DOI: 10.1006/abio.2000.4910. Determination of Macromolecular Folding and Structure by Synchrotron X-Ray Radiolysis Techniques

Determination of Macromolecular Folding and Structure by Synchrotron X-Ray Radiolysis Techniques

10.1006/abio.2000.4910

Crossref journal-article

Elsevier BV

Analytical Biochemistry (78)

Bibliography

Maleknia, S. D., Ralston, C. Y., Brenowitz, M. D., Downard, K. M., & Chance, M. R. (2001). Determination of Macromolecular Folding and Structure by Synchrotron X-Ray Radiolysis Techniques. Analytical Biochemistry, 289(2), 103â115.

Authors 5

Simin D. Maleknia (first)
Corie Y. Ralston (additional)
Michael D. Brenowitz (additional)
Kevin M. Downard (additional)
Mark R. Chance (additional)

References 69 Referenced 96

10.1038/nsb0596-397 / Nat. Struct. Biol. / Parallel worlds by Draper (1996)
{'key': '10.1006/abio.2000.4910_RF2', 'series-title': 'The RNA World', 'first-page': '239', 'article-title': 'Structure and mechanism of the large catalytic RNAs: Group I and group II introns and ribonuclease P', 'author': 'Cech', 'year': '1993'} / The RNA World / Structure and mechanism of the large catalytic RNAs: Group I and group II introns and ribonuclease P by Cech (1993)
10.1161/01.RES.83.2.117 / Circ. Res. / Stress (heat shock) proteins: Molecular chaperones in cardiovascular biology and disease by Benjamin (1998)
10.1016/S0959-440X(98)80016-X / Curr. Opin. Struct. Biol. / The alternative conformations of amyloidogenic proteins and their multi-step assembly pathways by Kelly (1998)
10.1016/S0968-0004(00)89100-8 / Trends Biochem Sci. / Defective protein folding as a basis of human disease by Thomas (1995)
10.1016/S0959-440X(99)00049-4 / Curr. Opin. Struct. Biol. / Amyloid fibrillogenesis: Themes and variations by Rochet (2000)
10.1006/jmbi.1999.2990 / J. Mol. Biol. / Protein misfolding and prion diseases by Cohen (1999)
10.1016/S0140-6736(99)11419-3 / Lancet / Reversion of prion protein conformational changes by synthetic beta-sheet breaker peptides by Soto (2000)
{'key': '10.1006/abio.2000.4910_RF9', 'first-page': '122', 'article-title': 'Protein folding mechanisms: New methods and emerging ideas', 'volume': '9', 'author': 'Brockwell', 'year': '1999', 'journal-title': 'Curr. Opin. Struct. Biol.'} / Curr. Opin. Struct. Biol. / Protein folding mechanisms: New methods and emerging ideas by Brockwell (1999)
10.1016/0076-6879(86)31035-8 / Methods Enzymol. / Fast-folding and slow-folding forms of unfolded proteins by Schmid (1986)
10.1016/0076-6879(86)31038-3 / Methods Enzymol. / Folding intermediates studied by circular dichroism by Labhardt (1986)
10.1146/annurev.physchem.49.1.173 / Annu. Rev. Phys. Chem. / Fast events in protein folding: The time evolution of primary processes by Callender (1998)
10.1073/pnas.93.12.5759 / Proc. Natl. Acad. Sci. USA / Direct observation of fast protein folding: The initial collapse of apomyoglobin by Ballew (1996)
10.1021/bi00231a001 / Biochemistry / Probing the stability of a partly folded apomyoglobin intermediate by site-directed mutagenesis by Hughson (1991)
10.1021/bi971161r / Biochemistry / UV resonance Raman determination of protein acid denaturation: Selective unfolding of helical segments of horse myoglobin by Chi (1998)
10.1038/nsb0398-222 / Nat. Struct. Biol. / Folding intermediates in cytochrome c by Yeh (1998)
10.1074/jbc.274.43.30357 / J. Biol. Chem. / UV resonance Raman spectra of ligand binding intermediates of sol-gel encapsulated hemoglobin by Juszczak (1999)
10.1038/13311 / Nat. Struct. Biol. / Folding dynamics of the B1 domain of protein G explored by ultrarapid mixing by Park (1999)
10.1126/science.283.5408.1676 / Science / Fluorescence spectroscopy of single biomolecules by Weiss (1999)
10.1126/science.8235610 / Science / Formation of a molten globule intermediate early in the kinetic folding pathway of apomyoglobin by Jennings (1993)
10.1002/prot.340200103 / Proteins / Protein stability parameters measured by hydrogen exchange by Bai (1994)
