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Differential Scanning Calorimetry of Proteins: an Overview and Some Recent Developments

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Advanced Techniques in Biophysics

Part of the book series: Springer Series in Biophysics ((BIOPHYSICS,volume 10))

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References

  • Baldwin RL (2002) Making a network of hydrophobic clusters. Science 295:487–489

    Article  Google Scholar 

  • Brandts JF, Hu CQ, Lin LN (1989) A simple model for proteins with interacting domains. Applications to scanning calorimetry data. Biochemistry 28:8588–8596

    Article  Google Scholar 

  • Conejero-Lara F, Mateo PL, Aviles FX, Sanchez-Ruiz JM (1991) Effect of Zn2+ on the thermal denaturation of carboxypeptidase B. Biochemistry 30:2067–2072

    Article  Google Scholar 

  • Cooper A (1976) Thermodynamic fluctuations in protein molecules. Proc Natl Acad Sci USA 73:2740–2741

    Article  ADS  Google Scholar 

  • Cooper A (2005) Heat capacity effects in protein folding and ligand binding: a re-evaluation of the role of water in biomolecular thermodynamics. Biophys Chem 115:89–97

    Article  Google Scholar 

  • Cunningham EL, Jaswal SS, Sohk JL, Agard DA (1999) Kinetic stability as mechanism for protein longevity. Proc Natl Acad Sci USA 96:11008–11014

    Article  ADS  Google Scholar 

  • Dragan AI, Privalov PL (2002) Unfolding of a leucine zipper is not a simple two-state transition. J Mol Biol 321:891–908

    Article  Google Scholar 

  • Forrer P, Chang C, Ott D, Wlodawer A, Plückthun A (2004) Kinetic stability and crystal structure of the viral capsid protein SHP. J Mol Biol 344:179–193

    Article  Google Scholar 

  • Foss TR, Kelker MS, Wiseman RL, Wilson IA, Kelly JW (2005) Kinetic stabilization of the native state by protein engineering: implications for inhibition of transthyretin amyloidogenesis. J Mol Biol 347:841–854

    Article  Google Scholar 

  • Freire E (1994) Statistical thermodynamics analysis of differential scanning calorimetry data: structural deconvolution of heat capacity function of proteins. Methods Enzymol 240:502–530

    Article  Google Scholar 

  • Freire E (1995) Differential scanning calorimetry. Methods Mol Biol 40:191–218

    Google Scholar 

  • Freire E, van Osdol WW, Mayorga OL, Sanchez-Ruiz JM (1990) Calorimetrically determined dynamics of complex unfolding transitions in proteins. Annu Rev Biophys Biophys Chem 19:159–188

    Article  Google Scholar 

  • Freire E, Murphy KP, Sanchez-Ruiz JM, Galisteo ML, Privalov PL (1992) The molecular basis of cooperativity in protein folding. Thermodynamic dissection of interdomain interactions in phosphoglycerate kinase. Biochemistry 31:250–256

    Article  Google Scholar 

  • Fukada H, Sturtevant JM, Quiocho F (1983) Thermodynamics of the binding of L-arabinose and of D-galactose to the L-arabinose-binding protein of Escherichia coli. J Biol Chem 258:13193–13198

    Google Scholar 

  • Garcia-Mira MM, Sadqui M, Fischer N, Sanchez-Ruiz JM, Muñoz V (2002) Experimental identification of downhill folding. Science 298:2191–2195

    Article  ADS  Google Scholar 

  • Gomez J, Hilser VJ, Xie D, Freire E (1995) The heat capacity of proteins. Proteins 22:404–412

    Article  Google Scholar 

  • Greene RF, Pace CN (1974) Urea and guanidinium chloride denaturation of ribonuclease, α-chymotrypsin, and β-lactoglobulin. J Biol Chem 249:5388–5393

