DOI: 10.1016/j.bbapap.2011.11.005. Thermodynamic and structural analysis of homodimeric proteins: Model of β-lactoglobulin

Thermodynamic and structural analysis of homodimeric proteins: Model of β-lactoglobulin

10.1016/j.bbapap.2011.11.005

Crossref journal-article

Elsevier BV

Biochimica et Biophysica Acta (BBA) - Proteins and Proteomics (78)

Bibliography

Burgos, I., Dassie, S. A., Villarreal, M. A., & Fidelio, G. D. (2012). Thermodynamic and structural analysis of homodimeric proteins: Model of Î²-lactoglobulin. Biochimica et Biophysica Acta (BBA) - Proteins and Proteomics, 1824(2), 383â391.

Authors 4

Inés Burgos (first)
Sergio A. Dassie (additional)
Marcos A. Villarreal (additional)
Gerardo D. Fidelio (additional)

References 66 Referenced 18

10.1126/science.181.4096.223 / Science / Principles that govern the folding of protein chains by Anfinsen (1973)
10.1021/bi00481a024 / Biochemistry / Study of strong to ultratight protein interactions using differential scanning calorimetry by Brandts (1990)
10.1016/j.bbapap.2005.05.003 / Biochim. Biophys. Acta / Ligand-induced thermostability in proteins: thermodynamic analysis of ANS-albumin interaction by Celej (2005)
10.1146/annurev.bb.12.060183.001441 / Annu. Rev. Biophys. Bioeng. / Thermodynamics of protein–ligand interactions: calorimetric approaches by Hinz (1983)
10.1016/S0021-9258(19)34083-9 / J. Biol. Chem. / Ligand-induced biphasic protein denaturation by Shrake (1990)
10.1002/bip.360320804 / Biopolymers / Origins and consequences of ligand-induced multiphasic thermal protein denaturation by Shrake (1992)
10.1016/j.jmb.2005.03.023 / J. Mol. Biol. / Regulation by oligomerization in a mycobacterial folate biosynthetic enzyme by Goulding (2005)
10.1146/annurev.bi.63.070194.001025 / Annu. Rev. Biochem. / The retroviral enzymes by Katz (1994)
10.1016/j.jmb.2003.08.047 / J. Mol. Biol. / A tetramer–octamer equilibrium in Mycobacterium leprae and Escherichia coli RuvA by analytical ultracentrifugation by Lee (2003)
10.1093/nar/gkq800 / Nucleic Acids Res. / Single-Molecule characterization of oligomerization kinetics and equilibria of the tumor suppressor p53 by Rajagopalan (2011)
10.1128/MCB.00283-07 / Mol. Cell. Biol. / Ubiquitination-induced conformational change within the deiodinase dimer is a switch regulating enzyme activity by Sagar (2007)
10.1021/bi0206560 / Biochemistry / Control of the reactivation kinetics of homodimeric triosephosphate isomerase from unfolded monomers by Zomosa-Signoret (2003)
10.1002/bip.1978.360170212 / Biopolymers / Statistical mechanical deconvolution of thermal transitions in macromolecules. I. Theory and application to homogeneous systems by Freire (1978)
{'key': '10.1016/j.bbapap.2011.11.005_bb0070', 'first-page': '123', 'article-title': 'Statistical thermodynamic analysis of the heat capacity function associated with protein folding–unfolding transitions', 'volume': '6', 'author': 'Freire', 'year': '1989', 'journal-title': 'Commun. Mol. Cell Biophys.'} / Commun. Mol. Cell Biophys. / Statistical thermodynamic analysis of the heat capacity function associated with protein folding–unfolding transitions by Freire (1989)
10.1006/jmbi.1997.1263 / J. Mol. Biol. / The structural stability of the co-chaperonin GroES by Boudker (1997)
10.1016/0167-4838(95)00129-I / Biochim. Biophys. Acta / The thermodynamics of association and unfolding of the 205–316 C-terminal fragment of thermolysin by Azuaga (1995)
10.1021/bi952358r / Biochemistry / Presence of a slow dimerization equilibrium on the thermal unfolding of the 205–316 thermolysin fragment at neutral pH by Conejero-Lara (1996)
10.1039/a809763a / Phys. Chem. Chem. Phys. / Statistical thermodynamic treatment of conformational transitions of monomeric and oligomeric proteins by Rösgen (1999)
10.1021/jp804465c / J. Phys. Chem. B / Thermodynamic model for the analysis of calorimetric data of oligomeric proteins by Burgos (2008)
10.3168/jds.S0022-0302(04)73222-1 / J. Dairy Sci. / Invited review: beta-lactoglobulin: binding properties, structure, and function by Kontopidis (2004)
10.1017/S0022029900019634 / J. Dairy Res. / The quantitative partition of the albumin fraction of milk serum proteins by gel chromatography by Davies (1974)
10.1016/0141-8130(96)01130-0 / Int. J. Biol. Macromol. / The effect of temperature and ionic strength on the dimerisation of beta-lactoglobulin by Aymard (1996)
10.1002/prot.21639 / Proteins / Energetics of protein homodimerization: effects of water sequestering on the formation of beta-lactoglobulin dimer by Bello (2008)
10.1016/S0969-2126(97)00205-0 / Structure / Bovine beta-lactoglobulin at 1.8 A resolution—still an enigmatic lipocalin by Brownlow (1997)
10.1021/ja01209a007 / J. Am. Chem. Soc. / Osmotic pressure of β-lactoglobulin solutions by Bull (1946)
10.1042/bj0440033 / Biochem. J. / The sedimentation constant, diffusion constant and molecular weight of lactoglobulin by Cecil (1949)
10.1016/0006-3002(62)90664-9 / Biochim. Biophys. Acta / Thermodynamic study of the reversible dissociation of beta-lactoglobulin B by pH greater than 5.5 by Georges (1962)
10.1021/ja01150a105 / J. Am. Chem. Soc. / X-ray molecular weight of β-lactoglobulin, ovoalbumin, lysozyme and serum albumin by light scattering by Halwer (1951)
10.1021/bi00793a605 / Biochemistry / A thermodynamic analysis of the monomer-dimer association of β-lactoglobulin A at the isoelectric point by Kelly (1971)
10.1021/ja01190a030 / J. Am. Chem. Soc. / X-ray molecular weight of β-lactoglobulin by Senti (1948)
10.1021/ja01497a047 / J. Am. Chem. Soc. / Molecular interactions in β -lactoglobulin. IV. The dissociation of β-lactoglobulin below pH 3.5 by Townend (1960)
10.1016/0003-9861(70)90289-4 / Arch. Biochem. Biophys. / Dissociation of beta-lactoglobulin near neutral pH by Zimmerman (1970)
