DOI: 10.1074/jbc.m111.315648. Interconnection of Salt-induced Hydrophobic Compaction and Secondary Structure Formation Depends on Solution Conditions

Interconnection of Salt-induced Hydrophobic Compaction and Secondary Structure Formation Depends on Solution Conditions

10.1074/jbc.m111.315648

Crossref journal-article

Elsevier BV

Journal of Biological Chemistry (78)

Bibliography

Haldar, S., & Chattopadhyay, K. (2012). Interconnection of Salt-induced Hydrophobic Compaction and Secondary Structure Formation Depends on Solution Conditions. Journal of Biological Chemistry, 287(14), 11546â11555.

Authors 2

Shubhasis Haldar (first)
Krishnananda Chattopadhyay (additional)

References 53 Referenced 26

10.1016/S0969-2126(96)00121-9 / Structure / Fast events in protein folding by Eaton (1996)
10.1073/pnas.93.21.11615 / Proc. Natl. Acad. Sci. U.S.A. / Diffusion-limited contact formation in unfolded cytochrome c: Estimating the maximum rate of protein folding by Hagen (1996)
10.1073/pnas.0500127102 / Proc. Natl. Acad. Sci. U.S.A. / The kinetics of conformational fluctuations in an unfolded protein measured by fluorescence methods by Chattopadhyay (2005)
10.1073/pnas.0704073104 / Proc. Natl. Acad. Sci. U.S.A. / Dynamics of equilibrium structural fluctuations of apomyoglobin measured by fluorescence correlation spectroscopy by Chen (2007)
10.1038/75932 / Nat. Struct. Biol. / Stepwise formation of α-helices during cytochrome c folding by Akiyama (2000)
10.1038/nsb0598-385 / Nat. Struct. Biol. / Evidence for barrier-limited protein folding kinetics on the microsecond time scale by Shastry (1998)
10.1021/bi012042l / Biochemistry / The intestinal fatty acid binding protein: The role of turns in fast and slow folding processes by Chattopadhyay (2002)
10.1038/nsb0197-44 / Nat. Struct. Biol. / Folding of cytochrome c initiated by submillisecond mixing by Takahashi (1997)
10.3390/ijms10041476 / Int. J. Mol. Sci. / Early events, kinetic intermediates, and the mechanism of protein folding in cytochrome c by Goldbeck (2009)
10.1021/ja0400077 / J. Am. Chem. Soc. / The earliest events in protein folding: A structural requirement for ultrafast folding in cytochrome c by Chen (2004)
10.1016/S0014-5793(02)02441-9 / FEBS Lett. / The chicken-egg scenario of protein folding revisited by Uversky (2002)
10.1002/(SICI)1097-0134(199604)24:4<413::AID-PROT1>3.0.CO;2-F / Proteins / Molecular collapse: The rate-limiting step in two-state cytochrome c folding by Sosnick (1996)
10.1073/pnas.94.16.8545 / Proc. Natl. Acad. Sci. U.S.A. / Ultrafast signals in protein folding and the polypeptide contracted state by Sosnick (1997)
10.1074/jbc.M110.116673 / J. Biol. Chem. / Role of protein stabilizers on the conformation of the unfolded state of cytochrome c and its early folding kinetics: Investigation at single molecular resolution by Haldar (2010)
10.1021/bi802065j / Biochemistry / Effect of arginine on protein aggregation studied by fluorescence correlation spectroscopy and other biophysical methods by Ghosh (2009)
10.1021/la200580z / Langmuir / Effects of arginine and other solution additives on the self-association of different surfactants: An investigation at single-molecule resolution by Haldar (2011)
10.1073/pnas.95.23.13573 / Proc. Natl. Acad. Sci. U.S.A. / Dynamics of fluorescence fluctuations in green fluorescent protein observed by fluorescence correlation spectroscopy by Haupts (1998)
10.1016/S0006-3495(03)75006-1 / Biophys. J. / Measuring size distribution in highly heterogeneous systems with fluorescence correlation spectroscopy by Sengupta (2003)
10.1117/1.1779234 / J. Biomed Opt / Quick tour of fluorescence correlation spectroscopy from its inception by Elson (2004)
10.1021/bi0118512 / Biochemistry / Biological and chemical applications of fluorescence correlation spectroscopy: A review by Hess (2002)
10.1073/pnas.0604712103 / Proc. Natl. Acad. Sci. U.S.A. / A two-dimensional view of the folding energy landscape of cytochrome c by Werner (2006)
10.1016/j.jmb.2004.10.085 / J. Mol. Biol. / Many faces of the unfolded state: Conformational heterogeneity in denatured yeast cytochrome c by Pletneva (2005)
10.1021/bi980535t / Biochemistry / Protein denaturation: A small-angle x-ray scattering study of the ensemble of unfolded states of cytochrome c by Segel (1998)
10.1016/S0014-5793(97)00058-6 / FEBS Lett. / Ribonuclease T1 has different dimensions in the thermally and chemically denatured states: A dynamic light scattering study by Gast (1997)
