottesen, J.J. and Imperiali, B. (2001) " Design of a discretely
folded mini-protein motif with predominantly beta-structure." Nat.
Struct. Biol.8(6), 535-9.
Imperiali, B. and Ottesen, J.J. (1999) "Uniquely folded mini-protein
motifs." J. Pept. Res. 54(3), 177-84. (Review)
Imperiali, B. and Ottesen, J.J. (1998) "Design strategies for
the construction of independently folded polypeptide motifs." Biopolymers
47(1), 23-9.
Struthers, M., Ottesen, J.J.and Imperiali B. (1998) "Design and
NMR analyses of compact, independently folded BBA motifs." Fold
Des. 3(2), 95-103.
