Scientific Publications:

Emerson, M.F. (maiden name)

1.  Emerson, M.F. and Holtzer, A., “On the Ionic Strength Dependence of Micelle Number I”, J. Phys. Chem., 69, 3718-3721 (1965). https://doi.org/10.1021/j100895a010

2.  Emerson, M.F. and Holtzer, A., “On the Ionic Strength Dependence of Micelle Number II”, J. Phys. Chem., 71, 1898-1907 (1967). https://doi.org/10.1021/j100865a057

3.  Emerson, M.F. and Holtzer, A., “The Hydrophobic Bond in Micellar Systems. Effects of the Various Additives on the Stability of Micelles of Sodium Dodecyl Sulfate and n-Dodecyltrimethylammonium Bromide”, J. Phys. Chem., 71, 3320-3330 (1967). https://doi.org/10.1021/j100869a031

4.  Olander, J., Emerson, M.F. and Holtzer, A., “On the Dissociation and Reassociation of the Polypeptide Chains of Tropomyosin and Paramyosin”, J. Amer. Chem. Soc., 89, 3058-3059 (1967). https://doi.org/10.1021/ja00988a051

5.  Holtzer, A. and Emerson, M.F. “On the Utility of the Concept of Water Structure in the Rationalization of the Properties of Aqueous Solutions of Proteins and Small Molecules”, J. Phys. Chem., 73, 26-33 (1969). https://doi.org/10.1021/j100721a005

6.  Holtzer, A. and Holtzer, M.F., “On the Use of the van't Hoff Relation in Determinations of the Enthalpy of Micelle Formation”, J. Phys. Chem., 78, 1442-1443 (1974). https://doi.org/10.1021/j100607a026

7.  Holtzer, M.E., Holtzer, A. and Skolnick, J., “α-Helix to Random-Coil Transitions of Two-Chain, Coiled-Coils. Theory and Experiments for Thermal Denaturation of α-Tropomyosin”, Macromolecules, 16, 173-180 (1983). 023-Helix-to-random-coil-transition.pdf (bpb-us-w2.wpmucdn.com)

8.  Holtzer, M.E., Holtzer, A. and Skolnick, J., “α-Helix to Random-Coil Transitions of Two-Chain, Coiled-Coils. Theory and Experiments for Thermal Denaturation of α-Tropomyosin at Acidic pH”, Macromolecules, 16, 462-465 (1983). https://doi.org/10.1021/ma00237a024

9.  Holtzer, A., Isom, L.L. and Holtzer, M.E., “On the Rationalization of the Helix-Coil Theory for Protein Chains in Solutions Containing Dodecyl Sulfate. Experiments on α-Tropomyosin and Bovine Serum Albumin”, Macromolecules, 16, 1063-1068 (1984). https://doi.org/10.1021/ma00241a007

10. Holtzer, M.E., Breiner, T. and Holtzer, A., “Hetero-α-Helical, Two-Chain Coiled-Coils.  α-β Hybrid Tropomyosin”, Biopolymers, 23, 1811-1833 (1984). https://doi.org/10.1002/bip.360231003

11. Isom, L.L., Holtzer, M.E. and Holtzer, A., “The α-Helix to Random-Coil Transition of Two-Chain, Coiled-Coils. Experiments on the Thermal Denaturation of α-Tropomyosin and β-Tropomyosin”, Macromolecules, 17, 2445-2447, (1984). https://doi.org/10.1021/ma00141a042

12. Yukioka, S., Noda, I., Nagasawa, M., Holtzer, M.E. and Holtzer, A., “The α-Helix to Random-Coil Transition of Two-Chain, Coiled-Coils. Light Scattering Experiments on the Thermal Denaturation of α-Tropomyosin”, Macromolecules, 18, 1083-1086, (1985). https://doi.org/10.1021/ma00148a006

13. Holtzer, M.E., Askins, K. and Holtzer, A., “α-Helix to Random Coil Transition of Two-Chain, Coiled Coils. Experiments on the Thermal Denaturation of Doubly Crosslinked ββ-Tropomyosin”, Biochemistry, 25, 1688-1692 (1986). https://doi.org/pdf/10.1021/bi00355a037

