Donna L. Luisi, Ph.D.
Affiliations: | 2000 | Stony Brook University, Stony Brook, NY, United States |
Google:
"Donna Luisi"Mean distance: 10.58
Parents
Sign in to add mentorDaniel P. Raleigh | grad student | 2000 | SUNY Stony Brook | |
(Characterization of the transition and the unfolded states of the N-terminal domain of the ribosomal protein L9.) |
BETA: Related publications
See more...
Publications
You can help our author matching system! If you notice any publications incorrectly attributed to this author, please sign in and mark matches as correct or incorrect. |
Luisi DL, Snow CD, Lin JJ, et al. (2003) Surface salt bridges, double-mutant cycles, and protein stability: An experimental and computational analysis of the interaction of the Asp 23 side chain with the N-terminus of the N-terminal domain of the ribosomal protein L9 Biochemistry. 42: 7050-7060 |
Luisi DL, Raleigh DP. (2000) pH-dependent interactions and the stability and folding kinetics of the N-terminal domain of L9. Electrostatic interactions are only weakly formed in the transition state for folding. Journal of Molecular Biology. 299: 1091-100 |
Sato S, Luisi DL, Raleigh DP. (2000) pH jump studies of the folding of the multidomain ribosomal protein L9: the structural organization of the N-terminal domain does not affect the anomalously slow folding of the C-terminal domain. Biochemistry. 39: 4955-62 |
Luisi DL, Kuhlman B, Sideras K, et al. (1999) Effects of varying the local propensity to form secondary structure on the stability and folding kinetics of a rapid folding mixed alpha/beta protein: characterization of a truncation mutant of the N-terminal domain of the ribosomal protein L9. Journal of Molecular Biology. 289: 167-74 |
Kuhlman B, Luisi DL, Young P, et al. (1999) pKa values and the pH dependent stability of the N-terminal domain of L9 as probes of electrostatic interactions in the denatured state. Differentiation between local and nonlocal interactions. Biochemistry. 38: 4896-903 |
Luisi DL, Wu WJ, Raleigh DP. (1999) Conformational analysis of a set of peptides corresponding to the entire primary sequence of the N-terminal domain of the ribosomal protein L9: evidence for stable native-like secondary structure in the unfolded state. Journal of Molecular Biology. 287: 395-407 |
Kuhlman B, Luisi DL, Evans PA, et al. (1998) Global analysis of the effects of temperature and denaturant on the folding and unfolding kinetics of the N-terminal domain of the protein L9. Journal of Molecular Biology. 284: 1661-70 |