10.1002/pro.5560020404 / Protein Sci. / Determination of amide hydrogen exchange by mass spectrometry: A new tool for protein structure elucidation by Zhang (1993)
10.1021/bi991609j / Biochemistry / Antigenic surveillance of the influenza virus by mass spectrometry by Kiselar (1999)
10.1021/ac991081o / Anal. Chem. / A generic strategy to analyze the spatial organization of multi-protein complexes by cross-linking and mass spectrometry by Rappsilber (2000)
10.1038/12277 / Nat. Struct. Biol. / Confirmation of the hierarchical folding of RNase H: A protein engineering study by Raschkle (1999)
10.1126/science.7618079 / Science / Protein folding intermediates: Native-state hydrogen exchange by Bai (1995)
10.1073/pnas.96.5.2007 / Proc. Natl. Acad. Sci USA / Specificity of native-like interhelical hydrophobic contacts in the apomyoglobin intermediate by Kay (1999)
10.1016/S0959-440X(99)00011-1 / Curr. Opin. Struct. Biol. / NMR spectroscopy of large molecules and multimolecular assemblies in solution by Wider (1999)
10.1006/jmbi.1996.0775 / J. Mol. Biol. / Time-resolved synchrotron X-ray “Footprinting,” a new approach to the study of nucleic acid structure and function: Application to protein–DNA interactions and RNA folding by Sclavi (1997)
10.1016/S0969-2126(97)00241-4 / Structure / Examining the conformational dynamics of macromolecules with time-resolved synchrotron X-ray “footprinting.” by Chance (1997)
10.1126/science.279.5358.1940 / Science / RNA folding at millisecond intervals by synchrotron hydroxyl radical footprinting by Sclavi (1998)
10.1016/S0076-6879(98)95050-9 / Methods Enzymol. / Following the folding of RNA with time-resolved synchrotron X-ray footprinting by Sclavi (1998)
10.1080/08940889808260960 / Synchrotron Radiat. News by Chance (1998)
10.1016/0076-6879(86)30011-9 / Methods Enzymol. / Quantitative DNase footprint titration: A method for studying protein–DNA interactions by Brenowitz (1986)
10.1073/pnas.83.22.8462 / Proc. Natl. Acad. Sci. USA by Brenowitz (1986)
10.1016/S0076-6879(96)74038-7 / Methods Enzymol. / Quantitative kinetics footprinting of protein–DNA association reactions by Hsieh (1996)
10.1021/bi00031a020 / Biochemistry / Thermodynamic and kinetic characterization of the binding of the TATA binding protein to the adenovirus E4 promoter by Petri (1995)
10.1016/0076-6879(92)10021-5 / Methods Enzymol. / Analysis of site-specific interaction parameters in protein–DNA complexes by Koblan (1992)
10.1126/science.2501870 / Science / Defining the inside and outside of a catalytic RNA molecule by Latham (1989)
10.1093/nar/5.9.3157 / Nucleic Acids Res. / DNase footprinting: A simple method for the detection of protein–DNA binding specificity by Galas (1978)
10.1016/0076-6879(87)55035-2 / Methods Enzymol. / Hydroxyl radical footprinting: A high-resolution method for mapping protein–DNA contacts by Tullius (1987)
10.1021/ja00039a068 / J. Am. Chem. Soc. / A stable solid that generates hydroxyl radical upon dissolution in aqueous solutions: Reaction with proteins and nucleic acid by King (1992)
10.1021/cr00078a006 / Chem. Rev. / Reaction mechanisms in the radiolysis of peptides, polypeptides, and proteins by Garrison (1987)
10.1016/S0021-9258(18)33827-4 / J. Biol. Chem. / Sites and structure of γ radiation-induced DNA strand breaks by Henner (1982)
10.1021/bi00059a031 / Biochemistry / Radiolytic footprinting, β rays, γ photons, and fast neutrons probe DNA–protein interactions by Franchet-Beuzit (1993)
10.1016/0076-6879(90)86148-O / Methods Enzymol. / Footprinting protein–DNA complexes with gamma-rays by Hayes (1990)
10.1021/ac990500e / Anal. Chem. / Millisecond radiolytic modification of peptides by synchrotron X-rays identified by mass spectrometry by Maleknia (1999)
{'key': '10.1006/abio.2000.4910_RF48', 'first-page': '214A', 'article-title': 'Synchrotron X-ray footprinting of protein antigens and their complexes', 'volume': '78', 'author': 'Maleknia', 'year': '2000', 'journal-title': 'Biophys. J.'} / Biophys. J. / Synchrotron X-ray footprinting of protein antigens and their complexes by Maleknia (2000)
