个人简介

NIH Career Development Award Dreyfus Teacher-Scholar Award Alfred P. Sloan Research Fellow Scientific Advisory Board, Biopolymers, 2002 forward

研究领域

Biophysical/Bioorganic/and Medicinal Chemistry

Research in the Andersen group focuses on both the fundamental thermodynamics and structural features associated with biorecognition phenomena and practical applications in drug and protein design. The primary biophysical tools employed are spectroscopic: NMR determinations of polypeptide structure and dynamics, IR- and fluorescence-monitored T-jump kinetics for folding pathways, CD studies of the melting of secondary and tertiary structure. Drug design efforts are supported by NMR structural data for protein hormones and enzymes for key steps required for the viability of bacteria. Active programs in mutant protein over-expression, peptide synthesis, and combinatorial synthesis of small molecule inhibitor libraries support this effort. Illustrative projects are briefly outlined in the following paragraphs.

近期论文

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Hyperstable Miniproteins: Additive Effects of D- and L-Ala Mutations, D. V. Williams, B. Barua, N. H. Andersen, Organic & Biomolecular Chemistry, 6,4287-4289 (2008). Probing the Lower Size Limit for Protein-like Fold Stability: Ten-residue Microproteins with Specific, Rigid Structures in Water, B. L. Kier & N. H. Andersen, J Am Chem. Soc., 130, 14675-14683 (2008). Lysine and arginine residues do not increase the helicity of alanine-rich peptide helices, J. M. Stewart, J. C. Lin & N. H. Andersen, Chem. Commun., 4765-4767 (2008). Structural insights for designed alanine-rich helices: Comparing NMR helicity measures and conformational ensembles from molecular dynamics, K. Song, J. Stewart, R. M. Fesinmeyer, N. H. Andersen & C. Simmerling, Biopolymers, 89, 747-760 (2008). The Trp-cage: Optimizing the Stability of a Globular Miniprotein, B. Barua, J. C. Lin, D. V. Williams, J. W. Neidigh, P. Kummler & N. H. Andersen, Protein Engineering Design and Selection, 21, 171-185 (2008). A pre-existing hydrophobic collapse in the unfolded state of an ultrafast folding protein, K. H. Mok, L. T. Kuhn, M. Goez, I. J. Day, J. C. Lin, N. H. Andersen & P. J. Hore, Nature, 447, 106-109 (2007). Measuring Cooperativity in the Formation of a Three-stranded b sheet (Double Hairpin), F. M. Hudson & N. H. Andersen, Biopolymers, 83, 424-433 (2006). Minimization and Optimization of Designed b Hairpin Folds, N. H. Andersen, K. A. Olsen, R. M. Fesinmeyer, X. Tan, F. M. Hudson, L. A. Eidenschink & S. R. Farazi, J. Am. Chem. Soc., 128, 6101-6110 (2006). Chemical Shifts Provide Fold Populations and Register of b-Hairpins and b-Sheets, R. M. Fesinmeyer, F. M. Hudson, K. A. Olsen, G. W. N. White, A. Euser & N. H. Andersen, J. Biomolecular NMR, 33, 213-231 (2005). Hairpin folding rates reflect mutations within and remote from the turn region, K. A. Olsen, R. M. Fesinmeyer, J. Stewart & N. H. Andersen, Proc. Natl. Acad. Sci. USA, 102, 15483-15487 (2005). Studies of Helix Fraying and Solvation Using 13C’ Isotopomers, R. M. Fesinmeyer, Eric S. Peterson, R. Brian Dyer & N. H. Andersen, Protein Sci., 14, 2324-2332 (2005). Hairpin Folding Dynamics: The Cold-denatured State is Predisposed for Rapid Refolding, R. B. Dyer, S. J. Maness, S. Franzen, R. M. Fesinmeyer, K. A. Olsen & N. H. Andersen, Biochemistry, 44, 10406-10415 (2005). The Helical Alanine Controversy: An (Ala)6 Insertion Dramatically Increases Helicity, J. C. Lin, B. Barua & N. H. Andersen, J. Am. Chem. Soc., 126, 13679-13684 (2004). Exenatide: NMR/CD Evaluation of the Medium Dependence of Conformation and Aggregation State, F. M. Hudson & Niels H. Andersen, Biopolymers (Peptide Science), 76, 298-308 (2004). The Mechanism of b Hairpin Formation, R. B. Dyer, S. J. Maness, E. S. Peterson, S. Franzen, R. M. Fesinmeyer & N. H. Andersen, Biochemistry, 43, 11560-11566 (2004). PMID: 15350142. Enhanced Hairpin Stability through Loop Design, the Case of the Protein G B1 Domain Hairpin, R. M. Fesinmeyer, F. M. Hudson & N. H. Andersen, J. Am. Chem. Soc., 126, 7238-7243 (2004). 19F NMR Studies of Tryptophan/Serum Albumin Binding, Bolong Cao, Stephanie Endsley & Niels H. Andersen, Bioorganic & Medicinal Chemistry, 11, 69-75 (2003). Determinants of Miniprotein Stability: Can anything replace a buried H-bonded Trp sidechain, Bipasha Barua & Niels H. Andersen, Letters in Peptide Science, 8, 221-226 (2002). Peptide Conformational Changes Induced by Tryptophan-Phosphocholine Interactions in a Micelle, J. W. Neidigh & N. H. Andersen, Biopolymers, 65, 354-361 (2002). Potent, Novel in Vitro Inhibitors of the Pseudomonas aeruginosa Deacetylase LpxC , T. Kline, N. H. Andersen, E. A. Harwood, J. Bowman, A. Malanda, S. Endsley, A. L. Erwin, M. Doyle, S. Fong, A. L. Harris, B. Mendelsohn, K. Mdluli, C. R. H. Raetz, C. K. Stover, P. R. Witte, A. Yabannavar & S. Zhu, J. Med. Chem., 45, 3112-3129 (2002). Activation of Erythropoietin Receptor through a Novel Extracellular Binding Site, T. Naranda, R. I. Kaufman, J. Li, K. Wong, A. Boge, D. Hallen, K. Y. C. Fung, M. W. Duncan, N. Andersen, A. Goldstein & L. Olsson, Endocrinology, 143, 2293-2302 (2002).