14. Holtzer, A. and Holtzer, M.E., “A Statistical Test of the Proposition that Intra-Helix Salt Bridges Constitute a Significant Stabilizing Feature of the Tropomyosin Coiled Coil Structure”, Macromolecules, 20, 671-675 (1987). https://doi.org/10.1021/ma00169a034

15. Bracken, W.C., Carey, J., Holtzer, M.E. and Holtzer, A., “α-Helix to Random-Coil Transitions in Two-Chain, Coiled Coils. Experiments on the Thermal Denaturation of ββ-Tropomyosin Crosslinked Selectively at C190”, Biopolymers, 27, 1223-1237 (1988). https://doi.org/10.1002/bip.360270804

16. Holtzer, M.E., Kumar, S., Holtzer, A. and Crimmins, D.L., “The Circular Dichroism of Two-Chain Coiled Coils. Experiments on Tropomyosin and Tropomyosin Segments in the Tyrosine/Disulfide Spectral Region”, Biopolymers, 28, 1597-1612 (1989). https://doi.org/10.1002/bip.360280909

17. Holtzer, M.E., Bracken, W.C. and Holtzer, A., “α-Helix-to-Random-Coil Transitions of Two-Chain Coiled Coils. Experiments on the Thermal Denaturation of ββ-Tropomyosin Selectively Crosslinked at C36”, Biopolymers, 29, 1045-1056 (1990). https://doi.org/10.1002/bip.360290615

18. Holtzer, A., Holtzer, M.E. and Skolnick, J., “Does the Unfolding Transition of Two-Chain Coiled-Coil Proteins Involve a Continuum of Intermediates?”, in Protein Folding, Gierasch, L.M. and King, J., eds., pp. 177-190, AAAS, Washington, D.C. (1990).

19. Holtzer, M.E., Holtzer, A. and Crimmins, D.L., “The Effect of Sulfhydryl Blocking Groups on the Thermal Unfolding of αα-Tropomyosin Coiled Coils”, Biochem. Biophys. Res. Commun., 166, 1279-1283 (1990). https://doi.org/10.1016/0006-291x(90)91004-c

20. Mo., J., Holtzer, M.E. and Holtzer, A., “The Thermal Denaturation of Nonpolymerizable αα-Tropomyosin and Its Segments as a Function of Ionic Strength”, Biopolymers, 30, 921-927 (1990). https://doi.org/10.1002/bip.360300907

21. Holtzer, M.E. and Holtzer, A., “α-Helix-to-Random-Coil Transitions of Two-Chain Coiled Coils. Experiments on the Equilibrium Thermal Unfolding of Isolated Segments of αα-Tropomyosin”, Biopolymers, 30, 985-993 (1990). https://doi.org/10.1002/bip.360300913

22. Holtzer, A. and Holtzer, M.E., “ α-Helix-to-Random-Coil Transitions of Two-Chain Coiled Coils. The Use of Physical Models In Treating Thermal Denaturation Equilibria of Isolated Sub-Sequences of αα-Tropomyosin”, Biopolymers, 30, 1231-1241, (1990). https://doi.org/10.1002/bip.360301308

23. Mo, J., Holtzer, M.E. and Holtzer, A., “Kinetics of Self-Assembly of αα-Tropomyosin Coiled Coils From Unfolded Chains”, Proc. Natl. Acad. Sci. USA, 88, 916-920 (1991). Kinetics of self-assembly of alpha alpha-tropomyosin coiled coils from unfolded chains. (pnas.org)

24. Crimmins, D.L. and Holtzer, M.E., “Chromatographic and Physical Studies of Tropomyosin in Aqueous/Organic Media at Low pH”, J. Chromatogr., 543, 327-343 (1991). https://doi.org/10.1016/S0021-9673(01)95785-1

25. Sturtevant, J.M., Holtzer, M.E. and Holtzer, A., “A Scanning Calorimetric Study of the Thermally Induced Unfolding of Various Forms of Tropomyosin”, Biopolymers, 31, 489-495 (1991). https://doi.org/10.1002/bip.360310504