{'key': '10.1006/abio.2000.4910_RF49', 'series-title': 'Radiation Chemistry: Principles and Applications', 'first-page': '29', 'article-title': 'Primary products in radiation chemistry', 'author': 'Klassen', 'year': '1987'} / Radiation Chemistry: Principles and Applications / Primary products in radiation chemistry by Klassen (1987)
10.1016/S0076-6879(00)17024-7 / Methods Enzymol. / Time-resolved synchrotron X-ray footprinting and its application to RNA folding by Ralston (2000)
10.1073/pnas.95.17.9738 / Proc. Natl. Acad. Sci. USA / DNA strand breaking by the hydroxyl radical is governed by the accessible surface areas of the hydrogen atoms of the DNA backbone by Balasubramanian (1998)
{'key': '10.1006/abio.2000.4910_RF52', 'series-title': 'Radiation Chemistry: Principles and Applications', 'first-page': '477', 'article-title': 'Radiation chemistry of biopolymers', 'author': 'Mee', 'year': '1987'} / Radiation Chemistry: Principles and Applications / Radiation chemistry of biopolymers by Mee (1987)
10.1073/pnas.89.14.6383 / Proc. Natl. Acad. Sci. USA / Conformation-dependent cleavage of staphylococcal nuclease with a disulfide-linked iron chelate by Ermacora (1992)
10.1021/bi00198a033 / Biochemistry / Mapping protein domains involved in macromolecular interactions: A novel protein footprinting approach by Heyduk (1994)
10.1021/ac00280a023 / Anal. Chem. / Electrospray interface for liquid chromatographs and mass spectrometers by Whitehouse (1985)
10.1006/jmbi.1993.1097 / J. Mol. Biol. / Structure of hen lysozyme in solution by Smith (1993)
10.1016/0022-2836(74)90570-1 / J. Mol. Biol. / Area, volumes, packing, and protein structure by Richards (1974)
10.1016/0022-2836(84)90231-6 / J. Mol. Biol. / The interpretation of protein structures: Total volume, group volume distributions and packing density by Richmond (1984)
{'key': '10.1006/abio.2000.4910_RF59', 'first-page': '251A', 'article-title': 'Synchrotron X-ray footprinting reveals unfolding of apomyoglobin helices', 'volume': '78', 'author': 'Maleknia', 'year': '2000', 'journal-title': 'Biophys. J.'} / Biophys. J. / Synchrotron X-ray footprinting reveals unfolding of apomyoglobin helices by Maleknia (2000)
Maleknia, S. D, Downard, K. M, and, Chance, M. R. 2000, Submitted.
10.1016/0076-6879(86)31045-0 / Methods Enzymol. / Determination and analysis of urea and guanidine hydrochloride denaturation curves by Pace (1986)
10.1021/bi00421a014 / Biochemistry / Unfolding free energy changes determined by the linear extrapolation method. 1. Unfolding of phenylmethanesulfonyl alpha-chymotrypsin using different denaturants by Santoro (1988)
10.1021/bi00421a015 / Biochemistry / Unfolding free energy changes determined by the linear extrapolation method. 2. Incorporation of delta G degrees N-U values in a thermodynamic cycle by Bolen (1998)
10.1006/jmbi.1995.0479 / J. Mol. Biol. / Intrinsic stability of individual a helices modulates structure and stability of the apomyoglobin molten globule form by Kiefhaber (1995)
10.1038/75139 / Nat. Struct. Biol. / Stability and cooperativity of individual tertiary contacts in RNA revealed through chemical denaturation by Ralston (2000)
10.1038/nsb1197-931 / Nat. Struct. Biol. / Intermediates and kinetic traps in the folding of a large ribozyme revealed by circular dichroism and UV absorbance spectroscopies and catalytic activity by Pan (1997)
10.1080/07391102.2000.10506621 / J. Biomol. Struct. Dyn. / The early folding intermediates of the Tetrahymena ribozyme are kinetically trapped by Ralston (2000)
10.1126/science.279.5358.1943 / Science / Kinetic intermediates trapped by native interactions in RNA folding by Treiber (1998)
10.1006/jmbi.1998.1960 / J. Mol. Biol. / Fast folding mutants of the Tetrahymena group I ribozyme reveal a rugged folding energy landscape by Rook (1998)