{'key': '10.1016/j.bbapap.2011.11.005_bb0165', 'series-title': 'Advanced Dairy Chemistry', 'article-title': 'β−lactoglobulin', 'author': 'Sawyer', 'year': '2003'} / Advanced Dairy Chemistry / β−lactoglobulin by Sawyer (2003)
10.1021/bi981016t / Biochemistry / Structural basis of the Tanford transition of bovine beta-lactoglobulin by Qin (1998)
10.1110/ps.17001 / Protein Sci. / Salt-dependent monomer-dimer equilibrium of bovine beta-lactoglobulin at pH 3 by Sakurai (2001)
10.1021/bi992629o / Biochemistry / Structural changes accompanying pH-induced dissociation of the beta-lactoglobulin dimer by Uhrinova (2000)
10.1007/BF01901568 / J. Protein Chem. / Reversible and irreversible modifications of beta-lactoglobulin upon exposure to heat by Cairoli (1994)
10.1021/bi00152a017 / Biochemistry / Calorimetric study of the heat and cold denaturation of beta-lactoglobulin by Griko (1992)
10.1016/0301-4622(89)80053-5 / Biophys. Chem. / Calorimetric and circular dichroic studies of the thermal denaturation of beta-lactoglobulin by Lapanje (1989)
10.1016/0167-4838(94)00225-6 / Biochim. Biophys. Acta / Thermal denaturation of beta-lactoglobulin: effect of protein concentration at pH 6.75 and 8.05 by Qi (1995)
10.1016/j.bbagen.2005.12.025 / Biochim. Biophys. Acta / Effects of heating at neutral and acid pH on the structure of beta-lactoglobulin A revealed by differential scanning calorimetry and circular dichroism spectroscopy by Wada (2006)
10.1021/bi00165a023 / Biochemistry / Influence of transition rates and scan rate on kinetic simulations of differential scanning calorimetry profiles of reversible and irreversible protein denaturation by Lepock (1992)
10.1016/S0065-3233(08)60468-4 / Adv. Protein Chem. / Stability of proteins. Proteins which do not present a single cooperative system by Privalov (1982)
10.1016/S0006-3495(92)81899-4 / Biophys. J. / Theoretical analysis of Lumry-Eyring models in differential scanning calorimetry by Sanchez-Ruiz (1992)
10.1146/annurev.pc.38.100187.002335 / Annu. Rev. Phys. Chem. / Biochemical applications of differential sacanning calorimetry by Sturtevant (1987)
{'key': '10.1016/j.bbapap.2011.11.005_bb0230', 'first-page': '35', 'article-title': 'Characterization of protein–protein interactions by isothermal titration calorimetry', 'volume': '261', 'author': 'Velazquez-Campoy', 'year': '2004', 'journal-title': 'Methods Mol. Biol.'} / Methods Mol. Biol. / Characterization of protein–protein interactions by isothermal titration calorimetry by Velazquez-Campoy (2004)
10.1016/S0076-6879(98)95045-5 / Methods Enzymol. / Prediction of binding energetics from structure using empirical parameterization by Baker (1998)
10.1016/S0065-3233(08)60556-2 / Adv. Protein Chem. / Thermodynamics of structural stability and cooperative folding behavior in proteins by Murphy (1992)
10.1110/ps.9.2.252 / Protein Sci. / Structure-based thermodynamic analysis of the dissociation of protein phosphatase-1 catalytic subunit and microcystin-LR docked complexes by Lavigne (2000)
10.1016/S0022-2836(05)80360-2 / J. Mol. Biol. / Basic local alignment search tool by Altschul (1990)
10.1110/ps.03154503 / Protein Sci. / A graph-theory algorithm for rapid protein side-chain prediction by Canutescu (2003)
10.1006/jmbi.2001.4865 / J. Mol. Biol. / Extending the accuracy limits of prediction for side-chain conformations by Xiang (2001)
10.1016/S0065-3233(08)60460-X / Adv. Protein Chem. / Stability of proteins: small globular proteins by Privalov (1979)
10.1046/j.0014-2956.2001.02484.x / Eur. J. Biochem. / Thermal unfolding of monomeric and dimeric beta-lactoglobulins by Fessas (2001)
10.1007/s11095-006-0142-8 / Pharm. Res. / FTIR and nDSC as analytical tools for high-concentration protein formulations by Matheus (2006)
10.1073/pnas.73.9.2955 / Proc. Natl. Acad. Sci. U. S. A. / An equation of state describing hydrophobic interactions by Gill (1976)
10.1016/S0022-2836(05)80197-4 / J. Mol. Biol. / Heat capacity of proteins. I. Partial molar heat capacity of individual amino acid residues in aqueous solution: hydration effect by Makhatadze (1990)
10.1016/j.bpc.2004.12.011 / Biophys. Chem. / Heat capacity effects in protein folding and ligand binding: a re-evaluation of the role of water in biomolecular thermodynamics by Cooper (2005)
10.1002/bip.360250307 / Biopolymers / Examination of the secondary structure of proteins by deconvolved FTIR spectra by Byler (1986)
10.1016/0167-4838(88)90152-5 / Biochim. Biophys. Acta / Structural and conformational changes of beta-lactoglobulin B: an infrared spectroscopic study of the effect of pH and temperature by Casal (1988)
10.1016/0079-6107(93)90006-6 / Prog. Biophys. Mol. Biol. / Quantitative studies of the structure of proteins in solution by Fourier-transform infrared spectroscopy by Arrondo (1993)
10.1016/0167-4838(88)90125-2 / Biochim. Biophys. Acta / The solution structure of concanavalin A probed by FT-IR spectroscopy by Arrondo (1988)
10.1016/0014-5793(96)00261-X / FEBS Lett. / Infrared evidence of a beta-hairpin peptide structure in solution by Arrondo (1996)
10.1110/ps.0217702 / Protein Sci. / A kinetic study of β-lactoglobulin amyloid fibril formation by urea by Hamada (2002)
{'key': '10.1016/j.bbapap.2011.11.005_bb0325', 'series-title': 'Protein Folding', 'first-page': '83', 'article-title': 'Physical basis of the stability of folded conformation of proteins', 'author': 'Privalov', 'year': '1992'} / Protein Folding / Physical basis of the stability of folded conformation of proteins by Privalov (1992)
10.1016/S0022-2836(05)80198-6 / J. Mol. Biol. / Heat capacity of proteins. II. Partial molar heat capacity of the unfolded polypeptide chain of proteins: protein unfolding effects by Privalov (1990)

