Journal Publications:

      

1. M. S. Cheung, I. Daizadeh, A. A. Stuchebrukhov, P. F. Heelis. “Pathways of Electron Transfer in E. coli DNA Photolyase”, Biophys. J., 76, 1241-1249 (1999)

The prediction was later experimentally verified (Aubert et al, Nature, 405, 586-590, 2000).

 

         2. M. S. Cheung, A. E. García, J. N. Onuchic. “Protein folding mediated by solvation: water expelling and formation of the hydrophobic core occurs after the structure collapse” Proc. Natl. Acad. Sci. U. S. A., 99, 685-690 (2002).

           This paper has 136 citations since being published.
 

3. C. Guo, M. S. Cheung, H. Levine, D. A. Kessler. “Mechanisms underlying sequence-independent beta-sheet formation” J. Chem. Phys. 116, 4353-4365 (2002).

         4. M. S. Cheung, J. M. Finke, B. Callahan, J. N. Onuchic. “Exploring the interplay of topology and secondary structural formation in the protein folding problem” J. Phys. Chem., B, 107, 11193-11200 (2003).

          

         5. M. S. Cheung, L. L. Chavez, J. N. Onuchic. “The Energy Landscape for Protein Folding and Possible Connections to Function” Polymer, 45, 547-555 (2004).

6. A. Fernandez-Escamilla, M. S. Cheung, M. C. Vega, M. Wilmanns, J. N. Onuchic, L. Serrano. “Solvation in protein folding analysis, combination of theoretical and experimental approaches” Proc. Natl. Acad. Sci. U. S. A.,  101, 2834-2839 (2004).

7.  J. M. Finke, M. S. Cheung, J. N. Onuchic. “A structural model of polyglutamine determined from a host-guest method combining experiments and landscape theory” Biophys. J. 87, 1900-1918 (2004).

8. S. Yang, S. S. Cho, Y. Levy, M. S. Cheung, H. Levine, P. G. Wolynes, J. N. Onuchic. “Domain swapping is a consequence of minimal frustration”. Proc. Natl. Acad. Sci. U. S. A., 101, 13786-13791 (2004).

9. M. S. Cheung, D. Klimov, D. Thirumalai. “Molecular crowding enhances native state stability and refolding rates”. Proc. Natl. Acad. Sci. U. S. A., 102, 4753-4758 (2005).            This paper was highlighted by Journal of Cell Biology in the April 11th, 2005 issue.

10. J. Chahine, M. S. Cheung. “Computational studies of the reversible domain swapping of p13suc1”, Biophys. J. 89, 1-9 (2005).

 

11. M. S. Cheung, D. Thirumalai. “Nanopore-protein interactions dramatically alter stability and yield of the native state in restricted spaces”, J. Mol. Biol. 357, 632-643 (2006).

 

 

12. M. E. Sardiu, M. S. Cheung, Y.-K. Yu. “Cysteine-Cysteine contact preference from disulfide reduction leads to target-focusing in protein folding”, Biophys. J. 93 1-14 (2007).

 

13. M. S. Cheung, D. Thirumalai. “Crowding and confinement effects on structures of the transition state ensemble in proteins”,J. Phys. Chem. B.111 8250-8257 (2007).

 

14. S.-Q.Zhang, M. S. Cheung. “Manipulating Biopolymer Dynamics by Anisotropic Nanoconfinement”, Nano Letters, 7, 3438-3442 (2007). This paper was in Research Highlights, Nature Nanotechnology on-line Oct 26th 2007 release.     

 

15. L. Stagg, S.-Q.Zhang, M. S. Cheung, P. Wittung-Stafshede. “Molecular crowding enhances native structure and stability of α/β protein flavodoxin”, Proc. Natl. Acad. Sci. U. S. A., 104, 18976-18981 (2007). This paper was featured in Nov 14th 07, Rice News

 

16. D. Homouz, M. Perham, A. Samiotakis, M. S. Cheung, and P. Wittung-Stafshede. “Crowded, cell-like environment induces shape changes in aspherical protein”, Proc. Natl. Acad. Sci. U. S. A.,105, 11754-11759 (2008). It is featured in the "News of the week" in Chemical & Engineering News (p14 Aug 18 2008) and in Research Highlights in Nature (vol 454, p21, 2008).

 

17. A. Kudlay, M. S. Cheung, and D. Thirumalai. “Crowding effects on the structural transitions in a flexible helical homopolymer”, submitted. (2008).

 

18. D. Homouz, L. Stagg, P. Wittung-Stafshede, and M. S. Cheung, “Macromolecular crowding modulates folding mechanism of α/β protein apoflavodoxin”, submitted (2008).