Curriculum
vitae
Timothy M. Logan
Education
1985 - 1991. Ph. D., Organic Chemistry. University of
Chicago, Chicago, IL.
Thesis Title: Monitoring Intact Metabolism using 13C-NMR
Spectroscopy
Thesis Advisor: David G. Lynn
1983
- 1985. Undergraduate Studies in Chemistry.
Calvin College, Grand Rapids, MI.
1979
- 1983. B.S., Physiology. Michigan State
University, E. Lansing, MI.
Professional
Experience
2005
– present Interim Director, Institute
of Molecular Biophysics, Kasha Laboratory
2004
- present Participating Investigator,
Consortium for Functional Glycomics
2002 - present Director, Molecular Biophysics Graduate
Program, Florida State
University, Tallahassee, FL
2000 - present Associate Professor, Chemistry Department,
Florida State University,
Tallahassee, FL
1997 - present Associate Director, High Resolution NMR
Program, National High
Magnetic Laboratory, Tallahassee, FL.
1996 - present Adjunct Faculty, Biology Department,
Florida State University,
Tallahassee, FL
1994 - 2000 Assistant Professor, Chemistry
Department. Florida State University,
Tallahassee, FL.
1994 - present Faculty, Center for Interdisciplinary
Magnetic Resonance,
National High Magnetic Field Laboratory, Tallahassee, FL.
1991 -
1994 Post-Doctoral
Research Associate with Dr. Stephen W. Fesik.
Abbott Laboratories, Abbott Park, IL.
1991 Post-Doctoral
Research Associate with Dr. Kevin S. Peters.
University of Colorado, Dept. of Chemistry &
Biochemistry, Boulder, CO.
Awards
and Professional Affiliations
R.J. Boucek Research
Award Winner, American Heart Association, Fl Affiliate, 1999
Lonza Research Creativity Prize Award Winner, Lonza
Biologics, 1999
Bernard Smaller Prize for Excellence in Magnetic Resonance
Research. University of Chicago, 1990.
American Chemical Society, 1986 - present
American Association for the Advancement of Science, 1987 -
present
Funded
Research Projects
National Institute of Health (2R01 AI021628, J.R. Murphy,
Boston University PI; Logan is FSU subcontract PI); Title: “Peptide activators
of diphtheria toxin repressor”. Total
Award: $940,308. T.M. Logan, co-P.I.
National Science Foundation / National High Magnetic Field
Laboratory (500/5032). 8/99-7/ 01. Total Award: $132,592. Title: “Triple
Resonance Microcoils for High-Field NMR Spectroscopy”. T.M. Logan, P.I.
American Heart Association (9950887V). 7/99 - 6/01. Total
award: $110,000. Title: “Regulation of Signal Transduction and Transcription by
SH3 Domains”. T.M. Logan, P.I.
National Institutes of Health (R21 GM58143). 7/98 - 6/00.
Total award: $201,482. Title: “Producing
Homogeneous Glycoproteins for Structural Biology”. T.M. Logan, P.I.
National Science Foundation. (DBI 9604787) 2/97 - 1/99.
Total Award: $240,255. Title: “Replacement of a 500 MHz NMR Console at
Florida State University”. T.M. Logan,
P.I.
National Institutes of Health. “Research Supplement for
Under-Represented Minorities” to GM54035 (6/97 - 5/99. Total Award: $11,336. T.M. Logan, P.I.
National Institutes of Health F.I.R.S.T award (29 GM54035)
5/96 - 4/01. Total award: $500,822. Title: “Unfolded States and Protein
Stability”. T.M. Logan, P.I.
American Chemical Society, Petroleum Research Fund. 6/95 -
5/97. Total award $20,000. Title
“Non-random Random Coils: The Role of the Unfolded State in Protein Folding”. T.M.
Logan, P.I.