Dates

Type	When
Created	13 years, 8 months ago (Dec. 8, 2011, 5:21 p.m.)
Deposited	3 years, 8 months ago (Dec. 19, 2021, 8:12 a.m.)
Indexed	1 month, 2 weeks ago (July 16, 2025, 9:51 a.m.)
Issued	13 years, 7 months ago (Feb. 1, 2012)
Published	13 years, 7 months ago (Feb. 1, 2012)
Published Print	13 years, 7 months ago (Feb. 1, 2012)

Funders 3

CONICET 10.13039/501100002923 Consejo Nacional de Investigaciones Científicas y Técnicas
Region: Americas
gov (National government)
Labels3
1. National Scientific and Technical Research Council
2. National Scientific and Technical Research Council of Argentina (Consejo Nacional de Investigaciones Científicas y Técnicas)
3. CONICET
ANPyCT (Foncyt)
SECyT-UNC

BibTeX

@article{Burgos_2012, title={Thermodynamic and structural analysis of homodimeric proteins: Model of β-lactoglobulin}, volume={1824}, ISSN={1570-9639}, url={http://dx.doi.org/10.1016/j.bbapap.2011.11.005}, DOI={10.1016/j.bbapap.2011.11.005}, number={2}, journal={Biochimica et Biophysica Acta (BBA) - Proteins and Proteomics}, publisher={Elsevier BV}, author={Burgos, Inés and Dassie, Sergio A. and Villarreal, Marcos A. and Fidelio, Gerardo D.}, year={2012}, month=feb, pages={383–391} }