26. Ozeki, S., Kato, T., Holtzer, M.E. and Holtzer, A., “The Kinetics of Chain Exchange in Two-Chain Coiled Coils: αα- and ββ- Tropomyosin”, Biopolymers, 31, 957-966 (1991). https://doi.org/10.1002/bip.360310805

27. Holtzer, M.E. and Holtzer, A., “Uncooperative Block in the Tropomyosin Coiled Coil”, J. Amer. Chem. Soc., 113, 7444-7445 (1991). https://doi.org/10.1021/ja00019a064

28. Mo, J., Holtzer, M.E. and Holtzer, A., “Kinetics of Folding and Unfolding of αα-Tropomyosin and of Nonpolymerizable αα-Tropomyosin”, Biopolymers, 31, 1417-1427 (1991). https://doi.org/10.1002/bip.360311208

29. Holtzer, M.E., Kidd, S.G., Crimmins, D.L. and Holtzer, A., “ββ Homodimers Exist in Rabbit Skeletal Muscle Tropomyosin and Increase after Denaturation-Renaturation”, Protein Science, 1, 335-341 (1992). https://onlinelibrary.wiley.com/doi/epdf/10.1002/pro.5560010305

30. Mo, J., Holtzer, M.E. and Holtzer, A., “Kinetics of Folding of αα-Tropomyosin Subsequences”, Biopolymers, 32, 751-756 (1992). https://doi.org/10.1002/bip.360320704

31. Mo, J., Holtzer, M.E. and Holtzer, A., “Kinetics of Folding and Unfolding of ββ-Tropomyosin”, Biopolymers, 32, 1581-1587 (1992). https://doi.org/10.1002/bip.360321115

32. Holtzer, M.E. and Holtzer, A., “α-Helix to Random Coil Transitions: Interpretation of the CD in the Region of Linear Temperature Dependence”, Biopolymers, 32, 1589-1591 (1992). https://doi.org/10.1002/bip.360321116

33. Holtzer, M.E. and Holtzer, A., “α-Helix to Random Coil Transitions: Determination of Peptide Concentration from the CD at the Isodichroic Point”, Biopolymers, 32, 1675-1677 (1992). https://doi.org/10.1002/bip.360321209

34. Mo, J., Holtzer, M.E. and Holtzer, A., “Rapid, spontaneous reassembly of homo- and heterodimeric tropomyosin two-chain coiled coils from unfolded α and β chains”, Protein Science, 2 128-130 (1993). https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2142300/pdf/8443587.pdf

35. Mo, J., Holtzer, M.E. and Holtzer, A., “Further Characterization of the Kinetic Intermediate of αα-Tropomyosin and of Its 142-281 Subsequence”, Biopolymers, 33, 823-825 (1993). https://doi.org/10.1002/bip.360330510

36. Wrabl, J., Holtzer, M.E. and Holtzer, A., “Thermal Unfolding Equilibria in Homodimeric Chicken Gizzard Tropomysoin Coiled Coils”, Biopolymers, 34, 1659-1667 (1994). https://doi.org/10.1002/bip.360341210

37. Holtzer, M.E., Crimmins, D.L. and Holtzer, A., “Structural Stability of Short Subsequences of the Tropomyosin Chain”, Biopolymers, 35, 125-136 (1995). https://doi.org/10.1002/bip.360350113

38. Holtzer, M.E., Downing, L.J. and Holtzer, A., “Some Properties of Acid Reassembled Tropomyosin” Biopolymers, 35, 239-244 (1995). https://doi.org/10.1002/bip.360350212

39. Muroga, Y., Muraki, M., Noda, I., Tagawa, H., Holtzer, A. and Holtzer, M.E., “Chain Unfolding Equilibria of α-Tropomyosin Coiled Coils Studied by Small Angle X-Ray Scattering”, J. Am. Chem. Soc., 117, 5622-5626 (1995).https://doi.org/10.1021/ja00126a002

40. Holtzer, M.E. and Holtzer, A., “The Use of Spectral Decomposition via the Convex Constraint Algorithm in Interpreting the CD-observed Unfolding Transitions of Coiled Coils”, Biopolymers, 36, 365-379 (1995). https://doi.org/10.1002/bip.360360310