American Heart Association, Florida Division. 7/96 - 6/99 Total Award: $150,000. (declined
award due to AHA regulations that precluded co-award with R29 from NIH). Title:
“Molecular Mechanisms of Nerve Growth Inhibition: Solution Structure of Thy-1”.
T.M.
Logan, P.I.
Refereed
Publications
1. Fu R, Brey WW, Shetty K, Gor'kov P, Saha S, Long JR, Grant
SC, Chekmenev EY, Hu J, Gan Z, Sharma M, Zhang F, Logan TM, Bruschweller R,
Edison A, Blue A, Dixon IR, Markiewicz WD, Cross TA. (2005) Ultra-wide bore 900
MHz high-resolution NMR at the National High Magnetic Field Laboratory. J. Magn. Reson. 177, 1-8.
2. Spencer, D.S., Xu, K. Logan, T.M., and Zhou, H.-X. (2005).
Effects of pH, salt, and macromolecular crowding on the stability of
FK506-binding protein: an integrated experimental and theoretical study. J. Mol. Biol. 351, 219-232.
3. Rangachari, V., Marin, C., Bienkiewicz, E.A., Semavina, M.,
Guererro, L., Love, J.F., Murphy, J.R., and Logan, T.M. (2005). Sequence of
ligand binding and structure change in diphtheria toxin repressor upon
activation by divalent transition metals. Biochemistry
44, 5672-5682.
4. Kim, J., Brych, S.R., Logan, T.M. and Blaber, M. (2005)
Sequence swapping does not result in conformation swapping for the beta4/beta5
and beta8/beta9 beta-hairpin turns in human acidif fibroblast growth factor. Protein Sci. 14:351-359.
5. Wylie, G.P., Rangachari, V., Bienkiewicz, E., Marin V.,
Bhattacharya, N., Love, J.F., Murphy, J.R., and Logan, T.M. (2005).
Prolylpeptide binding by trhe prokaryotic SH3-like domain of the diphtheria
toxin repressor: A regulatory switch. Biochemistry
44, 40-051.
6.
Brych S.R., Dubey, V.K., Bienkiewicz, W., Lee, J., Logan,
T.M. and Blaber, M. (2004) Symmetric primary and tertiary structure mutations
within a symmetric superfold: a solution, not a constraint, to achieve a
foldable polypeptide. J. Mol. Biol. 344,
769-780.
7. Green, T., O. Ganes, K. Perry, L. Smith, L.H. Phylip, T.M.
Logan, S.J Hagen, B.M. Dunn and A.S. Edison. (2004) “IA3, an Aspartic
Proteinase Inhibitor from Saccharomyces cerevisiae, is Intrinsically
Unstructured in Solution”, Biochemistry
43, 4071-4081.
8. Love, J., Guerrero, L., Marin, V., Logan, T.M. & Murphhy, J.R. (2004)
“Activation of the diphtheria toxin repressor (DtxR) by transition metal ions
occurs via a three-step mechanism”, in
the press, Proc. Natl. Acad. Sci., USA.101,2506-2511.
9. Mehndiratta, P., Walton, W.J., Pulido, S., Hare, J.,
Parthasarathy, G., Emmett, M., Marshall, A.G., & T.M. Logan. (2004)
“Expression, Purification and Characterization of Chicken Thy-1 Expressed in
Lec-1 and Insect Cells for Reduced Glycoform Heterogeneity”, Protein Expression and Purification,
33(2),274-287.
10. Li, Y., T.M. Logan, A.S. Edison, and A. Webb. (2003) “Design
of small-volume HX and triple resonance probes for improved limits of detection
in protein NMR experiments”, J. Magn.
Reson. 164, 128-135.
11. Kim, J., Brych, S.R., Lee, J., Logan, T.M. and Blaber, M.
(2003) “Identification of a Key Structural Element for Protein Folding Within b-Hairpin Turns”, J.