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      "article-title": "Ligand-induced thermostability in proteins: thermodynamic analysis of ANS-albumin interaction",
      "volume": "1750",
      "author": "Celej",
      "year": "2005",
      "journal-title": "Biochim. Biophys. Acta"
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      "first-page": "285",
      "DOI": "10.1146/annurev.bb.12.060183.001441",
      "article-title": "Thermodynamics of protein\u2013ligand interactions: calorimetric approaches",
      "volume": "12",
      "author": "Hinz",
      "year": "1983",
      "journal-title": "Annu. Rev. Biophys. Bioeng."
    },
    {
      "key": "10.1016/j.bbapap.2011.11.005_bb0025",
      "doi-asserted-by": "crossref",
      "first-page": "5055",
      "DOI": "10.1016/S0021-9258(19)34083-9",
      "article-title": "Ligand-induced biphasic protein denaturation",
      "volume": "265",
      "author": "Shrake",
      "year": "1990",
      "journal-title": "J. Biol. Chem."
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      "volume": "349",
      "author": "Goulding",
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    {
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      "first-page": "133",
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      "author": "Katz",
      "year": "1994",
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      "author": "Lee",
      "year": "2003",
      "journal-title": "J. Mol. Biol."
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    {
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      "author": "Rajagopalan",
      "year": "2011",
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      "author": "Zomosa-Signoret",
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      "volume": "272",
      "author": "Boudker",
      "year": "1997",
      "journal-title": "J. Mol. Biol."
    },
    {
      "key": "10.1016/j.bbapap.2011.11.005_bb0080",
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      "first-page": "95",
      "DOI": "10.1016/0167-4838(95)00129-I",
      "article-title": "The thermodynamics of association and unfolding of the 205\u2013316 C-terminal fragment of thermolysin",
      "volume": "1252",
      "author": "Azuaga",
      "year": "1995",
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    {
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      "author": "Conejero-Lara",
      "year": "1996",
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      "volume": "1",
      "author": "R\u00f6sgen",
      "year": "1999",
      "journal-title": "Phys. Chem. Chem. Phys."
    },
    {
      "key": "10.1016/j.bbapap.2011.11.005_bb0095",
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      "first-page": "14325",
      "DOI": "10.1021/jp804465c",
      "article-title": "Thermodynamic model for the analysis of calorimetric data of oligomeric proteins",
      "volume": "112",
      "author": "Burgos",
      "year": "2008",
      "journal-title": "J. Phys. Chem. B"
    },
    {
      "key": "10.1016/j.bbapap.2011.11.005_bb0100",
      "doi-asserted-by": "crossref",
      "first-page": "785",
      "DOI": "10.3168/jds.S0022-0302(04)73222-1",
      "article-title": "Invited review: beta-lactoglobulin: binding properties, structure, and function",
      "volume": "87",
      "author": "Kontopidis",
      "year": "2004",
      "journal-title": "J. Dairy Sci."
    },
    {
      "key": "10.1016/j.bbapap.2011.11.005_bb0105",
      "doi-asserted-by": "crossref",
      "first-page": "217",
      "DOI": "10.1017/S0022029900019634",
      "article-title": "The quantitative partition of the albumin fraction of milk serum proteins by gel chromatography",
      "volume": "41",
      "author": "Davies",
      "year": "1974",
      "journal-title": "J. Dairy Res."
    },
    {
      "key": "10.1016/j.bbapap.2011.11.005_bb0110",
      "doi-asserted-by": "crossref",
      "first-page": "213",
      "DOI": "10.1016/0141-8130(96)01130-0",
      "article-title": "The effect of temperature and ionic strength on the dimerisation of beta-lactoglobulin",
      "volume": "19",
      "author": "Aymard",
      "year": "1996",
      "journal-title": "Int. J. Biol. Macromol."
    },
    {
