Michael Gryk's NMR group, University of Connecticut, USA
Below is a copy of information about Gryk's lab from the website of University of Connecticut.
Michael R. Gryk
Associate Professor of Molecular, Microbial and Structural Biology
gryk@uchc.edu
|  | Areas of Interest
The focus of our laboratory is structural bioinformatics. We are currently involved in several projects on this topic, mainly the use of NMR spectroscopy as a tool for macromolecular characterization and molecular structure as an aid to bioinformatics.
Particular projects include the development of CONNJUR (http://connjur.uchc.edu – an open source integration platform for biomolecular NMR data processing; utilizing non-uniform sampling techniques and the use of maximum entropy methods for spectral reconstruction; and the development of a database of short linear motifs which confer specific functions to proteins (http://mnm.engr.uconn.edu). NMR studies involve DNA repair proteins of relatively large molecular weight for NMR spectroscopy (20-70 kDa). Current methods to overcome the difficulties inherent in studying these large systems include extensive labeling using stable isotopes and the use of TROSY-based pulse sequences. A critical mission of the lab is the facility approach to NMR, such that as advancements are made, they are tailored for ease-of-use both internally and externally when possible.
Publications
Selected Publications
Gryk M.R., Vyas J., & Maciejewski M.W. (2010) Biomolecular NMR data analysis. Prog Nucl Magn Reson Spectrosc., 56, 329-45.
Fox-Erlich S., Schiller M.R., Gryk M.R. (2009) Structural Conservation of a short, functional, peptide sequence motif. Front. Biosci. 14, 1143-1151.
Gryk, M.R. & Hoch, J.C. (2008) Local knowledge helps determine protein structures. PNAS, 105, 4533-4534.
Mobli M., Maciejewski M.W., Gryk M.R. & Hoch J.C. (2007) An automated tool for maximum entropy reconstruction of biomolecular NMR spectra. Nat. Methods, 4, 467-8.
Verdi, K.K., Ellis, H.J. & Gryk, M.R. (2007) Conceptual-level workflow modeling of scientific experiments using NMR as a case study. BMC Bioinformatics, 8:31.
Balla S., Thapar V., Verma S., Luong T., Faghri T., Huang C.H., Rajasekaran S., del Campo J.J., Shinn J.H., Mohler W.A., Maciejewski M.W., Gryk M.R., Piccirillo B., Schiller S.R., & Schiller M.R. (2006) Minimotif Miner: a tool for investigating protein function. Nature Methods, 3, 175-177.
Ellis, H.J.C., Fox-Erlich, S., Martyn, T.O., & Gryk, M.R. (2006) Development of an Integrated Framework for Protein Structure Determinations: A Logical Data Model for NMR Data Analysis. Third International Conference on Information Technology: New Generations, 613-618.
Fox-Erlich, S., Martyn, T.O., Ellis, H.J.C, & Gryk, M.R. (2004) Delineation and Analysis of the Conceptual Data Model Implied by the ‘IUPAC Recommendations for Biochemical Nomenclature’, Prot. Science, 13, 2559-2558.
Marintchev, A., Gryk, M.R., and Mullen, G.P. (2003) Site-Directed Mutagenesis Analysis of the Structural Interaction of the Single-Strand-Break Repair Protein, X-ray Cross-Complementing Group 1, with DNA Polymerase β Nucleic Acids Res., 31, 580-588.
Gryk, M.R., Marintchev, A., Maciejewski, M.W., Robertson, A., Wilson, W.H., and Mullen, G.P. (2002) Mapping of the interaction interface of DNA Polymerase β with XRCC1. Structure, 10, 1709-1720.
Maciejewski, M.W., Shin, R., Pan, B., Marintchev, A., Denninger, A., Mullen, M.A., Chen, K., Gryk, M.R., and Mullen, G.P. (2001). Solution structure of a viral DNA repair polymerase. Nature Struct. Biol. 8, 936-941.
 View more publications, see Pubmed listing.
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