Zheng-yu Peng
Affiliations: | University of Connecticut, Storrs, CT, United States |
Area:
BiochemistryGoogle:
"Zheng-yu Peng"Mean distance: (not calculated yet)
Children
Sign in to add trainee| Leila K. Mosavi | grad student | 2004 | University of Connecticut |
| Tobin J. Cammett | grad student | 2005 | University of Connecticut |
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Publications
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| Desrosiers DC, Peng ZY. (2005) A binding free energy hot spot in the ankyrin repeat protein GABPbeta mediated protein-protein interaction. Journal of Molecular Biology. 354: 375-84 |
| Mosavi LK, Cammett TJ, Desrosiers DC, et al. (2004) The ankyrin repeat as molecular architecture for protein recognition. Protein Science : a Publication of the Protein Society. 13: 1435-48 |
| Mosavi LK, Peng ZY. (2003) Structure-based substitutions for increased solubility of a designed protein. Protein Engineering. 16: 739-45 |
| Cammett TJ, Luo L, Peng ZY. (2003) Design and characterization of a hyperstable p16INK4a that restores Cdk4 binding activity when combined with oncogenic mutations. Journal of Molecular Biology. 327: 285-97 |
| Mosavi LK, Minor DL, Peng ZY. (2002) Consensus-derived structural determinants of the ankyrin repeat motif. Proceedings of the National Academy of Sciences of the United States of America. 99: 16029-34 |
| Bai P, Peng ZY. (2001) Cooperative folding of the isolated α-helical domain of hen egg-white lysozyme Journal of Molecular Biology. 314: 321-329 |
| Chakraborty S, Ittah V, Bai P, et al. (2001) Structure and dynamics of the α-lactalbumin molten globule: Fluorescence studies using proteins containing a single tryptophan residue Biochemistry. 40: 7228-7238 |
| Bai P, Song J, Luo L, et al. (2001) A model of dynamic side-chain--side-chain interactions in the alpha-lactalbumin molten globule. Protein Science. 10: 55-62 |
| Chakraborty S, Peng Z. (2000) Hierarchical unfolding of the alpha-lactalbumin molten globule: presence of a compact intermediate without a unique tertiary fold. Journal of Molecular Biology. 298: 1-6 |
| Bai P, Luo L, Peng Z. (2000) Side chain accessibility and dynamics in the molten globule state of alpha-lactalbumin: a (19)F-NMR study. Biochemistry. 39: 372-380 |