      "key": "10.1016/j.bbapap.2011.11.005_bb0115",
      "doi-asserted-by": "crossref",
      "first-page": "1475",
      "DOI": "10.1002/prot.21639",
      "article-title": "Energetics of protein homodimerization: effects of water sequestering on the formation of beta-lactoglobulin dimer",
      "volume": "70",
      "author": "Bello",
      "year": "2008",
      "journal-title": "Proteins"
    },
    {
      "key": "10.1016/j.bbapap.2011.11.005_bb0120",
      "doi-asserted-by": "crossref",
      "first-page": "481",
      "DOI": "10.1016/S0969-2126(97)00205-0",
      "article-title": "Bovine beta-lactoglobulin at 1.8 A resolution\u2014still an enigmatic lipocalin",
      "volume": "5",
      "author": "Brownlow",
      "year": "1997",
      "journal-title": "Structure"
    },
    {
      "key": "10.1016/j.bbapap.2011.11.005_bb0125",
      "doi-asserted-by": "crossref",
      "first-page": "742",
      "DOI": "10.1021/ja01209a007",
      "article-title": "Osmotic pressure of \u03b2-lactoglobulin solutions",
      "volume": "68",
      "author": "Bull",
      "year": "1946",
      "journal-title": "J. Am. Chem. Soc."
    },
    {
      "key": "10.1016/j.bbapap.2011.11.005_bb0130",
      "doi-asserted-by": "crossref",
      "first-page": "33",
      "DOI": "10.1042/bj0440033",
      "article-title": "The sedimentation constant, diffusion constant and molecular weight of lactoglobulin",
      "volume": "44",
      "author": "Cecil",
      "year": "1949",
      "journal-title": "Biochem. J."
    },
    {
      "key": "10.1016/j.bbapap.2011.11.005_bb0135",
      "doi-asserted-by": "crossref",
      "first-page": "737",
      "DOI": "10.1016/0006-3002(62)90664-9",
      "article-title": "Thermodynamic study of the reversible dissociation of beta-lactoglobulin B by pH greater than 5.5",
      "volume": "59",
      "author": "Georges",
      "year": "1962",
      "journal-title": "Biochim. Biophys. Acta"
    },
    {
      "key": "10.1016/j.bbapap.2011.11.005_bb0140",
      "doi-asserted-by": "crossref",
      "first-page": "2786",
      "DOI": "10.1021/ja01150a105",
      "article-title": "X-ray molecular weight of \u03b2-lactoglobulin, ovoalbumin, lysozyme and serum albumin by light scattering",
      "volume": "73",
      "author": "Halwer",
      "year": "1951",
      "journal-title": "J. Am. Chem. Soc."
    },
    {
      "key": "10.1016/j.bbapap.2011.11.005_bb0145",
      "doi-asserted-by": "crossref",
      "first-page": "2639",
      "DOI": "10.1021/bi00793a605",
      "article-title": "A thermodynamic analysis of the monomer-dimer association of \u03b2-lactoglobulin A at the isoelectric point",
      "volume": "10",
      "author": "Kelly",
      "year": "1971",
      "journal-title": "Biochemistry"
    },
    {
      "key": "10.1016/j.bbapap.2011.11.005_bb0150",
      "doi-asserted-by": "crossref",
      "first-page": "3318",
      "DOI": "10.1021/ja01190a030",
      "article-title": "X-ray molecular weight of \u03b2-lactoglobulin",
      "volume": "70",
      "author": "Senti",
      "year": "1948",
      "journal-title": "J. Am. Chem. Soc."
    },
    {
      "key": "10.1016/j.bbapap.2011.11.005_bb0155",
      "doi-asserted-by": "crossref",
      "first-page": "3175",
      "DOI": "10.1021/ja01497a047",
      "article-title": "Molecular interactions in \u03b2 -lactoglobulin. IV. The dissociation of \u03b2-lactoglobulin below pH 3.5",
      "volume": "82",
      "author": "Townend",
      "year": "1960",
      "journal-title": "J. Am. Chem. Soc."
    },
    {
      "key": "10.1016/j.bbapap.2011.11.005_bb0160",
      "doi-asserted-by": "crossref",
      "first-page": "101",
      "DOI": "10.1016/0003-9861(70)90289-4",
      "article-title": "Dissociation of beta-lactoglobulin near neutral pH",
      "volume": "138",
      "author": "Zimmerman",
      "year": "1970",
      "journal-title": "Arch. Biochem. Biophys."
    },
    {
      "key": "10.1016/j.bbapap.2011.11.005_bb0165",
      "series-title": "Advanced Dairy Chemistry",
      "article-title": "\u03b2\u2212lactoglobulin",
      "author": "Sawyer",
      "year": "2003"
    },
    {
      "key": "10.1016/j.bbapap.2011.11.005_bb0170",
      "doi-asserted-by": "crossref",
      "first-page": "14014",
      "DOI": "10.1021/bi981016t",
