Binding sites in Escherichia coli dihydrofolate reductase communicate by modulating the conformational ensemble.
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[1] N. Metropolis,et al. Equation of State Calculations by Fast Computing Machines , 1953, Resonance.
[2] J. Wyman,et al. LINKED FUNCTIONS AND RECIPROCAL EFFECTS IN HEMOGLOBIN: A SECOND LOOK. , 1964, Advances in protein chemistry.
[3] J. Bolin,et al. Crystal structures of Escherichia coli and Lactobacillus casei dihydrofolate reductase refined at 1.7 A resolution. I. General features and binding of methotrexate. , 1982, The Journal of biological chemistry.
[4] R. L. Baldwin,et al. Temperature dependence of the hydrophobic interaction in protein folding. , 1986, Proceedings of the National Academy of Sciences of the United States of America.
[5] S. Benkovic,et al. Construction and evaluation of the kinetic scheme associated with dihydrofolate reductase from Escherichia coli. , 1987, Biochemistry.
[6] S. Benkovic,et al. Probing the functional role of threonine-113 of Escherichia coli dihydrofolate reductase for its effect on turnover efficiency, catalysis, and binding. , 1989, Biochemistry.
[7] J. Wyman,et al. Binding and Linkage: Functional Chemistry of Biological Macromolecules , 1990 .
[8] S J Oatley,et al. Crystal structures of Escherichia coli dihydrofolate reductase: the NADP+ holoenzyme and the folate.NADP+ ternary complex. Substrate binding and a model for the transition state. , 1990, Biochemistry.
[9] J. Kraut,et al. Investigation of the functional role of tryptophan-22 in Escherichia coli dihydrofolate reductase by site-directed mutagenesis. , 1994, Biochemistry.
[10] K. P. Murphy,et al. Thermodynamics of structural stability and cooperative folding behavior in proteins. , 1992, Advances in protein chemistry.
[11] A. Palmer,et al. Effects of ion binding on the backbone dynamics of calbindin D9k determined by 15N NMR relaxation. , 1993, Biochemistry.
[12] D. Xie,et al. Structure based prediction of protein folding intermediates. , 1994, Journal of molecular biology.
[13] P E Wright,et al. Dynamics of a flexible loop in dihydrofolate reductase from Escherichia coli and its implication for catalysis. , 1994, Biochemistry.
[14] L M Amzel,et al. Estimation of changes in side chain configurational entropy in binding and folding: General methods and application to helix formation , 1994, Proteins.
[15] V. Hilser,et al. The heat capacity of proteins , 1995, Proteins.
[16] P. Wright,et al. Dynamics of the dihydrofolate reductase-folate complex: catalytic sites and regions known to undergo conformational change exhibit diverse dynamical features. , 1995, Biochemistry.
[17] K. P. Murphy,et al. Energetics of hydrogen bonding in proteins: A model compound study , 1996, Protein science : a publication of the Protein Society.
[18] E. Cera,et al. Thermodynamic Theory of Site-Specific Binding Processes in Biological Macromolecules , 1996 .
[19] Effects of point mutations at the flexible loop glycine-67 of Escherichia coli dihydrofolate reductase on its stability and function. , 1996, Journal of biochemistry.
[20] V. Hilser,et al. The magnitude of the backbone conformational entropy change in protein folding , 1996, Proteins.
[21] S. Fesik,et al. Backbone dynamics of the C-terminal domain of Escherichia coli topoisomerase I in the absence and presence of single-stranded DNA. , 1996, Biochemistry.
[22] V. Hilser,et al. Structure-based calculation of the equilibrium folding pathway of proteins. Correlation with hydrogen exchange protection factors. , 1996, Journal of molecular biology.
[23] M. Billeter,et al. MOLMOL: a program for display and analysis of macromolecular structures. , 1996, Journal of molecular graphics.
[24] B Honig,et al. On the calculation of binding free energies using continuum methods: Application to MHC class I protein‐peptide interactions , 1997, Protein science : a publication of the Protein Society.
[25] E. Olejniczak,et al. Changes in the NMR-derived motional parameters of the insulin receptor substrate 1 phosphotyrosine binding domain upon binding to an interleukin 4 receptor phosphopeptide. , 1997, Biochemistry.
[26] V. Hilser,et al. Predicting the equilibrium protein folding pathway: Structure‐based analysis of staphylococcal nuclease , 1997, Proteins.
[27] V. Hilser,et al. Structure-based statistical thermodynamic analysis of T4 lysozyme mutants: structural mapping of cooperative interactions. , 1997, Biophysical chemistry.
[28] J. Kraut,et al. Loop and subdomain movements in the mechanism of Escherichia coli dihydrofolate reductase: crystallographic evidence. , 1997, Biochemistry.
[29] G. K. Ackers,et al. Deciphering the molecular code of hemoglobin allostery. , 1998, Advances in protein chemistry.
[30] T. Oas,et al. The structural distribution of cooperative interactions in proteins: analysis of the native state ensemble. , 1998, Proceedings of the National Academy of Sciences of the United States of America.
[31] E. Cera. Site-specific analysis of mutational effects in proteins. , 1998 .
[32] E. Freire,et al. The propagation of binding interactions to remote sites in proteins: analysis of the binding of the monoclonal antibody D1.3 to lysozyme. , 1999, Proceedings of the National Academy of Sciences of the United States of America.
[33] Milos V. Novotny,et al. Increased protein backbone conformational entropy upon hydrophobic ligand binding , 1999, Nature Structural Biology.