Mol. Biol. 328, 951-961
12. Korepanova, A., C. Douglas, & T.M. Logan. (2002)
“Glutamine53 is a Gatekeeper Residue in the Folding of the FK506 Binding
Protein”, J. Mol. Biol. 323, 285-296.
13. Brych, S.R., S.I. Blaber, T.M. Logan, M. Blaber. (2001)
“Structure and stability effects of mutations designed to increase the primary
sequence symmetry within the core region of a b-trefoil.” Protein Science 10, 2587-2599.
14. Korepanova, A., Leyngold, I. & T.M. Logan. (2001)
“N-terminal extension changes the folding mechanism of the FK506 binding
protein.” Protein Science 10,
1905-1910.
15. Twigg, P.D., G. Parthasarathy, L. Guerrero, T.M. Logan &
D.l.D.Caspar. (2001) “Disorder-to- Order Transition in the Regulation of
Diphtheria Toxin Repressor Activity”. Proc.
Natl. Acad. Sci., USA 98, 11259-11264.
16. Callihan, D.E., & T.M. Logan. “Conformations of Peptide
Fragments from the FK506 Binding Protein: Comparison to the Native and
Urea-Unfolded States”. (1999) J. Mol.
Biol. 285, 2161- 2175.
17. Wang, G., G. Wylie, P. Twigg, D.L.D. Caspar, J.R. Murphy
& T.M. Logan. “Solution structure and proposed function of the C-terminal
SH3 domain in Diphtheria Toxin Repressor”. (1999) Proc.
Natl. Acad. Sci., USA 66, 6119-6124.
18. Murali, N., G. Wang, C. Jolivet, & T.M. Logan.
“Application of a High Resolution Superconducting NMR Probe in Natural Product
Structure Determination” (1999) Magn. Reson. Chem. 37, 512-515.
19. Twigg, P.D., G.P. Wylie, G. Wang, D.L.D. Caspar, J.R. Murphy
& T.M. Logan. “Expression and Assignment of the 1H, 15N,
and 13C Resonances of the C-terminal Domain of the Diphtheria Toxin
Repressor”.(1999) J. Biomol. NMR 13,
197-198.
20. Zhang, Z., Li, W., Li, M., Logan, T.M., & A.G. Marshall.
“Human recombinant [C22A] FK506 binding protein amide hydrogen exchange rates
from mass spectrometry match and extend those from NMR.” (1997) Protein Science 6, 2203-2217.
21. Marshall, A.G., M.W. Senko, W. Li, M. Li, S. Dillon, S.
Guan, & T.M. Logan. “Protein Molecular Mass to 1 Da by 13C, 15N
Double-Depletion and FT-ICR Mass Spectrometry.”
(1997) J. Am. Chem. Soc. 119,
433-434.
22. Callihan, D., J. West, S. Kumar, B.I. Schweitzer, & T.M.
Logan. “Simple Distortion-Free Homonuclear Spectra of Peptides and Nucleic
Acids in Water using Excitation Sculpting.” (1996) J. Magn. Reson. 112B, 82-85.
23. Vincent, S.J.F., Zwahlen, C., Bolton, P.H., T.M. Logan, &
G. Bodenhausen. “Measurement of cross-relaxation between amide protons in
N-15-enriched proteins with suppression of spin diffusion” (1996) J. Am. Chem. Soc. 118, 3531-3532.
24. Zhou, M.-M., Meadows, R.P., Logan, T.M., Yoon, H.S., Wade,
W.S., Ravichandran, K.S., Burakoff, S.J., & Fesik, S.W. 1995. “Solution
structure of the shc SH2 domain complexed with a tyrosine-phosphorylated
peptide from the T-cell receptor”. (1995) Proc.
Natl. Acad. Sci. USA 92, 7784-7788.
25.
Logan, T.M., Zhou, M.-M., Nettesheim, D.G., Meadows, R.P.,
van Etten, R. & Fesik, S.W. “Solution structure of a low molecular weight
protein tyrosine phosphatase.” (1994) Biochemistry 33, 11087-11096.