      "article-title": "Structural basis of the Tanford transition of bovine beta-lactoglobulin",
      "volume": "37",
      "author": "Qin",
      "year": "1998",
      "journal-title": "Biochemistry"
    },
    {
      "key": "10.1016/j.bbapap.2011.11.005_bb0175",
      "doi-asserted-by": "crossref",
      "first-page": "2325",
      "DOI": "10.1110/ps.17001",
      "article-title": "Salt-dependent monomer-dimer equilibrium of bovine beta-lactoglobulin at pH 3",
      "volume": "10",
      "author": "Sakurai",
      "year": "2001",
      "journal-title": "Protein Sci."
    },
    {
      "key": "10.1016/j.bbapap.2011.11.005_bb0180",
      "doi-asserted-by": "crossref",
      "first-page": "3565",
      "DOI": "10.1021/bi992629o",
      "article-title": "Structural changes accompanying pH-induced dissociation of the beta-lactoglobulin dimer",
      "volume": "39",
      "author": "Uhrinova",
      "year": "2000",
      "journal-title": "Biochemistry"
    },
    {
      "key": "10.1016/j.bbapap.2011.11.005_bb0185",
      "doi-asserted-by": "crossref",
      "first-page": "347",
      "DOI": "10.1007/BF01901568",
      "article-title": "Reversible and irreversible modifications of beta-lactoglobulin upon exposure to heat",
      "volume": "13",
      "author": "Cairoli",
      "year": "1994",
      "journal-title": "J. Protein Chem."
    },
    {
      "key": "10.1016/j.bbapap.2011.11.005_bb0190",
      "doi-asserted-by": "crossref",
      "first-page": "8810",
      "DOI": "10.1021/bi00152a017",
      "article-title": "Calorimetric study of the heat and cold denaturation of beta-lactoglobulin",
      "volume": "31",
      "author": "Griko",
      "year": "1992",
      "journal-title": "Biochemistry"
    },
    {
      "key": "10.1016/j.bbapap.2011.11.005_bb0195",
      "doi-asserted-by": "crossref",
      "first-page": "155",
      "DOI": "10.1016/0301-4622(89)80053-5",
      "article-title": "Calorimetric and circular dichroic studies of the thermal denaturation of beta-lactoglobulin",
      "volume": "34",
      "author": "Lapanje",
      "year": "1989",
      "journal-title": "Biophys. Chem."
    },
    {
      "key": "10.1016/j.bbapap.2011.11.005_bb0200",
      "doi-asserted-by": "crossref",
      "first-page": "43",
      "DOI": "10.1016/0167-4838(94)00225-6",
      "article-title": "Thermal denaturation of beta-lactoglobulin: effect of protein concentration at pH 6.75 and 8.05",
      "volume": "1248",
      "author": "Qi",
      "year": "1995",
      "journal-title": "Biochim. Biophys. Acta"
    },
    {
      "key": "10.1016/j.bbapap.2011.11.005_bb0205",
      "doi-asserted-by": "crossref",
      "first-page": "841",
      "DOI": "10.1016/j.bbagen.2005.12.025",
      "article-title": "Effects of heating at neutral and acid pH on the structure of beta-lactoglobulin A revealed by differential scanning calorimetry and circular dichroism spectroscopy",
      "volume": "1760",
      "author": "Wada",
      "year": "2006",
      "journal-title": "Biochim. Biophys. Acta"
    },
    {
      "key": "10.1016/j.bbapap.2011.11.005_bb0210",
      "doi-asserted-by": "crossref",
      "first-page": "12706",
      "DOI": "10.1021/bi00165a023",
      "article-title": "Influence of transition rates and scan rate on kinetic simulations of differential scanning calorimetry profiles of reversible and irreversible protein denaturation",
      "volume": "31",
      "author": "Lepock",
      "year": "1992",
      "journal-title": "Biochemistry"
    },
    {
      "key": "10.1016/j.bbapap.2011.11.005_bb0215",
      "doi-asserted-by": "crossref",
      "first-page": "1",
      "DOI": "10.1016/S0065-3233(08)60468-4",
      "article-title": "Stability of proteins. Proteins which do not present a single cooperative system",
      "volume": "35",
      "author": "Privalov",
      "year": "1982",
      "journal-title": "Adv. Protein Chem."
    },
    {
      "key": "10.1016/j.bbapap.2011.11.005_bb0220",
      "doi-asserted-by": "crossref",
      "first-page": "921",
      "DOI": "10.1016/S0006-3495(92)81899-4",
      "article-title": "Theoretical analysis of Lumry-Eyring models in differential scanning calorimetry",
      "volume": "61",
      "author": "Sanchez-Ruiz",
      "year": "1992",
      "journal-title": "Biophys. J."
    },
    {