Dates

Type	When
Created	22 years, 3 months ago (May 19, 2003, 12:51 p.m.)
Deposited	4 years, 4 months ago (May 3, 2021, 1:03 a.m.)
Indexed	1 year, 1 month ago (July 24, 2024, 6:34 p.m.)
Issued	24 years, 7 months ago (Feb. 1, 2001)
Published	24 years, 7 months ago (Feb. 1, 2001)
Published Print	24 years, 7 months ago (Feb. 1, 2001)

Funders 0

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BibTeX

@article{Maleknia_2001, title={Determination of Macromolecular Folding and Structure by Synchrotron X-Ray Radiolysis Techniques}, volume={289}, ISSN={0003-2697}, url={http://dx.doi.org/10.1006/abio.2000.4910}, DOI={10.1006/abio.2000.4910}, number={2}, journal={Analytical Biochemistry}, publisher={Elsevier BV}, author={Maleknia, Simin D. and Ralston, Corie Y. and Brenowitz, Michael D. and Downard, Kevin M. and Chance, Mark R.}, year={2001}, month=feb, pages={103–115} }

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      "first-page": "239",
      "article-title": "Structure and mechanism of the large catalytic RNAs: Group I and group II introns and ribonuclease P",
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      "article-title": "Stress (heat shock) proteins: Molecular chaperones in cardiovascular biology and disease",
      "volume": "83",
      "author": "Benjamin",
      "year": "1998",
      "journal-title": "Circ. Res."
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    {
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      "article-title": "The alternative conformations of amyloidogenic proteins and their multi-step assembly pathways",
      "volume": "8",
      "author": "Kelly",
      "year": "1998",
      "journal-title": "Curr. Opin. Struct. Biol."
    },
    {
      "key": "10.1006/abio.2000.4910_RF5",
      "doi-asserted-by": "crossref",
      "first-page": "456",
      "DOI": "10.1016/S0968-0004(00)89100-8",
      "article-title": "Defective protein folding as a basis of human disease",
      "volume": "20",
      "author": "Thomas",
      "year": "1995",
      "journal-title": "Trends Biochem Sci."
    },
    {
      "key": "10.1006/abio.2000.4910_RF6",
      "doi-asserted-by": "crossref",
      "first-page": "60",
      "DOI": "10.1016/S0959-440X(99)00049-4",
      "article-title": "Amyloid fibrillogenesis: Themes and variations",
      "volume": "10",
      "author": "Rochet",
      "year": "2000",
      "journal-title": "Curr. Opin. Struct. Biol."
    },
    {
      "key": "10.1006/abio.2000.4910_RF7",
      "doi-asserted-by": "crossref",
      "first-page": "313",
      "DOI": "10.1006/jmbi.1999.2990",
      "article-title": "Protein misfolding and prion diseases",
      "volume": "293",
      "author": "Cohen",
      "year": "1999",
      "journal-title": "J. Mol. Biol."
    },
    {
      "key": "10.1006/abio.2000.4910_RF8",
      "doi-asserted-by": "crossref",
      "first-page": "192",
      "DOI": "10.1016/S0140-6736(99)11419-3",
      "article-title": "Reversion of prion protein conformational changes by synthetic beta-sheet breaker peptides",
      "volume": "355",
      "author": "Soto",
      "year": "2000",
      "journal-title": "Lancet"
    },
    {
      "key": "10.1006/abio.2000.4910_RF9",
      "first-page": "122",
      "article-title": "Protein folding mechanisms: New methods and emerging ideas",
      "volume": "9",
      "author": "Brockwell",
      "year": "1999",
      "journal-title": "Curr. Opin. Struct. Biol."
    },
    {
      "key": "10.1006/abio.2000.4910_RF10",
      "doi-asserted-by": "crossref",
      "first-page": "70",
      "DOI": "10.1016/0076-6879(86)31035-8",
      "article-title": "Fast-folding and slow-folding forms of unfolded proteins",
      "volume": "131",
      "author": "Schmid",
      "year": "1986",
      "journal-title": "Methods Enzymol."
    },
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      "doi-asserted-by": "crossref",
      "first-page": "126",
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      "volume": "131",
      "author": "Labhardt",
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      "volume": "93",
      "author": "Ballew",
      "year": "1996",
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      "volume": "30",
      "author": "Hughson",
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      "journal-title": "Biochemistry"
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      "author": "Chi",
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      "volume": "274",
      "author": "Juszczak",
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      "volume": "283",
