DOI: 10.1006/jmbi.1996.0797. Crystal structures of Escherichia coli and Salmonella typhimurium 3-isopropylmalate dehydrogenase and comparison with their thermophilic counterpart from Thermus thermophilus

Crystal structures of Escherichia coli and Salmonella typhimurium 3-isopropylmalate dehydrogenase and comparison with their thermophilic counterpart from Thermus thermophilus

10.1006/jmbi.1996.0797

Crossref journal-article

Elsevier BV

Journal of Molecular Biology (78)

Bibliography

Wallon, G., Kryger, G., Lovett, S. T., Oshima, T., Ringe, D., & Petsko, G. A. (1997). Crystal structures of Escherichia coli and Salmonella typhimurium 3-isopropylmalate dehydrogenase and comparison with their thermophilic counterpart from Thermus thermophilus. Journal of Molecular Biology, 266(5), 1016â1031.

Authors 6

Gerlind Wallon (first)
Gitay Kryger (additional)
Susan T Lovett (additional)
Tairo Oshima (additional)
Dagmar Ringe (additional)
Gregory A Petsko (additional)

References 54 Referenced 121

10.1002/prot.340080106 / Proteins: Struct. Funct. Genet / Protein stability and electrostatic interactions between solvent exposed charged side chains by Akke (1990)
10.1016/S0022-2836(83)80079-5 / J. Mol. Biol / Ion-pairs in proteins by Barlow (1983)
10.1126/science.7761851 / Science / Mutagenesis and Laue structures of enzyme intermeidates by Bolduc (1995)
{'key': '10.1006/jmbi.1996.0797_BIB4', 'first-page': '267', 'article-title': 'The free R.-value', 'volume': '249', 'author': 'Brüenger', 'year': '1992', 'journal-title': 'Nature'} / Nature / The free R.-value by Brüenger (1992)
10.1126/science.235.4787.458 / Sciences / Crystallographic R.-factor refinement by molecular dynamics by Brüenger (1987)
10.1126/science.3892686 / Science / Aromatic-aromatic interaction by Burley (1985)
10.1006/jmbi.1993.1414 / J. Mol. Biol / Protein unfolding pathways explored through molecular dynamics simulations by Daggett (1993)
10.1021/bi00087a007 / Biochemistry / Kinetic mechanism of Escherichia coli isocitrate dehydrogenase by Dean (1993)
10.1002/pro.5560040708 / Protein Sci / N- and C-capping preferences for all 20 amino acids in α-helical peptides by Doig (1995)
10.1126/science.1553543 / Science / Response of a protein structure to cavity-creating mutations and its relatin to the hydrophobic effect by Erikson (1992)
10.1016/0959-440X(93)90205-Y / Curr. Opin. Struct. Biol / Principles in protein stability derived from protein engineering experiments by Fersht (1993)
10.1006/jmbi.1993.1576 / J. Mol. Biol / Refined crystal structure of the seryl-tRNA synthetase from Thermus thermophilus at 2.5 Å resolution by Fujinaga (1993)
10.1093/protein/7.3.425 / Protein Eng / The effect of engineering surface loops on the thermal stability of Bacillus subtilis neutral protease by Hardy (1994)
10.1002/pro.5560050313 / Protein Sci / A stable intermediate in the thermal unfolding process of a chimeric 3-isopropylmalate dehydrogenase between a thermophilic and a mesophilic enzyme by Hayashi-Iwasaki (1996)
10.1002/pro.5560030206 / Protein Sci / Do salt bridges stabilize proteins? A continuum electrostatic analysis by Hendsch (1994)
10.1016/S0969-2126(01)00267-2 / Structure / 2.0 Å structure of indole-3-glycerol phosphate synthase from the hyperthermophile Sulfolobus solfataricus by Hennig (1995)
10.1021/bi00146a008 / Biochemistry / Role of proline residues in human lysozyme stability by Herning (1992)
10.1016/S0022-2836(99)80018-7 / J. Mol. Biol / Strength and co-operativity of contributions of surface salt bridges to protein stability by Horovitz (1990)
10.1002/pro.5560031205 / Protein Sci / Cavities and packing at protein interfaces by Hubbard (1994)
10.1093/protein/7.5.613 / Protein Eng / Intramolecular cavities in globular proteins by Hubbard (1994)
10.1073/pnas.86.22.8635 / Proc. Natl Acad. Sci / Structure of a bacterial enzyme retgulated by phosphorylation, isocitrate dehydrogenase by Hurley (1989)
10.1021/bi00099a026 / Biochemistry / Catalytic mechanism of NADP+-dependent isocitrate dehydrogenase by Hurley (1991)
10.1016/0022-2836(91)90508-4 / J. Mol. Biol / Three-dimensional structure of a highly thermostable enzyme, 3-isopropylmalate dehydrogenase from Thermus thermophilus at 22 Å resolution by Imada (1991)
10.1021/bi00093a001 / Biochemistry / Effect of cavity creating mutations in the hydrophobic core of chymotrypsin inhibitor 2 by Jackson (1993)
10.1093/oxfordjournals.jbchem.a124975 / J. Biochem / Ligand-induced changes in the conformation of 3-isopropylmalate dehydrogenase from Thermus thermophilus by Kadono (1995)
10.1111/j.1432-1033.1994.tb18623.x / Eur. J. Biochem / Hydrophobic interaction at the subunit interface contributes to the thermostability of 3-isopropylmalate dehydrogenase from an extreme thermophile, Thermus thermophilus by Kirino (1994)
