Optimized representations and maximal information in proteins AD Solis, S Rackovsky Proteins: Structure, Function, and Bioinformatics 38 (2), 149-164, 2000 | 91 | 2000 |
“Hidden” sequence periodicities and protein architecture S Rackovsky Proceedings of the National Academy of Sciences 95 (15), 8580-8584, 1998 | 83 | 1998 |
Correlation of the structure of the transmembrane domain of the neu oncogene-encoded p185 protein with its function. PW Brandt-Rauf, S Rackovsky, MR Pincus Proceedings of the National Academy of Sciences 87 (21), 8660-8664, 1990 | 80 | 1990 |
Hydrophobicity, hydrophilicity, and the radial and orientational distributions of residues in native proteins. S Rackovsky, HA Scheraga Proceedings of the National Academy of Sciences 74 (12), 5248-5251, 1977 | 76 | 1977 |
Lessons from application of the UNRES force field to predictions of structures of CASP10 targets Y He, MA Mozolewska, P Krupa, AK Sieradzan, TK Wirecki, A Liwo, ... Proceedings of the National Academy of Sciences 110 (37), 14936-14941, 2013 | 69 | 2013 |
Quantitative organization of the known protein x‐ray structures. I. Methods and short‐length‐scale results S Rackovsky Proteins: Structure, Function, and Bioinformatics 7 (4), 378-402, 1990 | 68 | 1990 |
Class‐specific correlations between protein folding rate, structure‐derived, and sequence‐derived descriptors IB Kuznetsov, S Rackovsky Proteins: Structure, Function, and Bioinformatics 54 (2), 333-341, 2004 | 55 | 2004 |
On the properties and sequence context of structurally ambivalent fragments in proteins IB Kuznetsov, S Rackovsky Protein science 12 (11), 2420-2433, 2003 | 52 | 2003 |
On the nature of the protein folding code. S Rackovsky Proceedings of the National Academy of Sciences 90 (2), 644-648, 1993 | 52 | 1993 |
Sequence physical properties encode the global organization of protein structure space S Rackovsky Proceedings of the National Academy of Sciences 106 (34), 14345-14348, 2009 | 47 | 2009 |
Substitutions of proline 76 in yeast iso-1-cytochrome c. Analysis of residues compatible and incompatible with folding requirements. JF Ernst, DM Hampsey, JW Stewart, S Rackovsky, D Goldstein, ... Journal of Biological Chemistry 260 (24), 13225-13236, 1985 | 40 | 1985 |
Improvement of the treatment of loop structures in the UNRES force field by inclusion of coupling between backbone-and side-chain-local conformational states P Krupa, AK Sieradzan, S Rackovsky, M Baranowski, S Ołdziej, ... Journal of chemical theory and computation 9 (10), 4620-4632, 2013 | 38 | 2013 |
Comparative computational analysis of prion proteins reveals two fragments with unusual structural properties and a pattern of increase in hydrophobicity associated with … IB Kuznetsov, S Rackovsky Protein science 13 (12), 3230-3244, 2004 | 38 | 2004 |
Optimally informative backbone structural propensities in proteins AD Solis, S Rackovsky Proteins: Structure, Function, and Bioinformatics 48 (3), 463-486, 2002 | 36 | 2002 |
Improvement of statistical potentials and threading score functions using information maximization AD Solis, S Rackovsky Proteins: Structure, Function, and Bioinformatics 62 (4), 892-908, 2006 | 33 | 2006 |
On the redox conformational change in cytochrome c. S Rackovsky, DA Goldstein Proceedings of the National Academy of Sciences 81 (18), 5901-5905, 1984 | 32 | 1984 |
Global characteristics of protein sequences and their implications S Rackovsky Proceedings of the National Academy of Sciences 107 (19), 8623-8626, 2010 | 30 | 2010 |
Protein comparison and classification: a differential geometric approach. S Rackovsky, DA Goldstein Proceedings of the National Academy of Sciences 85 (3), 777-781, 1988 | 26 | 1988 |
Sequence-, structure-, and dynamics-based comparisons of structurally homologous CheY-like proteins Y He, GG Maisuradze, Y Yin, K Kachlishvili, S Rackovsky, HA Scheraga Proceedings of the National Academy of Sciences 114 (7), 1578-1583, 2017 | 22 | 2017 |
Protein sequence randomness and sequence/structure correlations RS Rahman, S Rackovsky Biophysical Journal 68 (4), 1531-1539, 1995 | 20 | 1995 |