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Prof. Jannette Carey (Princeton University)

Hodnost

Ph.D., Biochemistry
University of Illinois, Champaign-Urbana
Thesis Advisor: Olke C. Uhlenbeck
Thesis: "Interaction of Bacteriophage R17 Coat Protein with Its RNA Binding Site for Translational Repression"
Postdoctoral Fellow
Stanford University
Robert L. Baldwin,
Biochemistry Department
Charles Yanofsky,
Biological Sciences Department

Pozice

    1989-now: Professor at the Department of Chemistry,     Princeton University

2005-2006 Tage Erlander guest professor, Lund University, Sweden 

2008-now: distinguished visiting scientist at the Institute of Nanobiology and Structural Biology of GCRC, Academy of Sciences of the Czech Republic

Adresa
Zámek 136, CZ-373 33 Nové Hrady
jcarey@princeton.edu
www.molbio.princeton.edu/index.php?option=content&task=view&id=204

Současné zaměření

Jannette Carey is best known for her work in the theory and practice of protein-ligand interactions, and for her application of thermodynamics to biochemical systems. She has written a number of influential methods papers on those topics, and has organized Gordon conferences on Biopolymers and on Molecular recognition. She is the organizer of this year's J. Willard Gibbs conference on Biothermodynamics.

She recently spent a sabbatical year developing themes in systems biology at Lund university Sweden, where she was appointed by the swedish national research council as the Tage Erlander guest professor for years 2005-2006, the highest award in Sweden for a visiting professor. She was for many years on the grant review panel in biochemistry for the US National Science Foundation, and is an editor of biochimica et biophysica acta Proteins and Proteomics.

Dřívější výsledky

Jannette Carey s research interests are in the general area of biomolecular interactions. For the last several years her group has been working in parallel in the areas of protein folding and protein-ligand recognition, though her recent work suggests that these two areas are more convergent than strictly parallel. On the one hand, there is evidence of a significant role for protein folding in molecular recognition, and on the other hand protein folding can be viewed, both conceptually and experimentally, as a special case of molecular recognition in which the partners are normally intramolecular. A unifying theme of her work in these two areas is a focus on understanding the molecular origins of affinity, specificity, and cooperativity in the two kinds of recognition processes, and relating these features to the requirements of the biological systems they serve (for a review, see Szwajkajzer & Carey, 1997). She worked on a broad range of systems, usually choosing those that display intriguing features in their folding or ligand-recognition reactions, in the hope that detailed comparisons may elucidate general principles important for folding and recognition.

Odkazy

Selected Publications

Carey J, Lindman S, Bauer M, Linse S. (2007) Protein reconstitution and three-dimensional domain swapping: benefits and constraints of covalency. Protein Sci 16: 2317-2333 PubMed

Carey J, Brynda J, Wolfová J, Grandori R, Gustavsson T, Ettrich R, Smatanová IK. (2007) WrbA bridges bacterial flavodoxins and eukaryotic NAD(P)H:quinone oxidoreductases. Protein Sci 16: 2301-2305. PubMed

Natalello A, Doglia SM, Carey J, Grandori R. (2006) Role of flavin mononucleotide in the thermostability and oligomerization of Escherichia coli stress-defense orotein WrbA. Biochemistry 46: 543-553. PubMed

Ji H, Shen L, Carey J, Grandori R, Zhang H. (2006) Weaker binding of FMN by WrbA than by flavodoxin: a molecular modeling study. J Molec Struct Theo Chem 764: 155-160.

Nöll G, Kozma E, Grandori R, Carey J, Schödl T, Hauska G, Daub J. (2006) Spectroelectrochemical investigation of a flavoprotein with a flavin-modified gold electrode. Langmuir 22: 2378-2383. PubMed

Wolfova J, Grandori R, Kozma E, Chatterjee N, Carey J, Smatanova I. (2005) Crystallization of the flavoprotein WrbA optimized by using additives and gels. J Cryst Growth 284: 502-505.

Samalikova M, Carey J, Grandori R. (2005) Assembly of the hexameric Escherichia coli arginine repressor investigated by nano-ESI-TOF mass spectrometry. Rapid Comm Mass Spec 19: 2549-2552. PubMed

Patel KA, Bartoli K, Ngatchou AN, Wocj G, Carey J, Tanaka JC. (2005) Impaired function and trafficking of cyclic nucleotide-gated channel mutants from human cone CNGA3 causing achromatopsia 2. Invest Ophthamol Visual Sci 46: 2282-2290.