{'key': '10.1006/jmbi.1996.0797_BIB27', 'series-title': 'From First Map to Final Model', 'first-page': '59', 'article-title': 'Halloween...masks and bones', 'author': 'Kleywegt', 'year': '1994'} / From First Map to Final Model / Halloween...masks and bones by Kleywegt (1994)
10.1107/S0907444993011333 / Acta Crystallog sect. D / Detection, delineation, measurement and display of cavities in macromolecular structures by Kleywegt (1994)
10.1006/jmbi.1994.0103 / J. Mol. Biol / The crystal structure of holo-glyceraldehyde-3-phosphate dehydrogenase from the hyperthermophilic bacterium Thermotoga maritima at 2.5 Å resolution by Korndörfer (1995)
10.1128/jb.178.3.723-727.1996 / J. Bacteriol. (1996) / Further stabilization of 3-isopropylmalate dehydrogease of an extreme thermophile, Thermus thermophilus, by a supressor mutation method by Kotsuka (1996)
10.1016/0378-1119(95)00494-Q / Gene / Revision of the amino acid sequence of 3-isopropylmalate dehydrogenase from Salmonella typhimurium by means of X-ray crystallography by Kryger (1995)
10.1073/pnas.82.2.488 / Proc. Natl Acad. Sci. USA / Rapid and efficient site-specific mutagenesis without phenotypic selection by Kunkel (1985)
10.1002/pro.5560020505 / Protein Sci / Estimation of the maximum change in stability of globular proteins upon mutation of a hydrophobic residue to another of smaller size by Lee (1993)
10.1021/bi00001a046 / Biochemistry / Mutational analysis of the catalytic residues lysine 230 and tyrosine 160 in the NADP+-dependent isocitrate dehydrogenase from Escherichia coli by Lee (1995)
10.1126/science.3775366 / Science / Loops in globular proteins by Leszczynski (1986)
10.1021/bi00132a025 / Biochemistry / Structural and energetic consequences of disruptive mutations in a protein core by Lim (1992)
10.1073/pnas.84.19.6663 / Proc. Natl Acad. Sci. USA / Enhanced protein thermostability from site-directed mutations that decrease the entropy of unfolding by Matthews (1987)
{'key': '10.1006/jmbi.1996.0797_BIB38', 'series-title': 'Molecular Replacement', 'first-page': '87', 'article-title': 'AMoRE', 'author': 'Navaza', 'year': '1992'} / Molecular Replacement / AMoRE by Navaza (1992)
10.1016/0022-2836(77)90078-X / J. Mol. Biol / Reversible thermal unfolding of thermostable phosphoglycerate kinase. Thermostability associated with mean zero enthalpy change by Nojima (1977)
10.1146/annurev.bb.13.060184.001555 / Annu. Rev. Biophys. Bioeng / Fluctuations in protein structure from X-ray diffraction by Petsko (1984)
10.1126/science.3381086 / Science / Amino acid preferences for specific locations at the ends of α-helices by Richardson (1988)
10.1146/annurev.bb.22.060193.002121 / Annu. Rev. Biomol. Struct / Hydrogen bonding, hydrophobicity, packing, and protein folding by Rose (1993)
10.1016/S0969-2126(94)00118-9 / Structure / The crystal structure of citrate synthase from the thermophilic archeon Thermoplasma acidophilum by Russell (1994)
10.1038/342296a0 / Nature / Capping and α-helix stability by Serrano (1989)
10.1017/S0033583500004674 / Quart. Rev. Biophys / Mutational studies of protein structures and their stabilities by Shortle (1992)
10.1021/bi00087a008 / Biochemistry / Structure of isocitrate dehydrogenase with isocitrate, nicotinamide adenine dinucleotide phosphate, and calcium at 2.5-Å resolution by Stoddard (1993)
10.1006/jmbi.1995.0599 / J. Mol. Biol / Contribution of hydrophobic residues to the stability of human lysozyme by Takano (1995)
10.1093/protein/7.12.1471 / Protein Eng / The effect of ion pairs on the thermal stability of d-glyceraldehyde 3-phosphate dehydrogenase from the hyperthermophilic bacterium Thermotoga maritima by Tomschy (1994)
10.1038/nsb0295-122 / Nature Struct. Biol / Are buried salt bridges important for protein stability and conformational specificity by Waldburger (1995)
10.1016/S0167-4838(96)00157-4 / Biochim. Biophys. Acta, (1997) / Purification catalytic properties and thermostability of 3-isopropylmalate dehydrogenase from E. coli by Wallon (1996)
{'key': '10.1006/jmbi.1996.0797_BIB51', 'series-title': 'Biosynthesis and Molecular Regulation of Amino Acids in Plants', 'first-page': '69', 'article-title': 'Pressure points in the biosynthetic pathway for branched amino-acids', 'author': 'Wittenbach', 'year': '1992'} / Biosynthesis and Molecular Regulation of Amino Acids in Plants / Pressure points in the biosynthetic pathway for branched amino-acids by Wittenbach (1992)
10.1093/oxfordjournals.jbchem.a123220 / J. Biochem / Purification, catalytic properties and thermal stability of threo-ds-3-isopropylmalate dehydrogenase coded by leuB gene from an extreme thermophile, Thermus thermophilus strain HB8 by Yamada (1990)
10.1016/S0969-2126(01)00251-9 / Structure / The structure of Pyrococcus furiosus glutamate dehydrogenase reveals a key role for ion-pair networks in maintaining enzyme stability at extreme temperatures by Yip (1995)
10.1002/pro.5560040111 / Protein Sci / Modeling substrate binding in Thermus thermophilus isopropylmalate dehydrogenase by Zhang (1995)

