Three-state analysis of sperm whale apomyoglobin folding D Barrick, RL Baldwin Biochemistry 32 (14), 3790-3796, 1993 | 297 | 1993 |
The association rate constant for heme binding to globin is independent of protein structure MS Hargrove, D Barrick, JS Olson Biochemistry 35 (35), 11293-11299, 1996 | 275 | 1996 |
Limits of cooperativity in a structurally modular protein: response of the Notch ankyrin domain to analogous alanine substitutions in each repeat CM Bradley, D Barrick Journal of molecular biology 324 (2), 373-386, 2002 | 246 | 2002 |
The molten globule intermediate of apomyoglobin and the process of protein folding D Barrick, RL Baldwin Protein Science 2 (6), 869-876, 1993 | 239 | 1993 |
Replacement of the Proximal Ligand of Sperm Whale Myoglobin with Free Imidazole in the Mutant His-93. fwdarw. Gly D Barrick Biochemistry 33 (21), 6546-6554, 1994 | 234 | 1994 |
Probing the stability of a partly folded apomyoglobin intermediate by site-directed mutagenesis FM Hughson, D Barrick, RL Baldwin Biochemistry 30 (17), 4113-4118, 1991 | 220 | 1991 |
Urea unfolding of peptide helices as a model for interpreting protein unfolding JM Scholtz, D Barrick, EJ York, JM Stewart, RL Baldwin Proceedings of the National Academy of Sciences 92 (1), 185-189, 1995 | 210 | 1995 |
An experimentally determined protein folding energy landscape CC Mello, D Barrick Proceedings of the National Academy of Sciences 101 (39), 14102-14107, 2004 | 180 | 2004 |
Molecular mechanisms of acid denaturation: The role of histidine residues in the partial unfolding of apomyoglobin D Barrick, FM Hughson, RL Baldwin Journal of molecular biology 237 (5), 588-601, 1994 | 173 | 1994 |
The folding of single domain proteins—have we reached a consensus? TR Sosnick, D Barrick Current opinion in structural biology 21 (1), 12-24, 2011 | 170 | 2011 |
Measuring the stability of partly folded proteins using TMAO CC Mello, D Barrick Protein Science 12 (7), 1522-1529, 2003 | 166 | 2003 |
Structure and stability of the ankyrin domain of the Drosophila Notch receptor ME Zweifel, DJ Leahy, FM Hughson, D Barrick Protein Science 12 (11), 2622-2632, 2003 | 130 | 2003 |
Size and sequence and the volume change of protein folding JB Rouget, T Aksel, J Roche, JL Saldana, AE Garcia, D Barrick, CA Royer Journal of the American Chemical Society 133 (15), 6020-6027, 2011 | 126 | 2011 |
Studies of the Ankyrin Repeats of the Drosophila melanogaster Notch Receptor. 2. Solution Stability and Cooperativity of Unfolding ME Zweifel, D Barrick Biochemistry 40 (48), 14357-14367, 2001 | 122 | 2001 |
Consensus sequence design as a general strategy to create hyperstable, biologically active proteins M Sternke, KW Tripp, D Barrick Proceedings of the National Academy of Sciences 116 (23), 11275-11284, 2019 | 121 | 2019 |
Functional cavities in proteins: a general method for proximal ligand substitution in myoglobin GD DePillis, SM Decatur, D Barrick, SG Boxer Journal of the American Chemical Society 116 (15), 6981-6982, 1994 | 120 | 1994 |
Quantitative dissection of the Notch: CSL interaction: insights into the Notch-mediated transcriptional switch OY Lubman, MXG Ilagan, R Kopan, D Barrick Journal of molecular biology 365 (3), 577-589, 2007 | 119 | 2007 |
Repeat-protein folding: new insights into origins of cooperativity, stability, and topology E Kloss, N Courtemanche, D Barrick Archives of biochemistry and biophysics 469 (1), 83-99, 2008 | 112 | 2008 |
Control of transcriptional activity by design of charge patterning in the intrinsically disordered RAM region of the Notch receptor KP Sherry, RK Das, RV Pappu, D Barrick Proceedings of the National Academy of Sciences 114 (44), E9243-E9252, 2017 | 108 | 2017 |
Folding landscapes of ankyrin repeat proteins: experiments meet theory D Barrick, DU Ferreiro, EA Komives Current opinion in structural biology 18 (1), 27-34, 2008 | 108 | 2008 |