Observation of Solvent Penetration during Cold Denaturation of E. coli Phosphofructokinase-2
Tài liệu tham khảo
Matthews, 1993, Pathways of protein folding, Annu. Rev. Biochem., 62, 653, 10.1146/annurev.bi.62.070193.003253
Privalov, 1990, Cold denaturation of proteins, Crit. Rev. Biochem. Mol. Biol., 25, 281, 10.3109/10409239009090612
Privalov, 1986, Cold denaturation of myoglobin, J. Mol. Biol., 190, 487, 10.1016/0022-2836(86)90017-3
Privalov, 1988, Stability of protein structure and hydrophobic interaction, Adv. Protein Chem., 39, 191, 10.1016/S0065-3233(08)60377-0
Damaschun, 1993, Cold denaturation-induced conformational changes in phosphoglycerate kinase from yeast, Biochemistry, 32, 7739, 10.1021/bi00081a019
Richardson, 2000, Difference in the mechanisms of the cold and heat induced unfolding of thioredoxin h from Chlamydomonas reinhardtii: spectroscopic and calorimetric studies, Biochemistry, 39, 11154, 10.1021/bi000610b
Adrover, 2010, Understanding cold denaturation: the case study of Yfh1, J. Am. Chem. Soc., 132, 16240, 10.1021/ja1070174
Lopez, 2008, Mechanistic elements of protein cold denaturation, J. Phys. Chem. B, 112, 5961, 10.1021/jp075928t
Mandell, 1998, Identification of protein-protein interfaces by decreased amide proton solvent accessibility, Proc. Natl. Acad. Sci. USA, 95, 14705, 10.1073/pnas.95.25.14705
Hughes, 2001, Phosphorylation causes subtle changes in solvent accessibility at the interdomain interface of methylesterase CheB, J. Mol. Biol., 307, 967, 10.1006/jmbi.2001.4523
Truhlar, 2006, Regions of IkappaBalpha that are critical for its inhibition of NF-kappaB.DNA interaction fold upon binding to NF-kappaB, Proc. Natl. Acad. Sci. USA, 103, 18951, 10.1073/pnas.0605794103
Baez, 2012, Expanded monomeric intermediate upon cold and heat unfolding of phosphofructokinase-2 from Escherichia coli, Biophys. J., 103, 2187, 10.1016/j.bpj.2012.09.043
Griko YuV, 1994, Differences in the processes of beta-lactoglobulin cold and heat denaturations, Biophys. J., 67, 356, 10.1016/S0006-3495(94)80488-6
Mizuguchi, 2000, Cold denaturation of alpha-lactalbumin, Proteins, 38, 407, 10.1002/(SICI)1097-0134(20000301)38:4<407::AID-PROT6>3.0.CO;2-#
Kunugi, 2002, Cold denaturation of proteins under high pressure, Biochim. Biophys. Acta, 1595, 329, 10.1016/S0167-4838(01)00354-5
Azuaga, 1992, Heat and cold denaturation of beta-lactoglobulin B, FEBS Lett., 309, 258, 10.1016/0014-5793(92)80784-E
Chen, 1989, Low-temperature unfolding of a mutant of phage T4 lysozyme. 2. Kinetic investigations, Biochemistry, 28, 691, 10.1021/bi00428a042
Chen, 1989, Low-temperature unfolding of a mutant of phage T4 lysozyme. 1. Equilibrium studies, Biochemistry, 28, 685, 10.1021/bi00428a041
Dias, 2008, Microscopic mechanism for cold denaturation, Phys. Rev. Lett., 100, 118101, 10.1103/PhysRevLett.100.118101
Babul, 1978, Phosphofructokinases from Escherichia coli. Purification and characterization of the nonallosteric isozyme, J. Biol. Chem., 253, 4350, 10.1016/S0021-9258(17)34726-9
Bradford, 1976, A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding, Anal. Biochem., 72, 248, 10.1016/0003-2697(76)90527-3
Brown, 2006, Macromolecular size-and-shape distributions by sedimentation velocity analytical ultracentrifugation, Biophys. J., 90, 4651, 10.1529/biophysj.106.081372
Houtman, 2007, Studying multisite binary and ternary protein interactions by global analysis of isothermal titration calorimetry data in SEDPHAT: application to adaptor protein complexes in cell signaling, Protein Sci., 16, 30, 10.1110/ps.062558507
Schuck, 2003, On the analysis of protein self-association by sedimentation velocity analytical ultracentrifugation, Anal. Biochem., 320, 104, 10.1016/S0003-2697(03)00289-6
