Biochemistry & Biophysics

J. Martin Scholtz

scholtz Associate Professor of Medical Biochemistry and Genetics and of Biochemistry and Biophysics
Center for Advanced Biomolecular Research
Chemistry/Biology Interface Training Program
Molecular Biophysics Training Program

Phone: (979) 845-0828
Email: jm-scholtz@tamu.edu
Visit the Scholtz lab Home Page
B.S. University of Nebraska, Lincoln (1984)
Ph.D. University of California, Berkeley (1989)
Postdoc. Stanford University (1989-93)

Joined Texas A&M faculty in 1993

Helix Formation in Protein Folding and Stability
We are interested in the problem of protein folding - a description of the mechanism by which a protein adopts a given three dimensional structure using only the information encoded in the primary sequence of amino acids. We are currently testing the idea that protein folding and stability can be described in a hierarchical fashion: building stability and structure from the primary sequence through secondary structure to the tertiary structure of proteins. Toward this end, our efforts have concentrated on the role helix stability plays in governing protein folding and stability in several model proteins.

A variety of biochemical and biophysical techniques are employed to explore the energetics of helix formation in model peptides, in peptides derived from helical structures of proteins and in intact proteins. Our goal is to determine quantitative rules for helix formation in proteins, realizing that these rules may serve as useful tools to predict protein structure from sequence.

Recently, we have initiated a project on transmembrane helix formation with the realization that the "rules" for helix formation in membranes are likely to be very different than those for water-soluble proteins. Again, our goal is to formulate energetic rules for transmembrane helix formation that will aid in prediction and future protein design strategies.

Recent Publications
  1. McCluggage LK & Scholtz JM (2010) Golimumab: a tumor necrosis factor alpha inhibitor for the treatment of rheumatoid arthritis. Ann Pharmacother 44: 135-44
  2. McLean JR, McLean JA, Wu Z, Becker C, Pérez LM, Pace CN, Scholtz JM & Russell DH (2010) Factors that influence helical preferences for singly charged gas-phase peptide ions: the effects of multiple potential charge-carrying sites. J Phys Chem B 114: 809-16
  3. Cho Y, Sagle LB, Iimura S, Zhang Y, Kherb J, Chilkoti A, Scholtz JM & Cremer PS (2009) Hydrogen bonding of beta-turn structure is stabilized in D(2)O. J Am Chem Soc 131: 15188-93
  4. Fu H, Grimsley GR, Razvi A, Scholtz JM & Pace CN (2009) Increasing protein stability by improving beta-turns. Proteins 77: 491-8
  5. López-Alonso JP, Diez-García F, Font J, Ribó M, Vilanova M, Scholtz JM, González C, Vottariello F, Gotte G, Libonati M & Laurents DV (2009) Carbodiimide EDC Induces Cross-Links That Stabilize RNase A C-Dimer against Dissociation: EDC Adducts Can Affect Protein Net Charge, Conformation, and Activity. Bioconjug Chem
  6. Grimsley GR, Scholtz JM & Pace CN (2009) A summary of the measured pK values of the ionizable groups in folded proteins. Protein Sci 18: 247-51
  7. Pace CN, Grimsley GR & Scholtz JM (2009) Protein ionizable groups: pK values and their contribution to protein stability and solubility. J Biol Chem 284: 13285-9
  8. Shaw KL, Scholtz JM, Pace CN & Grimsley GR (2009) Determining the conformational stability of a protein using urea denaturation curves. Methods Mol Biol 490: 41-55
  9. Ilinskaya ON, Koschinski A, Repp H, Mitkevich VA, Dreyer F, Scholtz JM, Pace CN & Makarov AA (2008) RNase-induced apoptosis: fate of calcium-activated potassium channels. Biochimie 90: 717-25
  10. Trevino SR, Scholtz JM & Pace CN (2008) Measuring and increasing protein solubility. J Pharm Sci 97: 4155-66
  11. Alston RW, Lasagna M, Grimsley GR, Scholtz JM, Reinhart GD & Pace CN (2008) Peptide sequence and conformation strongly influence tryptophan fluorescence. Biophys J 94: 2280-7
  12. Alston RW, Lasagna M, Grimsley GR, Scholtz JM, Reinhart GD & Pace CN (2008) Tryptophan fluorescence reveals the presence of long-range interactions in the denatured state of ribonuclease Sa. Biophys J 94: 2288-96
  13. Trevino SR, Schaefer S, Scholtz JM & Pace CN (2007) Increasing protein conformational stability by optimizing beta-turn sequence. J Mol Biol 373: 211-8
  14. Wei Y, Huyghues-Despointes BM, Tsai J & Scholtz JM (2007) NMR study and molecular dynamics simulations of optimized beta-hairpin fragments of protein G. Proteins 69: 285-96
  15. Goodrich CP, Kirmizialtin S, Huyghues-Despointes BM, Zhu A, Scholtz JM, Makarov DE & Movileanu L (2007) Single-molecule electrophoresis of beta-hairpin peptides by electrical recordings and Langevin dynamics simulations. J Phys Chem B 111: 3332-5
  16. Trevino SR, Scholtz JM & Pace CN (2007) Amino acid contribution to protein solubility: Asp, Glu, and Ser contribute more favorably than the other hydrophilic amino acids in RNase Sa. J Mol Biol 366: 449-60
  17. Thurlkill RL, Grimsley GR, Scholtz JM & Pace CN (2006) Hydrogen bonding markedly reduces the pK of buried carboxyl groups in proteins. J Mol Biol 362: 594-604
  18. Razvi A & Scholtz JM (2006) Lessons in stability from thermophilic proteins. Protein Sci 15: 1569-78
  19. Thurlkill RL, Grimsley GR, Scholtz JM & Pace CN (2006) pK values of the ionizable groups of proteins. Protein Sci 15: 1214-8
  20. Razvi A & Scholtz JM (2006) A thermodynamic comparison of HPr proteins from extremophilic organisms. Biochemistry 45: 4084-92
Google