Jin L, Xue W-F, Fukayama JW, Yetter J, Pickering M, Carey J. (2005) Asymmetric allosteric activation of the symmetric ArgR hexamer. J Mol Biol 346: 43-56. PubMed

Xue W-F, Carey J, Linse S. (2004) Multi-method global analysis of thermodynamics and kinetics in reconstitution of monellin. Proteins: Structure, Function, and Bioinformatics. 57: 586-595. PubMed

Pursglove SE, Fladvad M, Bellanda M, Moshref A, Henriksson M, Carey J, Sunnerhagen M. (2004) Biophysical properties of regions flanking the bHLH-Zip motif in the p22 Max protein. Biochem Biophys Res Commun 323: 750-759. PubMed

Carey J (2004). Quantifying molecular recognition for drug discovery, in NMR in Drug Screening, Oxford University Press, in press.

Lawson CL, Benhoff B, Berger T, Berman HM, Carey J (2004). E. coli trp repressor forms a domain-swapped array in aqueous alcohol. Structure 12: 1099-1107. PubMed

Szwajkajzer D, Carey J (2003). RaPID plots: Affinity and mechanism at a glance. Biacore J 3: 19.

McWhirter A and Carey J (2003). T-cell receptor recognition of peptide antigen/MHC complexes. Biacore J 3: 18.

Tyler R, Pelczer I, Carey J, Copie V (2002). Three-dimensional solution NMR structure of apo-L75F-TrpR, a temperature-sensitive mutant of the tryptophan repressor protein. Biochemistry 41: 11954-11962. PubMed

Szwajkajzer D, Dai L, Fukayama JW, Abramczyk B, Fairman R, Carey J (2001). Quantitative analysis of DNA binding by E. coli arginine repressor. J Mol Biol 312: 949-962. PubMed

Scott S-P, Weber IT, Harrison RW, Carey J, Tanaka JC (2001). A functioning chimera of the cyclic nucleotide-binding domain from the bovine retinal rod ion channel and the DNA-binding domain from catabolite gene-activating protein. Biochemistry 40: 7464-7473. PubMed

Carey J (2000). Globularity and protein function. J Biomol Str Dyn 11: 87-88.

Carey J (2000). A systematic and general proteolytic method for defining structural and functional domains of proteins. Methods Enzymol 328: 499-514.  PubMed

Jin L, Fukayama JW, Pelczer I and Carey J (1999). Long-range effects on dynamics in a temperature-sensitive mutant of trp repressor. J Mol Biol 285: 361-378.  PubMed

Grandori R, Khalifah P, Boice JA, Fairman R, Giovanielli K, Carey J (1998). Biochemical characterization of WrbA, founding member of a new family of multimeric flavodoxin-like proteins. J Biol Chem 273: 20960-20966.  PubMed

Szwajkajzer D and Carey J (1997). Molecular and biological constraints on ligand-binding affinity and specificity. Biopolymers 44: 181-198.  PubMed

Sunnerhagen M, Nilges M, Otting G and Carey J (1997). Solution structure of the DNA-binding domain and model for the complex of multifunctional hexameric arginine repressor with DNA. Nat Struct Biol 4: 819-826.  PubMed

Grandori R, Lavoie TA, Pflumm M, Tian G, Niersbach H, Maas WK, Fairman R, Carey J (1995). The DNA-binding domain of the hexameric arginine repressor. J Mol Biol 254: 150-162.  PubMed

Wu LC, Grandori R and Carey J (1994). Autonomous subdomains in protein folding. Protein Sci 3: 369-371.  PubMed

Grandori R and Carey J (1994). Six new candidate members of the alpha/beta twisted open-sheet family detected by sequence similarity to flavodoxin. Protein Sci 3: 2185-2193.  PubMed

Wu LC, Laub PB, Elove GA, Carey J and Roder H (1993). A noncovalent peptide complex as a model for an early folding intermediate of cytochrome c. Biochemistry 32: 10271-10276.  PubMed

Lawson CL and Carey J (1993). Tandem binding in crystals of a trp repressor/operator half-site complex. Nature 366: 178-182.  PubMed

Jin L, Yang J and Carey J (1993). Thermodynamics of ligand binding to trp repressor. Biochemistry 32: 7302-7309.  PubMed

Tasayco ML and Carey J (1992). Ordered self-assembly of polypeptide fragments to form nativelike dimeric trp repressor. Science 255: 594-597.   PubMed

Ústavní publikace v impaktovaných časopisech