10.1073/pnas.2033863100 / Proc. Natl. Acad. Sci. U.S.A. / How fast is protein hydrophobic collapse? by Sadqi (2003)
10.1021/ja808305u / J. Am. Chem. Soc. / Protein folding, protein collapse, and tanford's transfer model: Lessons from single-molecule FRET by Ziv (2009)
10.1073/pnas.0407982102 / Proc. Natl. Acad. Sci. U.S.A. / Specific collapse followed by slow hydrogen-bond formation of β-sheet in the folding of single-chain monellin by Kimura (2005)
10.1039/B813961J / Phys. Chem. Chem. Phys. / Collapse transition in proteins by Ziv (2009)
10.1126/science.271.5255.1558 / Science / Protein folding triggered by electron transfer by Pascher (1996)
10.1016/S0006-3495(02)73990-8 / Biophys. J. / Focal volume optics and experimental artifacts in confocal fluorescence correlation spectroscopy by Hess (2002)
10.1006/jmbi.1993.1064 / J. Mol. Biol. / Molten globule of cytochrome c studied by small angle x-ray scattering by Kataoka (1993)
10.1073/pnas.0930122100 / Proc. Natl. Acad. Sci. U.S.A. / The molecular basis for the chemical denaturation of proteins by urea by Bennion (2003)
10.1016/S0969-2126(99)80064-1 / Structure / Structural details of urea binding to barnase: A molecular dynamics analysis by Caflisch (1999)
10.1039/b413167c / Phys. Chem. Chem. Phys. / Methane clustering in explicit water: Effect of urea on hydrophobic interactions by Oostenbrink (2005)
10.1002/(SICI)1097-0134(19980501)31:2<107::AID-PROT1>3.0.CO;2-J / Proteins / Urea effects on protein stability: Hydrogen bonding and the hydrophobic effect by Zou (1998)
10.1371/journal.pcbi.1000221 / PLoS Comput Biol. / Polar or apolar–the role of polarity for urea-induced protein denaturation by Stumpe (2008)
10.1021/ja069232+ / J. Am. Chem. Soc. / Interactions between hydrophobic and ionic solutes in aqueous guanidinium chloride and urea solutions: Lessons for protein denaturation mechanism by O'Brien (2007)
10.1073/pnas.0812588106 / Proc. Natl. Acad. Sci. U.S.A. / Urea, but not guanidinium, destabilizes proteins by forming hydrogen bonds to the peptide group by Lim (2009)
10.1006/jmbi.2000.3969 / J. Mol. Biol. / Two-state expansion and collapse of a polypeptide by Hagen (2000)
10.1021/ma00105a024 / Macromolecules / Two-stage kinetics of single-chain collapse polystyrene in cyclohexane by Chu (1995)
10.1063/1.474098 / J. Chem. Phys. / The longer time collapse kinetics of interfacial poly (N-isopropylacrylamide) in water by Zhu (1997)
10.1016/j.jmb.2007.04.061 / J. Mol. Biol. / Dissecting the non-specific and specific components of the initial folding reaction of barstar by multi-site FRET measurements by Sinha (2007)
10.1073/pnas.96.25.14258 / Proc. Natl. Acad. Sci. U.S.A. / A physical basis for protein secondary structure by Srinivasan (1999)
10.1016/S0968-0004(98)01345-0 / Trends Biochem. Sci. / Is protein folding hierarchic? II. Folding intermediates and transition states by Baldwin (1999)
10.1073/pnas.0604353104 / Proc. Natl. Acad. Sci. U.S.A. / Mapping protein collapse with single-molecule fluorescence and kinetic synchrotron radiation circular dichroism spectroscopy by Hoffmann (2007)
10.1073/pnas.0604748103 / Proc. Natl. Acad. Sci. U.S.A. / End-to-end distance distributions and intrachain diffusion constants in unfolded polypeptide chains indicate intramolecular hydrogen bond formation by Möglich (2006)
10.1073/pnas.0900622106 / Proc. Natl. Acad. Sci. U.S.A. / Single-molecule spectroscopy of the temperature-induced collapse of unfolded proteins by Nettels (2009)
10.1016/j.jmb.2005.01.009 / J. Mol. Biol. / Formation of native and non-native interactions in ensembles of denatured ACBP molecules from paramagnetic relaxation enhancement studies by Kristjansdottir (2005)
10.1021/ja0690159 / J. Am. Chem. Soc. / Highly populated turn conformations in natively unfolded Tau protein identified from residual dipolar couplings and molecular simulation by Mukrasch (2007)
10.1002/prot.23145 / Proteins / Analysis of electrostatic interactions in the denatured state ensemble of the N-terminal domain of L9 under native conditions by Meng (2011)
10.1021/bi9627626 / Biochemistry / NMR studies of unfolded states of an SH3 domain in aqueous solution and denaturing conditions by Zhang (1997)
10.1021/bi991765q / Biochemistry / Hydrodynamic radii of native and denatured proteins measured by pulse field gradient NMR techniques by Wilkins (1999)
10.1073/pnas.1001743107 / Proc. Natl. Acad. Sci. U.S.A. / From the cover: Charge interactions can dominate the dimensions of intrinsically disordered proteins by Müller-Späth (2010)