Baez, 2009, Reversible unfolding of dimeric phosphofructokinase-2 from Escherichia coli reveals a dominant role of inter-subunit contacts for stability, FEBS Lett., 583, 2054, 10.1016/j.febslet.2009.05.034
Mandell, 1998, Measurement of amide hydrogen exchange by MALDI-TOF mass spectrometry, Anal. Chem., 70, 3987, 10.1021/ac980553g
Wales, 2008, High-speed and high-resolution UPLC separation at zero degrees Celsius, Anal. Chem., 80, 6815, 10.1021/ac8008862
Bai, 1993, Primary structure effects on peptide group hydrogen exchange, Proteins, 17, 75, 10.1002/prot.340170110
Croy, 2004, Biophysical characterization of the free IkappaBalpha ankyrin repeat domain in solution, Protein Sci., 13, 1767, 10.1110/ps.04731004
Pometun, 2006, Cold denaturation of encapsulated ubiquitin, J. Am. Chem. Soc., 128, 10652, 10.1021/ja0628654
Luan, 2013, Cooperative cold denaturation: the case of the C-terminal domain of the ribosomal protein L9, Biochemistry, 52, 2402, 10.1021/bi3016789
Li, 2007, The cold denatured state is compact but expands at low temperatures: hydrodynamic properties of the cold denatured state of the C-terminal domain of L9, J. Mol. Biol., 368, 256, 10.1016/j.jmb.2007.02.011
Shan, 2010, The cold denatured state of the C-terminal domain of protein L9 is compact and contains both native and non-native structure, J. Am. Chem. Soc., 132, 4669, 10.1021/ja908104s
Romero-Romero, 2011, Highly anomalous energetics of protein cold denaturation linked to folding-unfolding kinetics, PLoS ONE, 6, e23050, 10.1371/journal.pone.0023050
Zhang, 1993, Determination of amide hydrogen exchange by mass spectrometry: a new tool for protein structure elucidation, Protein Sci., 2, 522, 10.1002/pro.5560020404
Engen, 1997, Identification and localization of slow, natural, cooperative unfolding in the hematopoietic cell kinase SH3 domain by amide hydrogen exchange and mass spectrometry, Biochemistry, 36, 14384, 10.1021/bi971635m
Engen, 1999, Hydrogen exchange shows peptide binding stabilizes motions in Hck SH2, Biochemistry, 38, 8926, 10.1021/bi982611y
Weber, 1993, Thermodynamics of the association and the pressure dissociation of oligomeric proteins, J. Phys. Chem., 97, 7108, 10.1021/j100129a031
Foguel, 1994, Cold denaturation of a repressor-operator complex: the role of entropy in protein-DNA recognition, Proc. Natl. Acad. Sci. USA, 91, 8244, 10.1073/pnas.91.17.8244
Baez, 2011, Folding kinetic pathway of phosphofructokinase-2 from Escherichia coli: a homodimeric enzyme with a complex domain organization, FEBS Lett., 585, 2158, 10.1016/j.febslet.2011.05.041
Oshima, 2009, A theoretical analysis on characteristics of protein structures induced by cold denaturation, J. Chem. Phys., 131, 205102, 10.1063/1.3265985
Das, 2012, Direct characterization of hydrophobic hydration during cold and pressure denaturation, J. Phys. Chem. B, 116, 5342, 10.1021/jp211832c
Panick, 1998, Structural characterization of the pressure-denatured state and unfolding/refolding kinetics of staphylococcal nuclease by synchrotron small-angle X-ray scattering and Fourier-transform infrared spectroscopy, J. Mol. Biol., 275, 389, 10.1006/jmbi.1997.1454
Davidovic, 2009, Protein cold denaturation as seen from the solvent, J. Am. Chem. Soc., 131, 1025, 10.1021/ja8056419
Levy, 2006, Water mediation in protein folding and molecular recognition, Annu. Rev. Biophys. Biomol. Struct., 35, 389, 10.1146/annurev.biophys.35.040405.102134
Parducci, 2006, Evidence for a catalytic Mg2+ ion and effect of phosphate on the activity of Escherichia coli phosphofructokinase-2: regulatory properties of a ribokinase family member, Biochemistry, 45, 9291, 10.1021/bi060026o
Bork, 1993, Convergent evolution of similar enzymatic function on different protein folds: the hexokinase, ribokinase, and galactokinase families of sugar kinases, Protein Sci., 2, 31, 10.1002/pro.5560020104