Dates

Type	When
Created	22 years, 10 months ago (Oct. 7, 2002, 12:23 p.m.)
Deposited	2 years, 5 months ago (April 4, 2023, 10:16 a.m.)
Indexed	4 months, 3 weeks ago (April 9, 2025, 1:37 a.m.)
Issued	28 years, 6 months ago (March 1, 1997)
Published	28 years, 6 months ago (March 1, 1997)
Published Print	28 years, 6 months ago (March 1, 1997)

Funders 0

None

BibTeX

@article{Wallon_1997, title={Crystal structures of Escherichia coli and Salmonella typhimurium 3-isopropylmalate dehydrogenase and comparison with their thermophilic counterpart from Thermus thermophilus}, volume={266}, ISSN={0022-2836}, url={http://dx.doi.org/10.1006/jmbi.1996.0797}, DOI={10.1006/jmbi.1996.0797}, number={5}, journal={Journal of Molecular Biology}, publisher={Elsevier BV}, author={Wallon, Gerlind and Kryger, Gitay and Lovett, Susan T and Oshima, Tairo and Ringe, Dagmar and Petsko, Gregory A}, year={1997}, month=mar, pages={1016–1031} }

JSON

{
  "indexed": {
    "date-parts": [
      [
        2025,
        4,
        9
      ]
    ],
    "date-time": "2025-04-09T05:37:08Z",
    "timestamp": 1744177028011
  },
  "reference-count": 54,
  "publisher": "Elsevier BV",
  "issue": "5",
  "license": [
    {
      "start": {
        "date-parts": [
          [
            1997,
            3,
            1
          ]
        ],
        "date-time": "1997-03-01T00:00:00Z",
        "timestamp": 857174400000
      },
      "content-version": "tdm",
      "delay-in-days": 0,
      "URL": "https://www.elsevier.com/tdm/userlicense/1.0/"
    }
  ],
  "content-domain": {
    "domain": [],
    "crossmark-restriction": false
  },
  "published-print": {
    "date-parts": [
      [
        1997,
        3
      ]
    ]
  },
  "DOI": "10.1006/jmbi.1996.0797",
  "type": "journal-article",
  "created": {
    "date-parts": [
      [
        2002,
        10,
        7
      ]
    ],
    "date-time": "2002-10-07T16:23:12Z",
    "timestamp": 1034007792000
  },
  "page": "1016-1031",
  "source": "Crossref",
  "is-referenced-by-count": 121,
  "title": "Crystal structures of Escherichia coli and Salmonella typhimurium 3-isopropylmalate dehydrogenase and comparison with their thermophilic counterpart from Thermus thermophilus",
  "prefix": "10.1006",
  "volume": "266",
  "author": [
    {
      "given": "Gerlind",
      "family": "Wallon",
      "sequence": "first",
      "affiliation": []
    },
    {
      "given": "Gitay",
      "family": "Kryger",
      "sequence": "additional",
      "affiliation": []
    },
    {
      "given": "Susan T",
      "family": "Lovett",
      "sequence": "additional",
      "affiliation": []
    },
    {
      "given": "Tairo",
      "family": "Oshima",
      "sequence": "additional",
      "affiliation": []
    },
    {
      "given": "Dagmar",
      "family": "Ringe",
      "sequence": "additional",
      "affiliation": []
    },
    {
      "given": "Gregory A",
      "family": "Petsko",
      "sequence": "additional",
      "affiliation": []
    }
  ],