Dates

Type	When
Created	13 years, 7 months ago (Feb. 2, 2012, 8:25 p.m.)
Deposited	3 years, 8 months ago (Jan. 4, 2022, 12:04 p.m.)
Indexed	4 weeks, 2 days ago (Aug. 6, 2025, 9:14 a.m.)
Issued	13 years, 6 months ago (March 1, 2012)
Published	13 years, 6 months ago (March 1, 2012)
Published Print	13 years, 6 months ago (March 1, 2012)

Funders 0

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BibTeX

@article{Haldar_2012, title={Interconnection of Salt-induced Hydrophobic Compaction and Secondary Structure Formation Depends on Solution Conditions}, volume={287}, ISSN={0021-9258}, url={http://dx.doi.org/10.1074/jbc.m111.315648}, DOI={10.1074/jbc.m111.315648}, number={14}, journal={Journal of Biological Chemistry}, publisher={Elsevier BV}, author={Haldar, Shubhasis and Chattopadhyay, Krishnananda}, year={2012}, month=mar, pages={11546–11555} }

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      "author": "Shastry",
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      "year": "2002",
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      "author": "Takahashi",
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      "volume": "10",
      "author": "Goldbeck",
      "year": "2009",
      "journal-title": "Int. J. Mol. Sci."
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      "article-title": "The earliest events in protein folding: A structural requirement for ultrafast folding in cytochrome c",
      "volume": "126",
      "author": "Chen",
      "year": "2004",
      "journal-title": "J. Am. Chem. Soc."
    },
    {
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      "volume": "515",
      "author": "Uversky",
      "year": "2002",
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      "volume": "285",
      "author": "Haldar",
      "year": "2010",
      "journal-title": "J. Biol. Chem."
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      "author": "Ghosh",
      "year": "2009",
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    {
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      "volume": "27",
      "author": "Haldar",
      "year": "2011",
      "journal-title": "Langmuir"
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      "volume": "84",
      "author": "Sengupta",
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      "author": "Elson",
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      "volume": "103",
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      "volume": "345",
      "author": "Pletneva",
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      "author": "Segel",
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    {
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      "first-page": "245",
      "DOI": "10.1016/S0014-5793(97)00058-6",
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      "volume": "403",
      "author": "Gast",
      "year": "1997",
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    {
      "key": "10.1074/jbc.M111.315648_bib25",
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      "first-page": "12117",
      "DOI": "10.1073/pnas.2033863100",
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      "author": "Sadqi",
      "year": "2003",
      "journal-title": "Proc. Natl. Acad. Sci. U.S.A."
    },
    {
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      "doi-asserted-by": "crossref",
      "first-page": "2942",
      "DOI": "10.1021/ja808305u",
      "article-title": "Protein folding, protein collapse, and tanford's transfer model: Lessons from single-molecule FRET",
      "volume": "131",