26.
Zhou, M.-M., Logan, T.M., Theriault, Y.T., van Etten, R.
& Fesik, S.W. “Backbone 1H, 13C, and 15N assignments
and secondary structure of bovine low molecular weight phosphotyrosyl protein
phosphatase.” (1994) Biochemistry 33,
5221-5229.
27.
Logan, T.M., Theriault, Y.T. & Fesik, S.W. “Structural
characterization of the FK506 binding protein unfolded in urea and guanidine
hydrochloride.” (1994) J. Molecular Biology 236, 637- 648.
28.
Logan, T.M., Olejniczak, E.T., Xu, R.X., & Fesik, S.W.
“A general method for assigning NMR spectra of denatured proteins using 3D
HC(CO)NH-TOCSY triple resonance experiments.” (1993) J. Biomolecular NMR 3, 225-231.
29.
Egan, D.A., Logan, T.M., Liang, H., Matayoshi, E., Fesik,
S.W. & Holzman, T.F. “Equilibrium denaturation of recombinant human FK506
binding protein in urea.” (1993) Biochemistry
32, 1920-1927.
30.
Theriault, Y.T., Logan, T.M., Meadows, R.P., Yu, L.,
Olejniczak, E.T., Holzman, T.F., Simmer, R.L., & Fesik, S.W. “Solution
structure of the cyclosporin A/cyclophilin complex by NMR” (1993) Nature 361, 88-91.
31.
Peters, K.S., Watson, T. & Logan, T.M. “Photoacoustic
calorimetry of human carboxyhemoglobin.” (1992) J. Am. Chem.Soc.114, 4276-4278.
32.
Logan, T.M., Olejniczak, E.T., Xu, R.X., & Fesik, S.W.
“Sidechain and backbone assignments in isotopically labeled proteins from two
heteronuclear triple resonance experiments.” (1992) FEBS Lett. 314, 413-418.
33.
Logan, T.M., Zhong, P., & Lynn, D.G. “Metabolic
thermotolerance: magnetic resonance detected protection of glutamate synthase.”
(1992) Biochemistry 32, 7256-7263.
34.
Neri, P., Meadows, R., Gemmecker, G., Olejniczak, E.,
Nettesheim, D., Logan, T., Simmer, R., Helfrich, R., Severin, J., & Fesik,
S. “1H, 13C and 15N backbone assignments of
cyclophilin when bound to cyclosporin A (CsA) and preliminary structural
characterization of the CsA binding site.” (1991) FEBS Lett. 294, 81-88.
35.
McLaggen, D., Logan, T.M., Lynn, D.G., & Epstein, W.
“Involvement of gamma-glutamyl peptides in osmoadaptation of Eschericia coli.” (1990) J. Bacteriol. 172, 3631-3636.
Invited
Lectures
November 2003.
Inaugural Lecture in Chemical Biology, University of West Florida. “Regulation
of Diphtheria Toxin Repressor Protein”.
August, 2002. American Chemical Society, San Juan, Puerto
Rico. “Regulation of Diphtheria Toxin Repressor Protein”.
November, 2001. Georgia State University, Department of
Chemistry, Atlanta, GA.“Disordered to Ordered Transition in the Activation of
Diphtheria Toxin Repressor.”
November, 2001. Enmory University, Department of Chemistry,
Atlanta, GA.“Disordered to Ordered Transition in the Activation of Diphtheria
Toxin Repressor.”
November, 2001. Wayne State University Medical School,
Department of Biochemistry, Wayne, MI.“Disordered to Ordered Transition in the
Activation of Diphtheria Toxin Repressor.”
October, 2001. SEMRC, Gainesville, FL. “Disordered to
Ordered Transition in the Activation of Diphtheria Toxin Repressor.”
September, 2001. SERMACS, Savannah, GA. “Conformational
Averaging in the Unfolded State of the FK506 Binding Protein Affects the
Folding Pathway”.