      "key": "10.1016/j.bbapap.2011.11.005_bb0225",
      "doi-asserted-by": "crossref",
      "first-page": "463",
      "DOI": "10.1146/annurev.pc.38.100187.002335",
      "article-title": "Biochemical applications of differential sacanning calorimetry",
      "volume": "38",
      "author": "Sturtevant",
      "year": "1987",
      "journal-title": "Annu. Rev. Phys. Chem."
    },
    {
      "key": "10.1016/j.bbapap.2011.11.005_bb0230",
      "first-page": "35",
      "article-title": "Characterization of protein\u2013protein interactions by isothermal titration calorimetry",
      "volume": "261",
      "author": "Velazquez-Campoy",
      "year": "2004",
      "journal-title": "Methods Mol. Biol."
    },
    {
      "key": "10.1016/j.bbapap.2011.11.005_bb0235",
      "doi-asserted-by": "crossref",
      "first-page": "294",
      "DOI": "10.1016/S0076-6879(98)95045-5",
      "article-title": "Prediction of binding energetics from structure using empirical parameterization",
      "volume": "295",
      "author": "Baker",
      "year": "1998",
      "journal-title": "Methods Enzymol."
    },
    {
      "key": "10.1016/j.bbapap.2011.11.005_bb0240",
      "doi-asserted-by": "crossref",
      "first-page": "313",
      "DOI": "10.1016/S0065-3233(08)60556-2",
      "article-title": "Thermodynamics of structural stability and cooperative folding behavior in proteins",
      "volume": "43",
      "author": "Murphy",
      "year": "1992",
      "journal-title": "Adv. Protein Chem."
    },
    {
      "key": "10.1016/j.bbapap.2011.11.005_bb0245",
      "doi-asserted-by": "crossref",
      "first-page": "252",
      "DOI": "10.1110/ps.9.2.252",
      "article-title": "Structure-based thermodynamic analysis of the dissociation of protein phosphatase-1 catalytic subunit and microcystin-LR docked complexes",
      "volume": "9",
      "author": "Lavigne",
      "year": "2000",
      "journal-title": "Protein Sci."
    },
    {
      "key": "10.1016/j.bbapap.2011.11.005_bb0250",
      "doi-asserted-by": "crossref",
      "first-page": "403",
      "DOI": "10.1016/S0022-2836(05)80360-2",
      "article-title": "Basic local alignment search tool",
      "volume": "215",
      "author": "Altschul",
      "year": "1990",
      "journal-title": "J. Mol. Biol."
    },
    {
      "key": "10.1016/j.bbapap.2011.11.005_bb0255",
      "doi-asserted-by": "crossref",
      "first-page": "2001",
      "DOI": "10.1110/ps.03154503",
      "article-title": "A graph-theory algorithm for rapid protein side-chain prediction",
      "volume": "12",
      "author": "Canutescu",
      "year": "2003",
      "journal-title": "Protein Sci."
    },
    {
      "key": "10.1016/j.bbapap.2011.11.005_bb0260",
      "doi-asserted-by": "crossref",
      "first-page": "421",
      "DOI": "10.1006/jmbi.2001.4865",
      "article-title": "Extending the accuracy limits of prediction for side-chain conformations",
      "volume": "311",
      "author": "Xiang",
      "year": "2001",
      "journal-title": "J. Mol. Biol."
    },
    {
      "key": "10.1016/j.bbapap.2011.11.005_bb0265",
      "doi-asserted-by": "crossref",
      "first-page": "167",
      "DOI": "10.1016/S0065-3233(08)60460-X",
      "article-title": "Stability of proteins: small globular proteins",
      "volume": "33",
      "author": "Privalov",
      "year": "1979",
      "journal-title": "Adv. Protein Chem."
    },
    {
      "key": "10.1016/j.bbapap.2011.11.005_bb0270",
      "doi-asserted-by": "crossref",
      "first-page": "5439",
      "DOI": "10.1046/j.0014-2956.2001.02484.x",
      "article-title": "Thermal unfolding of monomeric and dimeric beta-lactoglobulins",
      "volume": "268",
      "author": "Fessas",
      "year": "2001",
      "journal-title": "Eur. J. Biochem."
    },
    {
      "key": "10.1016/j.bbapap.2011.11.005_bb0275",
      "doi-asserted-by": "crossref",
      "first-page": "1350",
      "DOI": "10.1007/s11095-006-0142-8",
      "article-title": "FTIR and nDSC as analytical tools for high-concentration protein formulations",
      "volume": "23",
      "author": "Matheus",
      "year": "2006",
      "journal-title": "Pharm. Res."
    },
    {
      "key": "10.1016/j.bbapap.2011.11.005_bb0280",
      "doi-asserted-by": "crossref",
      "first-page": "2955",
