Electrostatic interactions in a peptide--RNA complex.
暂无分享,去创建一个
[1] T. Xia,et al. Designed arginine-rich RNA-binding peptides with picomolar affinity. , 2002, Journal of the American Chemical Society.
[2] J. M. Scholtz,et al. Osmolyte effects on helix formation in peptides and the stability of coiled‐coils , 2002, Protein science : a publication of the Protein Society.
[3] R. L. Baldwin,et al. The enthalpy of the alanine peptide helix measured by isothermal titration calorimetry using metal-binding to induce helix formation , 2002, Proceedings of the National Academy of Sciences of the United States of America.
[4] D. Draper,et al. A thermodynamic framework for Mg2+ binding to RNA , 2001, Proceedings of the National Academy of Sciences of the United States of America.
[5] Y. Shamoo,et al. Structure-based analysis of protein-RNA interactions using the program ENTANGLE. , 2001, Journal of molecular biology.
[6] I. Baskakov,et al. The osmophobic effect: natural selection of a thermodynamic force in protein folding. , 2001, Journal of molecular biology.
[7] T. Steitz,et al. The complete atomic structure of the large ribosomal subunit at 2.4 A resolution. , 2000, Science.
[8] D. Draper,et al. Mg(2+) binding to tRNA revisited: the nonlinear Poisson-Boltzmann model. , 2000, Journal of molecular biology.
[9] D. Draper,et al. Contributions of basic residues to ribosomal protein L11 recognition of RNA. , 2000, Journal of molecular biology.
[10] Barry Honig,et al. Calculating the electrostatic properties of RNA provides new insights into molecular interactions and function , 1999, Nature Structural Biology.
[11] D. Draper. Themes in RNA-protein recognition. , 1999, Journal of molecular biology.
[12] T. Lohman,et al. The importance of coulombic end effects: experimental characterization of the effects of oligonucleotide flanking charges on the strength and salt dependence of oligocation (L8+) binding to single-stranded DNA oligomers. , 1999, Biophysical journal.
[13] An-Suei Yang,et al. Electrostatic contributions to the binding free energy of the lambdacI repressor to DNA. , 1998, Biophysical journal.
[14] D. Turner,et al. Thermodynamic parameters for an expanded nearest-neighbor model for formation of RNA duplexes with Watson-Crick base pairs. , 1998, Biochemistry.
[15] Jack Greenblatt,et al. NMR Structure of the Bacteriophage λ N Peptide/boxB RNA Complex: Recognition of a GNRA Fold by an Arginine-Rich Motif , 1998, Cell.
[16] I. Baskakov,et al. Forcing Thermodynamically Unfolded Proteins to Fold* , 1998, The Journal of Biological Chemistry.
[17] M. Weiss,et al. RNA recognition by a bent alpha-helix regulates transcriptional antitermination in phage lambda. , 1997, Biochemistry.
[18] H. Chen,et al. An RNA enhancer in a phage transcriptional antitermination complex functions as a structural switch. , 1997, Genes & development.
[19] R. L. Baldwin,et al. Mechanism of helix induction by trifluoroethanol: a framework for extrapolating the helix-forming properties of peptides from trifluoroethanol/water mixtures back to water. , 1997, Biochemistry.
[20] T. Lohman,et al. Thermodynamics of oligoarginines binding to RNA and DNA. , 1997, Biochemistry.
[21] P. V. von Hippel,et al. Complexes of N antitermination protein of phage lambda with specific and nonspecific RNA target sites on the nascent transcript. , 1997, Biochemistry.
[22] C. Kundrot,et al. Crystal Structure of a Group I Ribozyme Domain: Principles of RNA Packing , 1996, Science.
[23] T. Lohman,et al. Large electrostatic differences in the binding thermodynamics of a cationic peptide to oligomeric and polymeric DNA. , 1996, Proceedings of the National Academy of Sciences of the United States of America.
[24] D. Court,et al. Transcription antitermination: the λ paradigm updated , 1995 .
[25] B Honig,et al. Salt effects on polyelectrolyte–ligand binding: Comparison of Poisson–Boltzmann, and limiting law/counterion binding models , 1995, Biopolymers.
[26] Kim A. Sharp,et al. Polyelectrolyte electrostatics: Salt dependence, entropic, and enthalpic contributions to free energy in the nonlinear Poisson–Boltzmann model , 1995 .
[27] A. Frankel,et al. Structural variety of arginine-rich RNA-binding peptides. , 1995, Proceedings of the National Academy of Sciences of the United States of America.
[28] B. Honig,et al. Classical electrostatics in biology and chemistry. , 1995, Science.
[29] P. Moore,et al. The sarcin/ricin loop, a modular RNA. , 1995, Journal of molecular biology.
[30] J. Bond,et al. Grand canonical Monte Carlo molecular and thermodynamic predictions of ion effects on binding of an oligocation (L8+) to the center of DNA oligomers. , 1995, Biophysical journal.
[31] A. Frankel,et al. Costabilization of peptide and RNA structure in an HIV Rev peptide-RRE complex. , 1994, Biochemistry.
[32] K. Flaherty,et al. Model for an RNA tertiary interaction from the structure of an intermolecular complex between a GAAA tetraloop and an RNA helix , 1994, Nature.
[33] Barry Honig,et al. Salt Effects on Protein-DNA Interactions: The λcI Repressor and EcoRI Endonuclease , 1994 .