November, 2000. University of Florida, Gainesville, FL.
“Solution structure and peptide binding by a prokaryotic SH3 domain.”
October, 2000. Clarkson University, Biology Department.
“Protein folding as a regulatory mechanism in a prokaryotic transcriptional
regulator”.
November, 1999. Trinity University, San Antonio, TX.
“Investigating long-range structure in unfolded proteins”
August, 1999. Sturtevant Symposium, Tallahassee, FL.
“Structural Characterization of the Urea Unfolded State of FK506 Binding
Protein”
June, 1999. Clarkson University. “Frontiers of NMR
Spectroscopy: What’s New and What’s Hot”
June 1999. Northeast Regional ACS Meeting. Title: “Solution
structure and peptide binding by a prokaryotic SH3 domain”.
May, 1999. FAME / FLACS, Orlando, FL. “Solution Structure
and Peptide Binding by C-terminal Domain of Diphtheria Toxin Repressor, a Prokaryotic
SH3 Domain”.
May, 1999. 4th NATO ASI Summer Course in Magnetic Resonance
and Structural Biology, Erice, Italy. “Solution structure and peptide binding
by a prokaryotic SH3 domain”.
May 1998. FAME / FLACS Meeting, Orlando, FL. “Chemical shift
assignments, secondary structure and folding topology of the C-terminal domain
of the diphtheria toxin repressor protein.”
November, 1997. 29th SEMRC, Gainesville, FL. “Chemical shift
assignments, secondary structure, and folding topology of the C-terminal domain
of the diphtheria toxin repressor protein.”
October, 1997. Calvin College, Grand Rapids, MI. “Structural
Characterization of Unfolded Proteins using Multidimensional NMR Spectroscopy”
October, 1997. Hope College, Holland, MI. “Structural
Characterization of Unfolded Proteins using Multidimensional NMR Spectroscopy”
September, 1997. U. South Florida, Tamp, FL. “Structural
Characterization of Unfolded Proteins using Multidimensional NMR Spectroscopy”
July, 1997. Center for Interdisciplinary Magnetic Resonance,
NHMFL, Tallahassee, FL. “Frontiers in Structural Characterization of Unfolded
Proteins”
January, 1997. PENCE Lecture, U. Toronto, Toronto, ON.
“Structural Characterization of Unfolded Proteins using Multidimensional NMR
Spectroscopy”
Posters
& Abstracts
April, 2001. American
Society for Mass Spectrometry.” “Characterizing recombinant chicken Thy-1 with
reduced glycoform distribution by MALDI-TOC and ESI FT-ICR MS of AspN digested
glycoprotein.”. P. Mehndiratta, S. Pulido, M.R. Emmett, W.J. walton, J. hare,
A.G. Marshall, & T.M. Logan
October, 1999.
Glycoprotein Society Meeting. “Cloning and High-level Expression of
Avian Thy-1 in Mammalian and Insect Cell Systems”. P. Mehndiratta, M. Tway, G.
Parthasarathy, & T.M. Logan
August, 1999. Sturtevant Symposium. “Conformations of
Peptide Fragments from FKBP: Comparison to the Native and Urea-unfolded
States”. D. Callihan & T.M. Logan
March, 1999. 4th Johns Hopkins Folding Meeting.
“Conformations of Peptide Fragments from FKBP: Comparison to the Native and Urea-unfolded
States”. D. Callihan & T.M. Logan
January, 1999. Frontiers of NMR in Molecular Biology,
Keystone Meeting. “Solution structure and peptide binding by the C-terminal
domain of the diphtheria toxin repressor protein”, G.Wang, G. Wylie, P Twigg,
J.R. Murphy, D.L.D. Caspar & T.M. Logan.
October, 1998. NMR Technologies Meeting. “Characterization
of a high-resolution NMR probe made from high temperature superconducting
materials, and application to natural product structure determination.” M.