41. Lovett, E., d'Avignon, D.A., Holtzer, M.E., Braswell, E.H., Zhu, D. and Holtzer, A., “Observation via One-Dimensional 13Cα NMR of Local Conformational Substates in Thermal Folding/Unfolding Equilibria of a Two-stranded GCN4 Leucine Zipper Analog”, Proc. Natl. Acad. Sci. USA, 93,1781-1785 (1996). https://www.ncbi.nlm.nih.gov/pmc/articles/PMC39858/pdf/pnas01509-0056.pdf

42. O'Brien, R., Sturtevant, J.M., Wrabl, J., Holtzer, M.E. and Holtzer, A., “A Scanning Calorimetric Study of Unfolding Equilibria in Homodimeric Chicken Gizzard Tropomyosins”, Biophys. J., 70, 2403-2407 (1996). https://www.ncbi.nlm.nih.gov/pmc/articles/PMC1225217/pdf/biophysj00047-0365.pdf

43. Holtzer, M.E., Adams, K., Lovett, E.G. and Holtzer, A., “Tyrosines in Two-Stranded Coiled Coils are CD Active Near 280 nm Even in the Absence of Interhelix Tyrosine-Tyrosine Interactions”, Biopolymers, 38(5), 669-671 (1996).

44. Holtzer, M.E., Lovett, E.G., d'Avignon, D.A., and Holtzer, A., “Thernal Unfolding in a GCN4-like Leucine Zipper. 13Cα NMR Chemical Shifts and Local Unfolding Curves”, Biophys. J., 73, 1031-1041 (1997). https://www.ncbi.nlm.nih.gov/pmc/articles/PMC1181000/pdf/biophysj00033-0483.pdf

45. d'Avignon, D.A., Bretthorst, G.L., Holtzer, M.E., and Holtzer, A., “Site-Specific Thermodynamics and Kinetics of a Coiled-Coil Transition by Spin Inversion Transfer NMR”, Biophys. J., 74, 3190-3197 (1998). Site-Specific Thermodynamics and Kinetics of a Coiled-Coil Transition by Spin Inversion Transfer NMR (cell.com)

46. d'Avignon, D.A., Bretthorst, G.L., Holtzer, M.E., and Holtzer, A., “Thermodynamics and Kinetics of a Folded-Folded' Transition at Valine-9 of a GCN4-like Leucine Zipper”, Biophys. J., 76, 2752-2759 (1999). https://www.ncbi.nlm.nih.gov/pmc/articles/PMC1300245/pdf/10233090.pdf

47. Holtzer, M.E., Braswell, E., Angeletti, R.H., Mints, L., Zhu, D. and Holtzer, A., “Ultracentrifugation and Circular Dichroism Studies of Folding Equilibria in a Retro GCN4-like Leucine Zipper”, Biophys. J., 78, 2037-2048 (2000). bj040002037p (nih.gov)

48. Holtzer, M.E., Bretthorst, G.L., d’Avignon, D.A., Angeletti, R.H., Mints, L., and Holtzer, A., “Temperature Dependence of the Folding and Unfolding Kinetics of the GCN4 Leucine Zipper via 13Cα-NMR”, Biophys. J., 80, 939-951 (2001). Temperature Dependence of the Folding and Unfolding Kinetics of the GCN4 Leucine Zipper via 13Ca-NMR (cell.com)

49. Holtzer, M.E., Mints, L., Angeletti, R.H., d’Avignon, D.A., and Holtzer, A., “CD and 13Cα-NMR Studies of Folding Equilibria in a Two-Stranded Coiled Coil Formed by Residues 190-254 of α-Tropomyosin”, Biopolymers, 59, 257-265 (2001). https://doi.org/10.1002/1097-0282(20011005)59:4%3C257::AID-BIP1022%3E3.0.CO;2-7

50. d’Avignon, D.A., Bretthorst, G.L., Holtzer, M.E., Schwarz, K.A., Angeletti, R.H., Mints, L., and Holtzer, A. “Site-specific Experiments on Folding/Unfolding of Jun Coiled Coils: Thermodynamic and Kinetic Parameters from Spin Inversion Transfer NMR at Leucine-19”, Biopolymers, 83, 255-267 (2006). Site-specific experiments on folding/unfolding of Jun coiled coils: Thermodynamic and kinetic parameters from spin inversion transfer nuclear magnetic resonance at leucine-18 (wustl.edu)

 ABSTRACTS AND POSTERS:

1.  Holtzer, M.E., Kumar, S. and Holtzer, A., “The Circular Dichroism of Two-Chain Coiled Coils in the Tyrosine/Disulfide Region”, Biophys. J., 53, 96a (1988).