[34] B Honig,et al. Salt effects on ligand-DNA binding. Minor groove binding antibiotics. , 1994, Journal of molecular biology.
[35] R. L. Baldwin,et al. Effect of a single aspartate on helix stability at different positions in a neutral alanine‐based peptide , 1993, Protein science : a publication of the Protein Society.
[36] A. Frankel,et al. Electrostatic interactions modulate the RNA-binding and transactivation specificities of the human immunodeficiency virus and simian immunodeficiency virus Tat proteins. , 1993, Proceedings of the National Academy of Sciences of the United States of America.
[37] J A McCammon,et al. Poisson-Boltzmann analysis of the lambda repressor-operator interaction. , 1992, Biophysical journal.
[38] D. Turner,et al. Context dependence of hydrogen bond free energy revealed by substitutions in an RNA hairpin. , 1992, Science.
[39] I. Tinoco,et al. Thermodynamic parameters for loop formation in RNA and DNA hairpin tetraloops. , 1992, Nucleic acids research.
[40] R. L. Baldwin,et al. Parameters of helix–coil transition theory for alanine‐based peptides of varying chain lengths in water , 1991, Biopolymers.
[41] H. Heus,et al. Structural features that give rise to the unusual stability of RNA hairpins containing GNRA loops. , 1991, Science.
[42] Bhyravabhotla Jayaram,et al. A theoretical study of polyelectrolyte effects in protein-DNA interactions: Monte Carlo free energy simulations on the ion atmosphere contribution to the thermodynamics of .lambda. repressor-operator complex formation , 1991 .
[43] S. Sarkar,et al. IQ and Heredity , 1991, Science.
[44] R. L. Baldwin,et al. Calorimetric determination of the enthalpy change for the alpha-helix to coil transition of an alanine peptide in water. , 1991, Proceedings of the National Academy of Sciences of the United States of America.
[45] B. Honig,et al. A rapid finite difference algorithm, utilizing successive over‐relaxation to solve the Poisson–Boltzmann equation , 1991 .
[46] D. Hudson,et al. Analysis of arginine-rich peptides from the HIV Tat protein reveals unusual features of RNA-protein recognition. , 1991, Genes & development.
[47] T. Lohman,et al. Thermodynamic extent of counterion release upon binding oligolysines to single-stranded nucleic acids. , 1990, Proceedings of the National Academy of Sciences of the United States of America.
[48] M. Record,et al. Monte Carlo description of oligoelectrolyte properties of DNA oligomers: range of the end effect and the approach of molecular and thermodynamic properties to the polyelectrolyte limits. , 1989, Proceedings of the National Academy of Sciences of the United States of America.
[49] R. L. Baldwin,et al. Helix stabilization by Glu-...Lys+ salt bridges in short peptides of de novo design. , 1987, Proceedings of the National Academy of Sciences of the United States of America.
[50] U. Singh,et al. A NEW FORCE FIELD FOR MOLECULAR MECHANICAL SIMULATION OF NUCLEIC ACIDS AND PROTEINS , 1984 .
[51] D. Turner,et al. Base-stacking and base-pairing contributions to helix stability: thermodynamics of double-helix formation with CCGG, CCGGp, CCGGAp, ACCGGp, CCGGUp, and ACCGGUp. , 1983, Biochemistry.
[52] G. S. Manning. The molecular theory of polyelectrolyte solutions with applications to the electrostatic properties of polynucleotides , 1978, Quarterly Reviews of Biophysics.
[53] T. Lohman,et al. Thermodynamic analysis of ion effects on the binding and conformational equilibria of proteins and nucleic acids: the roles of ion association or release, screening, and ion effects on water activity , 1978, Quarterly Reviews of Biophysics.
[54] T. Lohman,et al. Ion effects on ligand-nucleic acid interactions. , 1976, Journal of molecular biology.
[55] P. V. Hippel,et al. Ion effects on the solution structure of biological macromolecules , 1969 .
[56] P. R. Bevington,et al. Data Reduction and Error Analysis for the Physical Sciences , 1969 .
[57] H. A. Sober,et al. Protein-nucleic acid interactions. II. Oligopeptide-polyribonucleotide binding studies. , 1967, Biochemistry.
[58] B. Zimm,et al. Theory of the Phase Transition between Helix and Random Coil in Polypeptide Chains , 1959 .
[59] William H. Press,et al. Numerical recipes in C , 2002 .
[60] M. Record,et al. Analysis of effects of salts and uncharged solutes on protein and nucleic acid equilibria and processes: a practical guide to recognizing and interpreting polyelectrolyte effects, Hofmeister effects, and osmotic effects of salts. , 1998, Advances in protein chemistry.
[61] M. Record,et al. Salt-nucleic acid interactions. , 1995, Annual review of physical chemistry.
[62] H. Scheraga,et al. Helix‐coil stability constants for the naturally occurring amino acids in water. XXIV. Half‐cystine parameters from random poly(hydroxybutylglutamine‐CO‐S‐methylthio‐L‐cysteine) , 1990 .
[63] T. Lohman,et al. Equilibrium binding of Escherichia coli single-strand binding protein to single-stranded nucleic acids in the (SSB)65 binding mode. Cation and anion effects and polynucleotide specificity. , 1988, Biochemistry.
[64] D. Turner,et al. RNA structure prediction. , 1988, Annual review of biophysics and biophysical chemistry.