    Google Scholar 

  • Guzman-Casado M, Parody-Morreale A, Robic S, Marqusee S, Sanchez-Ruiz JM (2003) Energetic evidence for formation of a pH-dependent hydrophobic cluster in the denatured state of Thermus thermophilus ribonuclease H. J Mol Biol 329:731–743

    Article  Google Scholar 

  • Ibarra-Molero B, Perez-Jimenez R, Godoy-Ruiz R, Sanchez-Ruiz JM (2004) Linkage between temperature and chemical denaturant effects on protein stability: the interpretation of calorimetrically determined m values. In: Doyle M, Ladbury J (eds) Biocalorimetry II: applications of calorimetry in the biological sciences. Wiley, New York, pp 203–214

    Google Scholar 

  • Irun MP, Garcia-Mira MM, Sanchez-Ruiz JM, Sancho J (2001) Native hydrogen bonds in a molten globule: the apoflavodoxin thermal intermediate. J Mol Biol 306:877–888

    Article  Google Scholar 

  • Jackson SE (1998) How do small single-domain proteins fold? Folding Des 3:R81–R91

    Article  Google Scholar 

  • Jackson WM, Brandts JF (1970) Thermodynamics of protein denaturation. A calorimetric study of reversible denaturation of chymotrypsinogen and conclusions regarding accuracy of two-state approximation. Biochemistry 9:2294–2301

    Article  Google Scholar 

  • Jaswal SS, Sohl JL, Dans JH, Agard DA (2002) Energetic landscape of alpha-lytic protease optimizes longevity through kinetic stability. Nature 415:343–346

    Article  ADS  Google Scholar 

  • Jaswal SS, Truhlar SM, Dill KA, Agard DA (2005) Comprehensive analysis of protein folding activation thermodynamics reveals a universal behaviour violated by kinetically stable proteins. J Mol Biol 347:355–366

    Article  Google Scholar 

  • Jayaraman S, Gantz D, Gursky O (2005a) Structural basis for thermal stability of human low-density lipoprotein. Biochemistry 44:3965–3971

    Article  Google Scholar 

  • Jayaraman S, Gantz D, Gursky O (2005b) Kinetic stabilization and function of apoliporptein A-2-DMPC disks: camparison with apo A-1 and apo C-1. Biophys J 88:2907–2918

    Article  Google Scholar 

  • Kaushik JK, Ogasahara K, Yutani K (2002) The unusually slow relaxation kinetics of the folding-unfolding of pyrrolydone carboxyl peptidase from a hyperthermophile, pyroccocus furiosus. J Mol Biol 316:991–1003

    Article  Google Scholar 

  • Kaya H, Chan HS (2000) Polymer principles of protein calorimetric two-state cooperativity. Proteins 40:637–661

    Article  Google Scholar 

  • Kholodenko V, Freire E (1999) A simple method to measure the absolute heat capacity of proteins. Anal Biochem 270:336–338

    Article  Google Scholar 

  • Klein-Seetharaman J, Oikawa M, Grimshaw SB, Wimer J, Duchart E, Ueada T et al (2002) Long-range interactions a non-native protein. Science 295:1719–1722

    Article  ADS  Google Scholar 

  • Luque I, Freire E (1998) Structure-based prediction of binding affinities and molecular design of peptide ligands. Methods Enzymol 295:100–127

    Article  Google Scholar 

  • Luque I, Leavitt SA, Freire E (2002) The linkage between protein folding and functional cooperativity: two sides of the same coin? Annu Rev Biophys Biomol Struct 31:235–256

    Article  Google Scholar 

  • Lynch SM, Boswell SA, Colon W (2004) Kinetic stability of Cu/Zn superoxide dismutase is dependent on its metal ligands: implications for ALS. Biochemistry 43:16525–16531

    Article  Google Scholar 

  • Makhatadze GI (1998) Measuring protein thermostability by differential scanning calorimetry. Current protocols in protein science 7.9.1–7.9.14. Wiley, New York

    Google Scholar 

  • Makhatadze GI, Privalov PL (1995) Energetics of protein structure. Adv Protein Chem 47:307–425