      "author": "Ziv",
      "year": "2009",
      "journal-title": "J. Am. Chem. Soc."
    },
    {
      "key": "10.1074/jbc.M111.315648_bib27",
      "doi-asserted-by": "crossref",
      "first-page": "2748",
      "DOI": "10.1073/pnas.0407982102",
      "article-title": "Specific collapse followed by slow hydrogen-bond formation of \u03b2-sheet in the folding of single-chain monellin",
      "volume": "102",
      "author": "Kimura",
      "year": "2005",
      "journal-title": "Proc. Natl. Acad. Sci. U.S.A."
    },
    {
      "key": "10.1074/jbc.M111.315648_bib28",
      "doi-asserted-by": "crossref",
      "first-page": "83",
      "DOI": "10.1039/B813961J",
      "article-title": "Collapse transition in proteins",
      "volume": "11",
      "author": "Ziv",
      "year": "2009",
      "journal-title": "Phys. Chem. Chem. Phys."
    },
    {
      "key": "10.1074/jbc.M111.315648_bib29",
      "doi-asserted-by": "crossref",
      "first-page": "1558",
      "DOI": "10.1126/science.271.5255.1558",
      "article-title": "Protein folding triggered by electron transfer",
      "volume": "271",
      "author": "Pascher",
      "year": "1996",
      "journal-title": "Science"
    },
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      "first-page": "2300",
      "DOI": "10.1016/S0006-3495(02)73990-8",
      "article-title": "Focal volume optics and experimental artifacts in confocal fluorescence correlation spectroscopy",
      "volume": "83",
      "author": "Hess",
      "year": "2002",
      "journal-title": "Biophys. J."
    },
    {
      "key": "10.1074/jbc.M111.315648_bib31",
      "doi-asserted-by": "crossref",
      "first-page": "591",
      "DOI": "10.1006/jmbi.1993.1064",
      "article-title": "Molten globule of cytochrome c studied by small angle x-ray scattering",
      "volume": "229",
      "author": "Kataoka",
      "year": "1993",
      "journal-title": "J. Mol. Biol."
    },
    {
      "key": "10.1074/jbc.M111.315648_bib32",
      "doi-asserted-by": "crossref",
      "first-page": "5142",
      "DOI": "10.1073/pnas.0930122100",
      "article-title": "The molecular basis for the chemical denaturation of proteins by urea",
      "volume": "100",
      "author": "Bennion",
      "year": "2003",
      "journal-title": "Proc. Natl. Acad. Sci. U.S.A."
    },
    {
      "key": "10.1074/jbc.M111.315648_bib33",
      "doi-asserted-by": "crossref",
      "first-page": "477",
      "DOI": "10.1016/S0969-2126(99)80064-1",
      "article-title": "Structural details of urea binding to barnase: A molecular dynamics analysis",
      "volume": "7",
      "author": "Caflisch",
      "year": "1999",
      "journal-title": "Structure"
    },
    {
      "key": "10.1074/jbc.M111.315648_bib34",
      "doi-asserted-by": "crossref",
      "first-page": "53",
      "DOI": "10.1039/b413167c",
      "article-title": "Methane clustering in explicit water: Effect of urea on hydrophobic interactions",
      "volume": "7",
      "author": "Oostenbrink",
      "year": "2005",
      "journal-title": "Phys. Chem. Chem. Phys."
    },
    {
      "key": "10.1074/jbc.M111.315648_bib35",
      "doi-asserted-by": "crossref",
      "first-page": "107",
      "DOI": "10.1002/(SICI)1097-0134(19980501)31:2<107::AID-PROT1>3.0.CO;2-J",
      "article-title": "Urea effects on protein stability: Hydrogen bonding and the hydrophobic effect",
      "volume": "31",
      "author": "Zou",
      "year": "1998",
      "journal-title": "Proteins"
    },
    {
      "key": "10.1074/jbc.M111.315648_bib36",
      "doi-asserted-by": "crossref",
      "first-page": "e1000221",