      "author": "Weiss",
      "year": "1999",
      "journal-title": "Science"
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      "first-page": "892",
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      "volume": "262",
      "author": "Jennings",
      "year": "1993",
      "journal-title": "Science"
    },
    {
      "key": "10.1006/abio.2000.4910_RF21",
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      "first-page": "4",
      "DOI": "10.1002/prot.340200103",
      "article-title": "Protein stability parameters measured by hydrogen exchange",
      "volume": "20",
      "author": "Bai",
      "year": "1994",
      "journal-title": "Proteins"
    },
    {
      "key": "10.1006/abio.2000.4910_RF22",
      "doi-asserted-by": "crossref",
      "first-page": "522",
      "DOI": "10.1002/pro.5560020404",
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      "volume": "2",
      "author": "Zhang",
      "year": "1993",
      "journal-title": "Protein Sci."
    },
    {
      "key": "10.1006/abio.2000.4910_RF23",
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      "first-page": "14185",
      "DOI": "10.1021/bi991609j",
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      "volume": "38",
      "author": "Kiselar",
      "year": "1999",
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      "volume": "72",
      "author": "Rappsilber",
      "year": "2000",
      "journal-title": "Anal. Chem."
    },
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      "key": "10.1006/abio.2000.4910_RF25",
      "doi-asserted-by": "crossref",
      "first-page": "825",
      "DOI": "10.1038/12277",
      "article-title": "Confirmation of the hierarchical folding of RNase H: A protein engineering study",
      "volume": "6",
      "author": "Raschkle",
      "year": "1999",
      "journal-title": "Nat. Struct. Biol."
    },
    {
      "key": "10.1006/abio.2000.4910_RF26",
      "doi-asserted-by": "crossref",
      "first-page": "192",
      "DOI": "10.1126/science.7618079",
      "article-title": "Protein folding intermediates: Native-state hydrogen exchange",
      "volume": "269",
      "author": "Bai",
      "year": "1995",
      "journal-title": "Science"
    },
    {
      "key": "10.1006/abio.2000.4910_RF27",
      "doi-asserted-by": "crossref",
      "first-page": "2007",
      "DOI": "10.1073/pnas.96.5.2007",
      "article-title": "Specificity of native-like interhelical hydrophobic contacts in the apomyoglobin intermediate",
      "volume": "96",
      "author": "Kay",
      "year": "1999",
      "journal-title": "Proc. Natl. Acad. Sci USA"
    },
    {
      "key": "10.1006/abio.2000.4910_RF28",
      "doi-asserted-by": "crossref",
      "first-page": "594",
      "DOI": "10.1016/S0959-440X(99)00011-1",
      "article-title": "NMR spectroscopy of large molecules and multimolecular assemblies in solution",
      "volume": "9",
      "author": "Wider",
      "year": "1999",
      "journal-title": "Curr. Opin. Struct. Biol."
    },
    {
      "key": "10.1006/abio.2000.4910_RF29",
      "doi-asserted-by": "crossref",
      "first-page": "144",
      "DOI": "10.1006/jmbi.1996.0775",
      "article-title": "Time-resolved synchrotron X-ray \u201cFootprinting,\u201d a new approach to the study of nucleic acid structure and function: Application to protein\u2013DNA interactions and RNA folding",
      "volume": "266",
      "author": "Sclavi",
      "year": "1997",
      "journal-title": "J. Mol. Biol."
    },
    {
      "key": "10.1006/abio.2000.4910_RF30",
      "doi-asserted-by": "crossref",
      "first-page": "865",
      "DOI": "10.1016/S0969-2126(97)00241-4",
      "article-title": "Examining the conformational dynamics of macromolecules with time-resolved synchrotron X-ray \u201cfootprinting.\u201d",
      "volume": "5",
      "author": "Chance",
      "year": "1997",
      "journal-title": "Structure"
    },
    {
      "key": "10.1006/abio.2000.4910_RF31",
      "doi-asserted-by": "crossref",
      "first-page": "1940",
      "DOI": "10.1126/science.279.5358.1940",
      "article-title": "RNA folding at millisecond intervals by synchrotron hydroxyl radical footprinting",
      "volume": "279",
      "author": "Sclavi",
      "year": "1998",
      "journal-title": "Science"
    },
    {
      "key": "10.1006/abio.2000.4910_RF32",
      "doi-asserted-by": "crossref",
      "first-page": "379",
      "DOI": "10.1016/S0076-6879(98)95050-9",
      "article-title": "Following the folding of RNA with time-resolved synchrotron X-ray footprinting",
      "volume": "295",
