Quantifying the thermodynamics of protein unfolding using 2D NMR spectroscopy

[1]  Caitlin M. Davis,et al.  Quantifying protein dynamics and stability in a living organism , 2019, Nature Communications.

[2]  A. Pastore,et al.  Generalized View of Protein Folding: In Medio Stat Virtus. , 2019, Journal of the American Chemical Society.

[3]  G. Pielak,et al.  Surface Charge Modulates Protein-Protein Interactions in Physiologically Relevant Environments. , 2018, Biochemistry.

[4]  A. Pastore,et al.  The Emperor's new clothes: Myths and truths of in-cell NMR. , 2017, Archives of biochemistry and biophysics.

[5]  Annalisa Pastore,et al.  An optimized strategy to measure protein stability highlights differences between cold and hot unfolded states , 2017, Nature Communications.

[6]  G. Pielak,et al.  In-cell thermodynamics and a new role for protein surfaces , 2016, Proceedings of the National Academy of Sciences.

[7]  J. Danielsson,et al.  Thermodynamics of protein destabilization in live cells , 2015, Proceedings of the National Academy of Sciences.

[8]  Andreas Plückthun,et al.  Single-molecule spectroscopy of protein conformational dynamics in live eukaryotic cells , 2015, Nature Methods.

[9]  A. Pastore,et al.  Trapping a salt-dependent unfolding intermediate of the marginally stable protein Yfh1 , 2014, Front. Mol. Biosci..

[10]  A. Pastore,et al.  Yeast Frataxin Is Stabilized by Low Salt Concentrations: Cold Denaturation Disentangles Ionic Strength Effects from Specific Interactions , 2014, PloS one.

[11]  A. Pastore,et al.  The effect of crowding and confinement: a comparison of Yfh1 stability in different environments , 2013, Physical biology.

[12]  M. Gruebele,et al.  Protein stability and folding kinetics in the nucleus and endoplasmic reticulum of eucaryotic cells. , 2011, Biophysical journal.

[13]  P. Temussi,et al.  Cystatins: a versatile family , 2011, Biomolecular concepts.

[14]  John L. Markley,et al.  Simultaneous Quantification and Identification of Individual Chemicals in Metabolite Mixtures by Two-Dimensional Extrapolated Time-Zero 1H−13C HSQC (HSQC0) , 2011, Journal of the American Chemical Society.

[15]  A. Pastore,et al.  A natural and readily available crowding agent: NMR studies of proteins in hen egg white , 2010, Proteins.

[16]  A. Pastore,et al.  Cold denaturation of yeast frataxin offers the clue to understand the effect of alcohols on protein stability. , 2008, Journal of the American Chemical Society.

[17]  Annalisa Pastore,et al.  Unbiased cold denaturation: low- and high-temperature unfolding of yeast frataxin under physiological conditions. , 2007, Journal of the American Chemical Society.

[18]  G. Gellerstedt,et al.  Quantitative 2D HSQC NMR determination of polymer structures by selecting suitable internal standard references , 2007, Magnetic resonance in chemistry : MRC.

[19]  T. Szyperski,et al.  Combined NMR-observation of cold denaturation in supercooled water and heat denaturation enables accurate measurement of ΔCp of protein unfolding , 2006, European Biophysics Journal.

[20]  Andrea Bernini,et al.  Three-dimensional computation of atom depth in complex molecular structures , 2005, Bioinform..

[21]  A. Pastore,et al.  The Factors Governing the Thermal Stability of Frataxin Orthologues: How To Increase a Protein's Stability , 2004 .

[22]  A. Pastore,et al.  Letter to the Editor: NMR assignment of the 1H, 15N and 13C resonances of the E. coli frataxin orthologue, CyaY , 2003, Journal of biomolecular NMR.

[23]  Franca Fraternali,et al.  POPS: a fast algorithm for solvent accessible surface areas at atomic and residue level , 2003, Nucleic Acids Res..

[24]  A. Pastore,et al.  A structural approach to understanding the iron-binding properties of phylogenetically different frataxins. , 2002, Human molecular genetics.

[25]  L Mayne,et al.  Mechanisms and uses of hydrogen exchange. , 1996, Current opinion in structural biology.

[26]  M. Billeter,et al.  MOLMOL: a program for display and analysis of macromolecular structures. , 1996, Journal of molecular graphics.

[27]  K. Thompson,et al.  Thermodynamic characterization of the structural stability of the coiled-coil region of the bZIP transcription factor GCN4. , 1993, Biochemistry.

[28]  V. Saudek,et al.  Gradient-tailored excitation for single-quantum NMR spectroscopy of aqueous solutions , 1992, Journal of biomolecular NMR.

[29]  G. Montelione,et al.  2D chemical exchange NMR spectroscopy by proton-detected heteronuclear correlation , 1989 .

[30]  W. J. Becktel,et al.  Protein stability curves , 1987, Biopolymers.

[31]  G. Bodenhausen,et al.  Two-dimensional correlation of directly and remotely connected transitions by z-filtered COSY , 1986 .

[32]  W. Kabsch,et al.  Dictionary of protein secondary structure: Pattern recognition of hydrogen‐bonded and geometrical features , 1983, Biopolymers.

[33]  L. Gierasch,et al.  A method for direct measurement of protein stability in vivo. , 2009, Methods in molecular biology.

[34]  A. Pastore,et al.  The factors governing the thermal stability of frataxin orthologues: how to increase a protein's stability. , 2004, Biochemistry.

[35]  F. Sérgio.  In medio stat virtus , 2002 .

[36]  Clare Woodward,et al.  Hydrogen exchange rates and protein folding , 1994 .