    Article  Google Scholar 

  • Manly SP, Mathews KS, Sturtevant JM (1985) Thermal denaturation of the core protein of lac repressor. Biochemistry 24:3842–3846

    Article  Google Scholar 

  • Manning M, Colon W (2004) Structural basis of protein kinetic stability: resistance to sodium dodecyl sulphate suggests a central role for rigidity and a bias toward beta-sheet structure. Biochemistry 43:11248–11254

    Article  Google Scholar 

  • Mehta R, Gantz DL, Gusky O (2003) Human plasma high-density lipoproteins are stabilized by kinetic factors. J Mol Biol 328:183–192

    Article  Google Scholar 

  • Muñoz V, Sanchez-Ruiz JM (2004) Exploring protein-folding ensembles: a variable-barrier model for the analysis of equilibrium unfolding experiments. Proc Natl Acad Sci USA 101:17646–17651

    Article  ADS  Google Scholar 

  • Myers JK, Pace CN, Scholtz JM (1995) Denaturant m values and heat capacity changes: relation to changes in accessible surface areas of protein unfolding. Protein Sci 4:2138–2148

    Article  Google Scholar 

  • Naganathan AN, Perez-Jimenez R, Sanchez-Ruiz JM, Muñoz V (2005) Robustness of downhill folding: guidelines for the analysis of equilibrium folding experiments on small proteins. Biochemistry 44:7435–7449

    Article  Google Scholar 

  • Oliva FY, Muñoz V (2004) A simple thermodynamic test to discriminate between two-state and downhill folding. J Am Chem Soc 126:8596–8597

    Article  Google Scholar 

  • Perez-Jimenez R, Godoy-Ruiz R, Ibarra-Molero B, Sanchez-Ruiz JM (2004) The efficiency of different salts to screen charge interactions in proteins: a Hofmeister effect? Biophys J 86:2414–2429

    Article  Google Scholar 

  • Persikov AV, Brodsky B (2000) Unstable molecules from stable tissues. Proc Natl Acad Sci USA 99:1101–1103

    Article  Google Scholar 

  • Petrassi MM, Johnson SM, Purkey HE, Chiang KP, Walkup T, Jinag X, Powers ET, Kelly JW (2005) Potent and selective structure-based dibenzofuran inhibitors of transthyretin amylodogenedis: kinetic stabilization of the native state. J Am Chem Soc 127:6662–6671

    Article  Google Scholar 

  • Plaza del Pino IM, Pace CN, Freire E (1992) Temperature and guanidinium chloride dependence of the structural stability of ribonuclease T1. Biochemistry 31:11196–11202

    Article  Google Scholar 

  • Plaza del Pino IM, Ibarra-Molero B, Sanchez-Ruiz JM (2000) Lower kinetic limit to protein thermal stability: a proposal regarding protein stability in vivo and its relation with misfolding diseases. Proteins 40:58–70

    Article  Google Scholar 

  • Plotnikov VV, Brandts JM, Lin LN, Brandts JF (1997) A new ultrasensitive scanning calorimeter. Anal Biochem 250:237–244

    Article  Google Scholar 

  • Privalov PL (1979) Stability of proteins: Small globular proteins. Adv Protein Chem 33:167–241

    Article  Google Scholar 

  • Privalov PL (1980) Scanning microcalorimeters for studying macromolecules. Pure Appl Chem 52:479–497

    Article  Google Scholar 

  • Privalov PL (1982) Stability of proteins. Proteins which do not present a single cooperative system. Adv Protein Chem 35:1–104

    Article  Google Scholar 

  • Privalov PL (1989) Thermodynamic problems of protein structure. Annu Rev Biophys Biophys Chem 18:47–69

    Article  Google Scholar 

  • Ramsay G, Freire E (1989) Linked thermal and solute perturbation analysis of cooperative domain interactions in proteins. Structural stability of diphtheria toxin. Biochemistry 29:8677–8683