      "DOI": "10.1371/journal.pcbi.1000221",
      "article-title": "Polar or apolar\u2013the role of polarity for urea-induced protein denaturation",
      "volume": "4",
      "author": "Stumpe",
      "year": "2008",
      "journal-title": "PLoS Comput Biol."
    },
    {
      "key": "10.1074/jbc.M111.315648_bib37",
      "doi-asserted-by": "crossref",
      "first-page": "7346",
      "DOI": "10.1021/ja069232+",
      "article-title": "Interactions between hydrophobic and ionic solutes in aqueous guanidinium chloride and urea solutions: Lessons for protein denaturation mechanism",
      "volume": "129",
      "author": "O'Brien",
      "year": "2007",
      "journal-title": "J. Am. Chem. Soc."
    },
    {
      "key": "10.1074/jbc.M111.315648_bib38",
      "doi-asserted-by": "crossref",
      "first-page": "2595",
      "DOI": "10.1073/pnas.0812588106",
      "article-title": "Urea, but not guanidinium, destabilizes proteins by forming hydrogen bonds to the peptide group",
      "volume": "106",
      "author": "Lim",
      "year": "2009",
      "journal-title": "Proc. Natl. Acad. Sci. U.S.A."
    },
    {
      "key": "10.1074/jbc.M111.315648_bib39",
      "doi-asserted-by": "crossref",
      "first-page": "1019",
      "DOI": "10.1006/jmbi.2000.3969",
      "article-title": "Two-state expansion and collapse of a polypeptide",
      "volume": "301",
      "author": "Hagen",
      "year": "2000",
      "journal-title": "J. Mol. Biol."
    },
    {
      "key": "10.1074/jbc.M111.315648_bib40",
      "doi-asserted-by": "crossref",
      "first-page": "180",
      "DOI": "10.1021/ma00105a024",
      "article-title": "Two-stage kinetics of single-chain collapse polystyrene in cyclohexane",
      "volume": "28",
      "author": "Chu",
      "year": "1995",
      "journal-title": "Macromolecules"
    },
    {
      "key": "10.1074/jbc.M111.315648_bib41",
      "doi-asserted-by": "crossref",
      "first-page": "6492",
      "DOI": "10.1063/1.474098",
      "article-title": "The longer time collapse kinetics of interfacial poly (N-isopropylacrylamide) in water",
      "volume": "106",
      "author": "Zhu",
      "year": "1997",
      "journal-title": "J. Chem. Phys."
    },
    {
      "key": "10.1074/jbc.M111.315648_bib42",
      "doi-asserted-by": "crossref",
      "first-page": "385",
      "DOI": "10.1016/j.jmb.2007.04.061",
      "article-title": "Dissecting the non-specific and specific components of the initial folding reaction of barstar by multi-site FRET measurements",
      "volume": "370",
      "author": "Sinha",
      "year": "2007",
      "journal-title": "J. Mol. Biol."
    },
    {
      "key": "10.1074/jbc.M111.315648_bib43",
      "doi-asserted-by": "crossref",
      "first-page": "14258",
      "DOI": "10.1073/pnas.96.25.14258",
      "article-title": "A physical basis for protein secondary structure",
      "volume": "96",
      "author": "Srinivasan",
      "year": "1999",
      "journal-title": "Proc. Natl. Acad. Sci. U.S.A."
    },
    {
      "key": "10.1074/jbc.M111.315648_bib44",
      "doi-asserted-by": "crossref",
      "first-page": "77",
      "DOI": "10.1016/S0968-0004(98)01345-0",
      "article-title": "Is protein folding hierarchic? II. Folding intermediates and transition states",
      "volume": "24",
      "author": "Baldwin",
      "year": "1999",
      "journal-title": "Trends Biochem. Sci."
    },
    {
      "key": "10.1074/jbc.M111.315648_bib45",
      "doi-asserted-by": "crossref",
      "first-page": "105",
      "DOI": "10.1073/pnas.0604353104",
      "article-title": "Mapping protein collapse with single-molecule fluorescence and kinetic synchrotron radiation circular dichroism spectroscopy",