2.  Kumar, S., Holtzer, M.E. and Holtzer, A., “Helix-Coil Transition in Two-Chain, Coiled Coils. A Backbone CD Study of Equilibrium Thermal Unfolding of Isolated Segments of the Tropomyosin Molecule”, Biophys. J., 53, 97a (1988).

3.  Holtzer, M.E., Bracken, W.C. and Holtzer, A., “Experiments of the Thermal Denaturation of ββ Tropomyosin Crosslinked Selectively at C36”, Biophys. J., 55, 356a (1989).

4.  Holtzer, A. and Holtzer, M.E., “Folding and Association of Tropomyosin Peptides”, J. Cell Biochem., Supp. 14A, 3 (1990).

5.  Mo, J., Holtzer, M.E. and Holtzer, A., “The Ionic Strength Dependence of Coiled-Coil Unfolding Equilibria”, Biophys. J., 57, 443a (1990).

6.  Ozeki, S., Holtzer, M.E. and Holtzer, A., “Kinetics of Heterodimer Formation in Tropomyosin Coiled-Coils”, Biophys. J., 57, 443a (1990).

7.  Crimmins, D.L. and Holtzer, M.E., “C4-HPLC and SEC-HPLC Analysis of Various SS Crosslinked Tropomyosin Dimers”, Fourth Symposium of The Protein Society, Abstract T146, San Diego, CA, Aug. 1990.

8.  Mo, J., Holtzer, M.E. and Holtzer, A., “Random Coils to Coiled Coils: The Folding Kinetics of Nonpolymerizable Tropomyosin”, Biophys. J., 59, 482a (1991).

9.  Mo, J., Holtzer, M.E. and Holtzer, A., “Random Coils to Coiled Coils: The Folding Kinetics of αα-Tropomyosin Sub-Sequences”, Biophys. J., 59, 482a (1991).

10. Kato, T., Ozeki, S., Holtzer, M.E. and Holtzer, A., “Kinetics of Heterodimer Formation in Tropomyosin Coiled Coils”, Biophys. J., 59, 482a (1991).

11. Holtzer, M.E., Crimmins, D.L., Kidd, S.G. and Holtzer, A., “ββ Homodimers Exist in Native Rabbit Skeletal Tropomyosin”, Fifth Symposium of The Protein Society”, Abstract T117, Baltimore, MD, June 1991.

12. Holtzer, M.E. and Holtzer, A., “Intrinsic Local Stability in Tropomyosin Subsequence 253-280”, Sixth Symposium of The Protein Society”, Abstract S53, San Diego, CA, July 1992.

13. Holtzer, M.E., Downing, L.J. and Holtzer, A., “Do Tropomyosin Coiled Coils Reassemble Anti-Parallel at Low pH”, Sixth Symposium of The Protein Society”, Abstract S54, San Diego, CA, July 1992.

14. Holtzer, M.E. and Holtzer, A., “Structural Stability of Short Subsequences of the Tropomyosin Chain”, Biophys. J., 61, A175 (1993).

15. Lovett, E.G., d'Avignon, D.A., Holtzer, M.E. and Holtzer, A., “Local Probes of Coiled-Coil Structure: Tyrosine CD and Natural Abundance 13C-NMR of a GCN4-like Peptide”, Abstract 55M, San Diego, CA, July 1994.

16.  d'Avignon, D.A., Bretthorst, G. L., Lovett, E.G., Holtzer, M.E. and Holtzer, A., “13C-NMR Elucidation of the Population of Local Conformational Substates in Coiled-Coil Peptides and the Dynamics of Interconversion”, 37th Experimental Nuclear Magnetic Resonance Conference, Pacific Groves, CA, March 1996.