Murali, G. Wang, C. Jolivet & T.M. Logan
July, 1998. 12th Protein Society Meeting. “Solution
structure and peptide binding by the C- terminal domain of the diphtheria toxin
repressor protein”, G.Wang, G. Wylie, P Twigg, J.R. Murphy, D.L.D. Caspar &
T.M. Logan.
January, 1998. Magnetic Resonance Gordon Conference.
“Characterization of a high- resolution NMR probe made from high temperature
superconducting materials, and application to natural product structure
determination.” M. Murali, G. Wang, C. Jolivet & T.M. Logan
November, 1997. 29th SEMRC. “Probing long-range interactions
in unfolded proteins”, D. Callihan, P. Fajer, K. Hideg, T. Kalai & TM Logan
July, 1997 11th Protein Society Meeting. “Probing long-range
interactions in unfolded proteins”, D. Callihan, P. Fajer, K. Hideg, T. Kalai
& TM Logan
July, 1997. 11th Protein Society Meeting. “Identification of
E. coli protein profiles by HPLC/FT-
ICR mass spectrometry of proteins grown on 13C,15N
doubly-depleted media” W. Li, M. Li, Z. Zhang, M. Emmett, T.M. Logan, & A.G.
Marshall.
October, 1996 NIH Protein Folding Meeting. “Local versus
long range interactions in secondary structure formation in unfolded proteins”
D. Callihan, T. Shepherd, L. Stirling, & T.M. Logan
July, 1996 10th Protein Society Meeting “FK506 Binding protein
conformation from protein amide hydrogen exchange determined by FT-ICR mass
spectrometry”. Z. ZHang, W. Li, M. Li, TM Logan, S. Guan & AG Marshall.
July, 1996 10th Protein Society Meeting “Sharpening of
protein mass spectrometric profiles by depletion of minor isotopes of carbon
and nitrogen.” Z. Zhang, M.W. Senko, M. Li, T.M. Logan & AG Marshall.
July, 1996 10th Protein Society Meeting. “Local versus
Long-Range Interactions in Non- Random Structure Formation in Unfolded
Proteins” D. Callihan, T.M. Shepherd, L. Stirling, & T.M. Logan
July, 1996. 10th Protein Society Meeting. “Does Non-Random
Structure in an Unfolded Protein Affect Native State Stability?” Ming Li and Timothy M. Logan.
July, 1996. 10th Protein Society Meeting. “Isolation and
Characterization of a Novel Thy-1 Saffron from Chicken Brain” G. Parthasarathy,
J.E. Williams, & T.M. Logan
December, 1995. 27th SEMRC, Tallahassee, FL. “Peptide models
of unfolded FKBP” D.Callihan & TM Logan.
Teaching
Experience
Courses
Taught: BCH
4053 General Biochemistry I
BCH 5745 Chemical and Physical Characterization of
Biopolymers
BCH 5886 Macromolecular NMR Spectroscopy
BCH 6896r & BCH 6897r
Graduate Seminar in Biochemistry and
Molecular Biophysics
Students and Other Trainees:
Postdoctoral Associates: Dr. Guangshun Wang, Dr. Steven
Whitten, Dr. R.
Vijayraghavan.
PhD Students:
Dana Callihan (Ph.D., 2000); Alla Korepanova (Ph.D., 2001);
Gregory Wylie (Ph.D., 2002); Promod Mehndiratta (Ph.D.,
2002);
Vedrana Marin, Wendy Walton, Ilker Sen, Maria Semavina,
Sumiko Takahashi, Nilakshee Bhattacharya, Aga Kasprczyk
Masters Students: Ming Li (1997); Kefei Zhou (2000), Laura
Mertz
(2000).
Undergraduate Students: 20; 8 currently in graduate or
medical school.
Graduate Student Committees:
23 in Chemistry, Biology,
Molecular
Biophysics, and
Engineering.