      "author": "Sclavi",
      "year": "1998",
      "journal-title": "Methods Enzymol."
    },
    {
      "key": "10.1006/abio.2000.4910_RF33",
      "doi-asserted-by": "crossref",
      "first-page": "7",
      "DOI": "10.1080/08940889808260960",
      "volume": "11",
      "author": "Chance",
      "year": "1998",
      "journal-title": "Synchrotron Radiat. News"
    },
    {
      "key": "10.1006/abio.2000.4910_RF34",
      "doi-asserted-by": "crossref",
      "first-page": "132",
      "DOI": "10.1016/0076-6879(86)30011-9",
      "article-title": "Quantitative DNase footprint titration: A method for studying protein\u2013DNA interactions",
      "volume": "130",
      "author": "Brenowitz",
      "year": "1986",
      "journal-title": "Methods Enzymol."
    },
    {
      "key": "10.1006/abio.2000.4910_RF35",
      "doi-asserted-by": "crossref",
      "first-page": "8462",
      "DOI": "10.1073/pnas.83.22.8462",
      "volume": "83",
      "author": "Brenowitz",
      "year": "1986",
      "journal-title": "Proc. Natl. Acad. Sci. USA"
    },
    {
      "key": "10.1006/abio.2000.4910_RF36",
      "doi-asserted-by": "crossref",
      "first-page": "478",
      "DOI": "10.1016/S0076-6879(96)74038-7",
      "article-title": "Quantitative kinetics footprinting of protein\u2013DNA association reactions",
      "volume": "274",
      "author": "Hsieh",
      "year": "1996",
      "journal-title": "Methods Enzymol."
    },
    {
      "key": "10.1006/abio.2000.4910_RF37",
      "doi-asserted-by": "crossref",
      "first-page": "9977",
      "DOI": "10.1021/bi00031a020",
      "article-title": "Thermodynamic and kinetic characterization of the binding of the TATA binding protein to the adenovirus E4 promoter",
      "volume": "34",
      "author": "Petri",
      "year": "1995",
      "journal-title": "Biochemistry"
    },
    {
      "key": "10.1006/abio.2000.4910_RF38",
      "doi-asserted-by": "crossref",
      "first-page": "405",
      "DOI": "10.1016/0076-6879(92)10021-5",
      "article-title": "Analysis of site-specific interaction parameters in protein\u2013DNA complexes",
      "volume": "210",
      "author": "Koblan",
      "year": "1992",
      "journal-title": "Methods Enzymol."
    },
    {
      "key": "10.1006/abio.2000.4910_RF39",
      "doi-asserted-by": "crossref",
      "first-page": "276",
      "DOI": "10.1126/science.2501870",
      "article-title": "Defining the inside and outside of a catalytic RNA molecule",
      "volume": "245",
      "author": "Latham",
      "year": "1989",
      "journal-title": "Science"
    },
    {
      "key": "10.1006/abio.2000.4910_RF40",
      "doi-asserted-by": "crossref",
      "first-page": "3157",
      "DOI": "10.1093/nar/5.9.3157",
      "article-title": "DNase footprinting: A simple method for the detection of protein\u2013DNA binding specificity",
      "volume": "5",
      "author": "Galas",
      "year": "1978",
      "journal-title": "Nucleic Acids Res."
    },
    {
      "key": "10.1006/abio.2000.4910_RF41",
      "doi-asserted-by": "crossref",
      "first-page": "537",
      "DOI": "10.1016/0076-6879(87)55035-2",
      "article-title": "Hydroxyl radical footprinting: A high-resolution method for mapping protein\u2013DNA contacts",
      "volume": "155",
      "author": "Tullius",
      "year": "1987",
      "journal-title": "Methods Enzymol."
    },
    {
      "key": "10.1006/abio.2000.4910_RF42",
      "doi-asserted-by": "crossref",
      "first-page": "5430",
      "DOI": "10.1021/ja00039a068",
      "article-title": "A stable solid that generates hydroxyl radical upon dissolution in aqueous solutions: Reaction with proteins and nucleic acid",
      "volume": "114",
      "author": "King",
      "year": "1992",
      "journal-title": "J. Am. Chem. Soc."
    },
    {
      "key": "10.1006/abio.2000.4910_RF43",
      "doi-asserted-by": "crossref",
      "first-page": "381",
      "DOI": "10.1021/cr00078a006",
      "article-title": "Reaction mechanisms in the radiolysis of peptides, polypeptides, and proteins",
      "volume": "87",
      "author": "Garrison",
      "year": "1987",
      "journal-title": "Chem. Rev."
    },
    {
      "key": "10.1006/abio.2000.4910_RF44",
      "doi-asserted-by": "crossref",
      "first-page": "11750",
      "DOI": "10.1016/S0021-9258(18)33827-4",
      "article-title": "Sites and structure of \u03b3 radiation-induced DNA strand breaks",
      "volume": "257",
      "author": "Henner",
      "year": "1982",
      "journal-title": "J. Biol. Chem."
    },
    {
      "key": "10.1006/abio.2000.4910_RF45",