    Article  Google Scholar 

  • Robertson A, Murphy KP (1997) Protein structure and the energetics of protein stability. Chem Rev 97:1251–1268

    Article  Google Scholar 

  • Robic S, Guzman-Casado M, Sanchez-Ruiz JM, Marqusee S (2003) Role of residual structure in the unfolded state of a thermophilic protein. Proc Natl Acad Sci USA 100:11345–11349

    Article  ADS  Google Scholar 

  • Rosgen J, Hinz HJ (2001) Folding energetics of ligand binding proteins. I. Theoretical model. J Mol Biol 306:825–835

    Article  Google Scholar 

  • Rosssengarth A, Rosgen J, Hinz HJ, Gerke V (2001) Folding energetics of ligand binding proteins. II. Cooperative binding of Ca2+ to annexin. J Mol Biol 306:825–835

    Article  Google Scholar 

  • Sanchez-Ruiz JM (1992) A theoretical analysis of Lumry-Eyring models in differential scanning calorimetry. Biophys J 61:921–935

    Article  Google Scholar 

  • Sanchez-Ruiz JM (1995) Differential scanning calorimetry of proteins. Subcell Biochem 24:133–176

    Google Scholar 

  • Sanchez-Ruiz JM, Mateo PL (1987) Differential scanning calorimetry of membrane proteins. Revis Biol Celular 11:15–45

    Google Scholar 

  • Schnyrov VL, Zhadan GG, Cobaleda C, Muñoz-Barroso I, Villar E (1997) A differential scanning calorimetric study of Newcastle disease virus: identification of proteins involved in thermal transitions. Arch Biochem Biophys 341:89–97

    Article  Google Scholar 

  • Shortle D, Ackerman MS (2001) Persistence of native-like topology in a denatured protein in 8 M urea. Science 293:487–489

    Article  Google Scholar 

  • Thórólfsson M, Ibarra-Molero B, Fojan P, Petersen SB, Sanchez-Ruiz JM, Martínez A (2002) L-Phenylalanine binding and domain organization in human phenylalanine hydroxylase: a differential scanning calorimetry study. Biochemistry 41:7573–7585

    Article  Google Scholar 

  • Vogl T, Jattzke C, Hinz HJ, Benz J, Huber R (1997) Thermodynamic stability of annexin VE17G: equilibrium parameters from an irreversible unfolding transition. Biochemistry 36:1657–1668

    Article  Google Scholar 

  • Wiseman RL, Johnson SM, Kelker MS, Foss T, Wilson IA, Kelly JW (2005) Kinetic stabilization of an oligomeric protein by a single ligand event. J Am Chem Soc 127:5540–5541

    Article  Google Scholar 

  • Zhou YQ, Hall CK, Karplus M (1999) The calorimetric criterion for a two-state process revisited. Protein Sci 8:1064–1074

    Article  Google Scholar 

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Authors and Affiliations

  1. Facultad de Ciencias, Departamento de Quimica Fisica, Universidad de Granada, Fuentenueva s/n, 18071, Granada, Spain

    Beatriz Ibarra-Molero & Jose M. Sanchez-Ruiz

Authors
  1. Beatriz Ibarra-Molero
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  2. Jose M. Sanchez-Ruiz
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Editors and Affiliations

  1. Departamento de Bioquímica y Biología Molecular, Unidad de Biofísica (Centro Mixto CSIC-UPV), P.O. Box 644, 48080, Bilbao, Spain

    José Luis R. Arrondo  & Alicia Alonso  & 

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Ibarra-Molero, B., Sanchez-Ruiz, J.M. (2006). Differential Scanning Calorimetry of Proteins: an Overview and Some Recent Developments. In: Arrondo, J.L.R., Alonso, A. (eds) Advanced Techniques in Biophysics. Springer Series in Biophysics, vol 10. Springer, Berlin, Heidelberg . https://doi.org/10.1007/3-540-30786-9_2

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