Section: Publications

C. Robert Matthews, Ph.D.

Academic Role: Professor

Faculty Appointment(s) In:
   Biochemistry and Molecular Pharmacology

Other Affiliation(s):
   Center for AIDS Research

Representative Publications

Wu,Y., Matthews, C.R. "Proline replacements and the simplification of the folding mechanism for the alpha subunit of Trp synthase, a TIM barrel protein." J. Mol. Biol., 330, 1131-1144 (2003).

Aria, M., Kataoka, M., Kumajima, K., Matthews, C.R., Iwakura, M. "Effects of the Difference in the Unfolded-state Ensemble on the Folding of Escherichia coli Dihydrofolate Reductase."    J. Mol. Biol. 329, 779-791 (2003).

Svensson, A.K., O'Neil, J.C. Jr., Matthews, C.R. "The Coordination of the Isomerization of a Connserved Non-prolyl cic Peptide Bond with the Rate-limiting Steps in the Folding of Dihydrofolate Reductase." J. Mol. Biol. 326, 569-583 (2003).

Vadrevu, R. Falzone, C.J., Matthews, C.R. "Partial NMR Assignements and Secondary Structure Mapping of the Isolated Subunits of Escherichia coli tryptophan synthase, a 29kDa TIM Barrel Protein." Protein Science, 12, 185-191 (2003).

Knappenberger, J.A., Smith, J.E., Thorpe, S.H., Zitzewitz, J.A., Matthews, C.R. A Buried Polar Residue in the Hydrophobic Interface of the Coiled-coil Peptide, GCN4-p1, Plays a Thermodynamic, not a Kinetic Role in Folding. J. Molec. Biol, 321, 1-6 (2002).

Forsyth, W.R., Matthews, C.R. Folding Mechanism of Indole-3-glycerol Phosphate Synthase from Sulfurous solfactaricus: A Test of the Conservation of Folding Mechanisms Hypothesis in (ba)8 Barrels. J. Molec. Biol., 320, 1119-1133, (2002).

Steinbach, P.J., Ionescu, R., Matthews, C.R. Analysis of Kinetics Using a Hybrid Maximum-Entropy/Nonlinear-Least-Squares Method: Application to Protein Folding. Biophys. J., 82, 2244-2255, (2002).

Wallace, L. and Matthews, C.R. Highly Divergent Dihydrofolate Reductases Conserve Complex Folding Mechanisms. J. Molec. Biol. 315, 193-211, (2002).

Gloss, L. M., Simler, B. R., Matthews, C. R. Rough Energy Landscapes in protein Folding: Dimeric E. coli Trp Repressor Folds Through Three Parallel Channels. J. Molec. Biology 312, 1121-1134, (2001).

Smith, V. F., Matthews, C. R. Testing the Role of Chain Connectivity on the Stability and Structure of Dihydrofolate Reductase from E. coli: Fragment Complementation and Circular Permutation Reveal Stable, Alternatively Folded Forms. Protein Science, 10, 116-128 (2001).

Ibarra-Molero, B., Makhatadze, G. I., Matthews, C. R. Mapping the Energy Surface for the Folding Reaction of the Coiled-Coil Peptide GCN4-p1. Biochemistry, 40, 719-731 (2001).

Bilsel, O., Matthews, C. R. (2000) Barriers in protein folding reactions. Advances in Protein Chemistry 53, 154-207.

Zitzewitz J.A., Ibarra-Molero, B., Fishel, D.R., Terry, K.L., Matthews C.R. (2000) Preformed secondary structure drives the association reaction of GCN4-p1, a model coiled system. J. Mol. Biol. 296, 1105-1116.

Ionescu, R.M., Smith, V.F., O'Neill Jr., J.C., Matthews, C.R. (2000) Multistate equilibrium unfolding of Escherichia coli dihydrofolate reductase: thermodynamic and spectroscopic description of the native, intermediate, and unfolded ensembles. Biochemistry 39, 9540-9550.

O'Neill Jr, J.C., Matthews, C.R. (2000) Localized, stereochemically-sensitive hydrophobic packing in an early intermediate of dihydrofolate reductase of Escherichia coli. J. Mol. Biol. 295, 737-744.