      "doi-asserted-by": "crossref",
      "first-page": "2104",
      "DOI": "10.1021/bi00059a031",
      "article-title": "Radiolytic footprinting, \u03b2 rays, \u03b3 photons, and fast neutrons probe DNA\u2013protein interactions",
      "volume": "32",
      "author": "Franchet-Beuzit",
      "year": "1993",
      "journal-title": "Biochemistry"
    },
    {
      "key": "10.1006/abio.2000.4910_RF46",
      "doi-asserted-by": "crossref",
      "first-page": "545",
      "DOI": "10.1016/0076-6879(90)86148-O",
      "article-title": "Footprinting protein\u2013DNA complexes with gamma-rays",
      "volume": "186",
      "author": "Hayes",
      "year": "1990",
      "journal-title": "Methods Enzymol."
    },
    {
      "key": "10.1006/abio.2000.4910_RF47",
      "doi-asserted-by": "crossref",
      "first-page": "3965",
      "DOI": "10.1021/ac990500e",
      "article-title": "Millisecond radiolytic modification of peptides by synchrotron X-rays identified by mass spectrometry",
      "volume": "71",
      "author": "Maleknia",
      "year": "1999",
      "journal-title": "Anal. Chem."
    },
    {
      "key": "10.1006/abio.2000.4910_RF48",
      "first-page": "214A",
      "article-title": "Synchrotron X-ray footprinting of protein antigens and their complexes",
      "volume": "78",
      "author": "Maleknia",
      "year": "2000",
      "journal-title": "Biophys. J."
    },
    {
      "key": "10.1006/abio.2000.4910_RF49",
      "series-title": "Radiation Chemistry: Principles and Applications",
      "first-page": "29",
      "article-title": "Primary products in radiation chemistry",
      "author": "Klassen",
      "year": "1987"
    },
    {
      "key": "10.1006/abio.2000.4910_RF50",
      "doi-asserted-by": "crossref",
      "first-page": "353",
      "DOI": "10.1016/S0076-6879(00)17024-7",
      "article-title": "Time-resolved synchrotron X-ray footprinting and its application to RNA folding",
      "volume": "317",
      "author": "Ralston",
      "year": "2000",
      "journal-title": "Methods Enzymol."
    },
    {
      "key": "10.1006/abio.2000.4910_RF51",
      "doi-asserted-by": "crossref",
      "first-page": "9738",
      "DOI": "10.1073/pnas.95.17.9738",
      "article-title": "DNA strand breaking by the hydroxyl radical is governed by the accessible surface areas of the hydrogen atoms of the DNA backbone",
      "volume": "95",
      "author": "Balasubramanian",
      "year": "1998",
      "journal-title": "Proc. Natl. Acad. Sci. USA"
    },
    {
      "key": "10.1006/abio.2000.4910_RF52",
      "series-title": "Radiation Chemistry: Principles and Applications",
      "first-page": "477",
      "article-title": "Radiation chemistry of biopolymers",
      "author": "Mee",
      "year": "1987"
    },
    {
      "key": "10.1006/abio.2000.4910_RF53",
      "doi-asserted-by": "crossref",
      "first-page": "6383",
      "DOI": "10.1073/pnas.89.14.6383",
      "article-title": "Conformation-dependent cleavage of staphylococcal nuclease with a disulfide-linked iron chelate",
      "volume": "89",
      "author": "Ermacora",
      "year": "1992",
      "journal-title": "Proc. Natl. Acad. Sci. USA"
    },
    {
      "key": "10.1006/abio.2000.4910_RF54",
      "doi-asserted-by": "crossref",
      "first-page": "9643",
      "DOI": "10.1021/bi00198a033",
      "article-title": "Mapping protein domains involved in macromolecular interactions: A novel protein footprinting approach",
      "volume": "33",
      "author": "Heyduk",
      "year": "1994",
      "journal-title": "Biochemistry"
    },
    {
      "key": "10.1006/abio.2000.4910_RF55",
      "doi-asserted-by": "crossref",
      "first-page": "675",
      "DOI": "10.1021/ac00280a023",
      "article-title": "Electrospray interface for liquid chromatographs and mass spectrometers",
      "volume": "57",
      "author": "Whitehouse",
      "year": "1985",
      "journal-title": "Anal. Chem."
    },
    {
      "key": "10.1006/abio.2000.4910_RF56",
      "doi-asserted-by": "crossref",
      "first-page": "930",
      "DOI": "10.1006/jmbi.1993.1097",
      "article-title": "Structure of hen lysozyme in solution",
      "volume": "229",
      "author": "Smith",
      "year": "1993",
      "journal-title": "J. Mol. Biol."
    },
    {
      "key": "10.1006/abio.2000.4910_RF57",
      "doi-asserted-by": "crossref",
      "first-page": "1",
      "DOI": "10.1016/0022-2836(74)90570-1",
      "article-title": "Area, volumes, packing, and protein structure",
      "volume": "82",
      "author": "Richards",
      "year": "1974",
      "journal-title": "J. Mol. Biol."