      "volume": "104",
      "author": "Hoffmann",
      "year": "2007",
      "journal-title": "Proc. Natl. Acad. Sci. U.S.A."
    },
    {
      "key": "10.1074/jbc.M111.315648_bib46",
      "doi-asserted-by": "crossref",
      "first-page": "12394",
      "DOI": "10.1073/pnas.0604748103",
      "article-title": "End-to-end distance distributions and intrachain diffusion constants in unfolded polypeptide chains indicate intramolecular hydrogen bond formation",
      "volume": "103",
      "author": "M\u00f6glich",
      "year": "2006",
      "journal-title": "Proc. Natl. Acad. Sci. U.S.A."
    },
    {
      "key": "10.1074/jbc.M111.315648_bib47",
      "doi-asserted-by": "crossref",
      "first-page": "20740",
      "DOI": "10.1073/pnas.0900622106",
      "article-title": "Single-molecule spectroscopy of the temperature-induced collapse of unfolded proteins",
      "volume": "106",
      "author": "Nettels",
      "year": "2009",
      "journal-title": "Proc. Natl. Acad. Sci. U.S.A."
    },
    {
      "key": "10.1074/jbc.M111.315648_bib48",
      "doi-asserted-by": "crossref",
      "first-page": "1053",
      "DOI": "10.1016/j.jmb.2005.01.009",
      "article-title": "Formation of native and non-native interactions in ensembles of denatured ACBP molecules from paramagnetic relaxation enhancement studies",
      "volume": "347",
      "author": "Kristjansdottir",
      "year": "2005",
      "journal-title": "J. Mol. Biol."
    },
    {
      "key": "10.1074/jbc.M111.315648_bib49",
      "doi-asserted-by": "crossref",
      "first-page": "5235",
      "DOI": "10.1021/ja0690159",
      "article-title": "Highly populated turn conformations in natively unfolded Tau protein identified from residual dipolar couplings and molecular simulation",
      "volume": "129",
      "author": "Mukrasch",
      "year": "2007",
      "journal-title": "J. Am. Chem. Soc."
    },
    {
      "key": "10.1074/jbc.M111.315648_bib50",
      "doi-asserted-by": "crossref",
      "first-page": "3500",
      "DOI": "10.1002/prot.23145",
      "article-title": "Analysis of electrostatic interactions in the denatured state ensemble of the N-terminal domain of L9 under native conditions",
      "volume": "79",
      "author": "Meng",
      "year": "2011",
      "journal-title": "Proteins"
    },
    {
      "key": "10.1074/jbc.M111.315648_bib51",
      "doi-asserted-by": "crossref",
      "first-page": "3959",
      "DOI": "10.1021/bi9627626",
      "article-title": "NMR studies of unfolded states of an SH3 domain in aqueous solution and denaturing conditions",
      "volume": "36",
      "author": "Zhang",
      "year": "1997",
      "journal-title": "Biochemistry"
    },
    {
      "key": "10.1074/jbc.M111.315648_bib52",
      "doi-asserted-by": "crossref",
      "first-page": "16424",
      "DOI": "10.1021/bi991765q",
      "article-title": "Hydrodynamic radii of native and denatured proteins measured by pulse field gradient NMR techniques",
      "volume": "38",
      "author": "Wilkins",
      "year": "1999",
      "journal-title": "Biochemistry"
    },
    {
      "key": "10.1074/jbc.M111.315648_bib53",
      "doi-asserted-by": "crossref",
      "first-page": "14609",
      "DOI": "10.1073/pnas.1001743107",
      "article-title": "From the cover: Charge interactions can dominate the dimensions of intrinsically disordered proteins",
      "volume": "107",
      "author": "M\u00fcller-Sp\u00e4th",
      "year": "2010",
      "journal-title": "Proc. Natl. Acad. Sci. U.S.A."
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