Donna L. Luisi, Ph.D. - Publications
Affiliations: | 2000 | Stony Brook University, Stony Brook, NY, United States |
Year | Citation | Score | |||
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2003 | Luisi DL, Snow CD, Lin JJ, Hendsch ZS, Tidor B, Raleigh DP. 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. PMID 12795600 DOI: 10.1021/Bi027202N | 0.57 | |||
2000 | Luisi DL, Raleigh DP. 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. PMID 10843860 DOI: 10.1006/Jmbi.2000.3752 | 0.567 | |||
2000 | Sato S, Luisi DL, Raleigh DP. 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. PMID 10769155 DOI: 10.1021/Bi992608U | 0.605 | |||
1999 | Luisi DL, Kuhlman B, Sideras K, Evans PA, Raleigh DP. 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. PMID 10339414 DOI: 10.1006/Jmbi.1999.2742 | 0.641 | |||
1999 | Kuhlman B, Luisi DL, Young P, Raleigh DP. 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. PMID 10200179 DOI: 10.1021/Bi982931H | 0.612 | |||
1999 | Luisi DL, Wu WJ, Raleigh DP. 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. PMID 10080901 DOI: 10.1006/Jmbi.1999.2595 | 0.578 | |||
1998 | Kuhlman B, Luisi DL, Evans PA, Raleigh DP. 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. PMID 9878377 DOI: 10.1006/Jmbi.1998.2246 | 0.592 | |||
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