    },
    {
      "key": "10.1006/abio.2000.4910_RF58",
      "doi-asserted-by": "crossref",
      "first-page": "63",
      "DOI": "10.1016/0022-2836(84)90231-6",
      "article-title": "The interpretation of protein structures: Total volume, group volume distributions and packing density",
      "volume": "178",
      "author": "Richmond",
      "year": "1984",
      "journal-title": "J. Mol. Biol."
    },
    {
      "key": "10.1006/abio.2000.4910_RF59",
      "first-page": "251A",
      "article-title": "Synchrotron X-ray footprinting reveals unfolding of apomyoglobin helices",
      "volume": "78",
      "author": "Maleknia",
      "year": "2000",
      "journal-title": "Biophys. J."
    },
    {
      "key": "10.1006/abio.2000.4910_RF60",
      "unstructured": "Maleknia, S. D, Downard, K. M, and, Chance, M. R. 2000, Submitted."
    },
    {
      "key": "10.1006/abio.2000.4910_RF61",
      "doi-asserted-by": "crossref",
      "first-page": "266",
      "DOI": "10.1016/0076-6879(86)31045-0",
      "article-title": "Determination and analysis of urea and guanidine hydrochloride denaturation curves",
      "volume": "131",
      "author": "Pace",
      "year": "1986",
      "journal-title": "Methods Enzymol."
    },
    {
      "key": "10.1006/abio.2000.4910_RF62",
      "doi-asserted-by": "crossref",
      "first-page": "8063",
      "DOI": "10.1021/bi00421a014",
      "article-title": "Unfolding free energy changes determined by the linear extrapolation method. 1. Unfolding of phenylmethanesulfonyl alpha-chymotrypsin using different denaturants",
      "volume": "27",
      "author": "Santoro",
      "year": "1988",
      "journal-title": "Biochemistry"
    },
    {
      "key": "10.1006/abio.2000.4910_RF63",
      "doi-asserted-by": "crossref",
      "first-page": "8069",
      "DOI": "10.1021/bi00421a015",
      "article-title": "Unfolding free energy changes determined by the linear extrapolation method. 2. Incorporation of delta G degrees N-U values in a thermodynamic cycle",
      "volume": "27",
      "author": "Bolen",
      "year": "1998",
      "journal-title": "Biochemistry"
    },
    {
      "key": "10.1006/abio.2000.4910_RF64",
      "doi-asserted-by": "crossref",
      "first-page": "122",
      "DOI": "10.1006/jmbi.1995.0479",
      "article-title": "Intrinsic stability of individual a helices modulates structure and stability of the apomyoglobin molten globule form",
      "volume": "252",
      "author": "Kiefhaber",
      "year": "1995",
      "journal-title": "J. Mol. Biol."
    },
    {
      "key": "10.1006/abio.2000.4910_RF65",
      "doi-asserted-by": "crossref",
      "first-page": "371",
      "DOI": "10.1038/75139",
      "article-title": "Stability and cooperativity of individual tertiary contacts in RNA revealed through chemical denaturation",
      "volume": "7",
      "author": "Ralston",
      "year": "2000",
      "journal-title": "Nat. Struct. Biol."
    },
    {
      "key": "10.1006/abio.2000.4910_RF66",
      "doi-asserted-by": "crossref",
      "first-page": "931",
      "DOI": "10.1038/nsb1197-931",
      "article-title": "Intermediates and kinetic traps in the folding of a large ribozyme revealed by circular dichroism and UV absorbance spectroscopies and catalytic activity",
      "volume": "4",
      "author": "Pan",
      "year": "1997",
      "journal-title": "Nat. Struct. Biol."
    },
    {
      "key": "10.1006/abio.2000.4910_RF67",
      "doi-asserted-by": "crossref",
      "first-page": "195",
      "DOI": "10.1080/07391102.2000.10506621",
      "article-title": "The early folding intermediates of the Tetrahymena ribozyme are kinetically trapped",
      "volume": "2",
      "author": "Ralston",
      "year": "2000",
      "journal-title": "J. Biomol. Struct. Dyn."
    },
    {
      "key": "10.1006/abio.2000.4910_RF68",
      "doi-asserted-by": "crossref",
      "first-page": "1943",
      "DOI": "10.1126/science.279.5358.1943",
      "article-title": "Kinetic intermediates trapped by native interactions in RNA folding",
      "volume": "279",
      "author": "Treiber",
      "year": "1998",
      "journal-title": "Science"
    },
    {
      "key": "10.1006/abio.2000.4910_RF69",
      "doi-asserted-by": "crossref",
      "first-page": "609",
      "DOI": "10.1006/jmbi.1998.1960",
      "article-title": "Fast folding mutants of the Tetrahymena group I ribozyme reveal a rugged folding energy landscape",
      "volume": "281",
      "author": "Rook",
      "year": "1998",
      "journal-title": "J. Mol. Biol."
    }
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