      "DOI": "10.1073/pnas.73.9.2955",
      "article-title": "An equation of state describing hydrophobic interactions",
      "volume": "73",
      "author": "Gill",
      "year": "1976",
      "journal-title": "Proc. Natl. Acad. Sci. U. S. A."
    },
    {
      "key": "10.1016/j.bbapap.2011.11.005_bb0285",
      "doi-asserted-by": "crossref",
      "first-page": "375",
      "DOI": "10.1016/S0022-2836(05)80197-4",
      "article-title": "Heat capacity of proteins. I. Partial molar heat capacity of individual amino acid residues in aqueous solution: hydration effect",
      "volume": "213",
      "author": "Makhatadze",
      "year": "1990",
      "journal-title": "J. Mol. Biol."
    },
    {
      "key": "10.1016/j.bbapap.2011.11.005_bb0290",
      "doi-asserted-by": "crossref",
      "first-page": "89",
      "DOI": "10.1016/j.bpc.2004.12.011",
      "article-title": "Heat capacity effects in protein folding and ligand binding: a re-evaluation of the role of water in biomolecular thermodynamics",
      "volume": "115",
      "author": "Cooper",
      "year": "2005",
      "journal-title": "Biophys. Chem."
    },
    {
      "key": "10.1016/j.bbapap.2011.11.005_bb0295",
      "doi-asserted-by": "crossref",
      "first-page": "469",
      "DOI": "10.1002/bip.360250307",
      "article-title": "Examination of the secondary structure of proteins by deconvolved FTIR spectra",
      "volume": "25",
      "author": "Byler",
      "year": "1986",
      "journal-title": "Biopolymers"
    },
    {
      "key": "10.1016/j.bbapap.2011.11.005_bb0300",
      "doi-asserted-by": "crossref",
      "first-page": "11",
      "DOI": "10.1016/0167-4838(88)90152-5",
      "article-title": "Structural and conformational changes of beta-lactoglobulin B: an infrared spectroscopic study of the effect of pH and temperature",
      "volume": "957",
      "author": "Casal",
      "year": "1988",
      "journal-title": "Biochim. Biophys. Acta"
    },
    {
      "key": "10.1016/j.bbapap.2011.11.005_bb0305",
      "doi-asserted-by": "crossref",
      "first-page": "23",
      "DOI": "10.1016/0079-6107(93)90006-6",
      "article-title": "Quantitative studies of the structure of proteins in solution by Fourier-transform infrared spectroscopy",
      "volume": "59",
      "author": "Arrondo",
      "year": "1993",
      "journal-title": "Prog. Biophys. Mol. Biol."
    },
    {
      "key": "10.1016/j.bbapap.2011.11.005_bb0310",
      "doi-asserted-by": "crossref",
      "first-page": "261",
      "DOI": "10.1016/0167-4838(88)90125-2",
      "article-title": "The solution structure of concanavalin A probed by FT-IR spectroscopy",
      "volume": "952",
      "author": "Arrondo",
      "year": "1988",
      "journal-title": "Biochim. Biophys. Acta"
    },
    {
      "key": "10.1016/j.bbapap.2011.11.005_bb0315",
      "doi-asserted-by": "crossref",
      "first-page": "35",
      "DOI": "10.1016/0014-5793(96)00261-X",
      "article-title": "Infrared evidence of a beta-hairpin peptide structure in solution",
      "volume": "384",
      "author": "Arrondo",
      "year": "1996",
      "journal-title": "FEBS Lett."
    },
    {
      "key": "10.1016/j.bbapap.2011.11.005_bb0320",
      "doi-asserted-by": "crossref",
      "first-page": "2417",
      "DOI": "10.1110/ps.0217702",
      "article-title": "A kinetic study of \u03b2-lactoglobulin amyloid fibril formation by urea",
      "volume": "11",
      "author": "Hamada",
      "year": "2002",
      "journal-title": "Protein Sci."
    },
    {
      "key": "10.1016/j.bbapap.2011.11.005_bb0325",
      "series-title": "Protein Folding",
      "first-page": "83",
      "article-title": "Physical basis of the stability of folded conformation of proteins",
      "author": "Privalov",
      "year": "1992"
    },
    {
      "key": "10.1016/j.bbapap.2011.11.005_bb0330",
      "doi-asserted-by": "crossref",
      "first-page": "385",
      "DOI": "10.1016/S0022-2836(05)80198-6",
      "article-title": "Heat capacity of proteins. II. Partial molar heat capacity of the unfolded polypeptide chain of proteins: protein unfolding effects",
      "volume": "213",
      "author": "Privalov",
      "year": "1990",
      "journal-title": "J. Mol. Biol."
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