Abstract

Although a staggering amount of new structural and dynamical information has been obtained regarding the molecular recognitions processes involving the ubiquitous calcium-binding regulatory protein, calmodulin (CaM), much remains to be understood. This is the overarching goal of the continuing studies proposed by Dr. Joshua Wand, whose research efforts over the past decade have contributed significantly to our growing knowledge. In particular, Dr. Wand proposes to use both conventional and novel NMR techniques to study representatives of three different classes of interactions involving CaM: calcium-dependent target binding, calcium-independent target binding, and the binding of target proteins that contain multiple CaM-binding domains. In order to understand fully the intricate interplay of CaM with its many cellular targets, detailed information about all types of interactions will be needed. The studies proposed by Dr. Wand for the next funding period of this 10-year effort should contribute significant new information and insights.

  Funding Agency

Agency
National Institute of Health (NIH)
Institute
National Institute of Diabetes and Digestive and Kidney Diseases (NIDDK)
Type
Research Project (R01)
Project #
5R01DK039806-15
Application #
6177038
Study Section
Biophysical Chemistry Study Section (BBCB)
Program Officer
Sato, Sheryl M
Project Start
1988-09-01
Project End
2002-03-31
Budget Start
2000-04-01
Budget End
2001-03-31
Support Year
15
Fiscal Year
2000
Total Cost
$253,535
Indirect Cost

  Institution

Name
University of Pennsylvania
Department
Biochemistry
Type
Schools of Medicine
DUNS #
042250712
City
Philadelphia
State
PA
Country
United States
Zip Code
19104

  Publications

Caro, José A; Wand, A Joshua (2018) Practical aspects of high-pressure NMR spectroscopy and its applications in protein biophysics and structural biology. Methods 148:67-80
Farid, Tammer A; Kodali, Goutham; Solomon, Lee A et al. (2013) Elementary tetrahelical protein design for diverse oxidoreductase functions. Nat Chem Biol 9:826-833
Wand, A Joshua; Moorman, Veronica R; Harpole, Kyle W (2013) A surprising role for conformational entropy in protein function. Top Curr Chem 337:69-94
Zelent, B; Buettger, C; Grimsby, J et al. (2012) Thermal stability of glucokinase (GK) as influenced by the substrate glucose, an allosteric glucokinase activator drug (GKA) and the osmolytes glycerol and urea. Biochim Biophys Acta 1824:769-84
Gledhill Jr, John M; Wand, A Joshua (2012) Al NMR: a novel NMR data processing program optimized for sparse sampling. J Biomol NMR 52:79-89
Fu, Yinan; Kasinath, Vignesh; Moorman, Veronica R et al. (2012) Coupled motion in proteins revealed by pressure perturbation. J Am Chem Soc 134:8543-50
Sarachan, Kathryn L; Valentine, Kathleen G; Gupta, Kushol et al. (2012) Solution structure of the core SMN-Gemin2 complex. Biochem J 445:361-70
Moorman, Veronica R; Valentine, Kathleen G; Wand, A Joshua (2012) The dynamical response of hen egg white lysozyme to the binding of a carbohydrate ligand. Protein Sci 21:1066-73
Lichtenstein, Bruce R; Moorman, Veronica R; Cerda, José F et al. (2012) Electrochemical and structural coupling of the naphthoquinone amino acid. Chem Commun (Camb) 48:1997-9
Gledhill Jr, John M; Kasinath, Vignesh; Wand, A Joshua (2011) Optimized linear prediction for radial sampled multidimensional NMR experiments. J Magn Reson 212:240-4

Showing the most recent 10 out of 51 publications