Zitzewitz J.A., Matthews C.R. (1999) Molecular dissection of the folding mechanism of the alpha subunit of tryptophan synthase: an amino-terminal autonomous folding unit controls several rate-limiting steps in the folding of a single domain protein. Biochemistry 38, 10205-10214.

Gualfetti, P., Iwakura, M., Lee, J., Kihara, H., Bilsel, O., Zitzewitz J.A., Matthews C.R. (1999) Apparent radii of the native, stable intermediates and unfolded conformers of the alpha-subunit of tryptophan synthase from E. coli, a TIM barrel protein. Biochemistry 38, 13367-13378.

Gualfetti, P., Bilsel, O., Matthews C.R. (1999) The progressive development of structure and stability during the folding of the alpha subunit of tryptophan synthase from E. coli. Protein Science 8, 1623-1635.

Bilsel O., Zitzewitz J.A., Bowers K.E., Matthews C.R. (1999) Folding mechanism of the alpha-subunit of tryptophan synthase, an alpha/beta barrel protein: global analysis highlights the interconversion of multiple native, intermediate, and unfolded forms through parallel channels. Biochemistry 38, 1018-1029.

Bilsel, O., Yang, L., Zitzewitz J.A., Beechem, J., Matthews C.R. (1999) Time-resolved fluorescence anisotropy study of the refolding reaction of the alpha-subunit of tryptophan synthase reveals a non-monotonic behavior of the rotational correlation time. Biochemistry 38, 4177-4187.

Zitzewitz J.A., Gualfetti, P.J., Perkons, I.E., Wasta, S.A., Matthews C.R. (1999) Identifying the structural boundaries of independent folding domains in the alpha/beta barrel protein, alpha tryptophan synthase. Protein Science 8, 1200-1209.

Zhang, J., Matthews, C.R. (1998) The role of ligand binding in the kinetic folding mechanism of human p21 (H-ras) protein. Biochemistry 37, 14891-14899.

Zhang, J., Matthews, C.R. (1998) Ligand binding is the principal determinant of stability for the p21 (H-ras) protein. Biochemistry 37, 14881-14890.

Gloss, L.M., Matthews C.R. (1998) Mechanism of folding of the dimeric core domain of Escherichia coli trp repressor: a nearly diffusion-limited reaction leads to the formation of an on-pathway dimeric intermediate. Biochemistry 37, 15990-15999.

Gloss L.M., Matthews C.R. (1998) The barriers in the bimolecular and unimolecular folding reactions of the dimeric core domain of Escherichia coli Trp repressor are dominated by enthalpic contributions. Biochemistry 37, 16000-16010.

Shao X., Matthews C.R. (1998) Single-tryptophan mutants of monomeric tryptophan repressor: optical spectroscopy reveals nonnative structure in a model for an early folding intermediate. Biochemistry 37, 7850-7858.

Goldberg, M., Zhang, J., Sondek, S., Matthews, C.R., Fox, R., Horwich, A. (1997) Native-like structure of a protein-folding intermediate bound to the chaperonin GroEL. Proc. Natl. Acad. Sci. USA 94, 1080-1085.

Gegg C.V., Bowers K.E., Matthews C.R. (1997) Probing minimal independent folding units in dihydrofolate reductase by molecular dissection. Protein Science 6, 1885-92.

Gegg C.V., Bowers K.E., Matthews C.R. (1997) A general approach for the design and isolation of protein fragments: the molecular dissection of dihydrofolate reductase in Techniques in Protein Chemistry VII (Marshak, D., Ed.) pp. 439-448, Academic Press, Inc., San Diego, CA.

Shao X., Hensley P., Matthews C.R. (1997) Construction and characterization of monomeric tryptophan repressor: a model for an early intermediate in the folding of a dimeric protein. Biochemistry 36, 9941-9949.

Gloss L.M., Matthews C.R. (1997) Urea and thermal equilibrium denaturation studies on the dimerization domain of Escherichia coli Trp repressor.Biochemistry 36, 5612-5623.

Office: LRB 928, Lab 970 A-D
Phone: 508 856-2251
E-mail: C.Robert.Matthews@umassmed.edu
Keywords: Protein Folding, Biophysics, Biochemistry

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