  "member": "78",
  "reference": [
    {
      "key": "10.1006/jmbi.1996.0797_BIB1",
      "doi-asserted-by": "crossref",
      "first-page": "23",
      "DOI": "10.1002/prot.340080106",
      "article-title": "Protein stability and electrostatic interactions between solvent exposed charged side chains",
      "volume": "8",
      "author": "Akke",
      "year": "1990",
      "journal-title": "Proteins: Struct. Funct. Genet"
    },
    {
      "key": "10.1006/jmbi.1996.0797_BIB2",
      "doi-asserted-by": "crossref",
      "first-page": "867",
      "DOI": "10.1016/S0022-2836(83)80079-5",
      "article-title": "Ion-pairs in proteins",
      "volume": "168",
      "author": "Barlow",
      "year": "1983",
      "journal-title": "J. Mol. Biol"
    },
    {
      "key": "10.1006/jmbi.1996.0797_BIB3",
      "doi-asserted-by": "crossref",
      "first-page": "1312",
      "DOI": "10.1126/science.7761851",
      "article-title": "Mutagenesis and Laue structures of enzyme intermeidates",
      "volume": "268",
      "author": "Bolduc",
      "year": "1995",
      "journal-title": "Science"
    },
    {
      "key": "10.1006/jmbi.1996.0797_BIB4",
      "first-page": "267",
      "article-title": "The free R.-value",
      "volume": "249",
      "author": "Br\u00fcenger",
      "year": "1992",
      "journal-title": "Nature"
    },
    {
      "key": "10.1006/jmbi.1996.0797_BIB5",
      "doi-asserted-by": "crossref",
      "first-page": "458",
      "DOI": "10.1126/science.235.4787.458",
      "article-title": "Crystallographic R.-factor refinement by molecular dynamics",
      "volume": "235",
      "author": "Br\u00fcenger",
      "year": "1987",
      "journal-title": "Sciences"
    },
    {
      "key": "10.1006/jmbi.1996.0797_BIB6",
      "doi-asserted-by": "crossref",
      "first-page": "23",
      "DOI": "10.1126/science.3892686",
      "article-title": "Aromatic-aromatic interaction",
      "volume": "229",
      "author": "Burley",
      "year": "1985",
      "journal-title": "Science"
    },
    {
      "key": "10.1006/jmbi.1996.0797_BIB7",
      "doi-asserted-by": "crossref",
      "first-page": "600",
      "DOI": "10.1006/jmbi.1993.1414",
      "article-title": "Protein unfolding pathways explored through molecular dynamics simulations",
      "volume": "232",
      "author": "Daggett",
      "year": "1993",
      "journal-title": "J. Mol. Biol"
    },
    {
      "key": "10.1006/jmbi.1996.0797_BIB8",
      "doi-asserted-by": "crossref",
      "first-page": "9302",
      "DOI": "10.1021/bi00087a007",
      "article-title": "Kinetic mechanism of Escherichia coli isocitrate dehydrogenase",
      "volume": "32",
      "author": "Dean",
      "year": "1993",
      "journal-title": "Biochemistry"
    },
    {
      "key": "10.1006/jmbi.1996.0797_BIB9",
      "doi-asserted-by": "crossref",
      "first-page": "1325",
      "DOI": "10.1002/pro.5560040708",
      "article-title": "N- and C-capping preferences for all 20 amino acids in \u03b1-helical peptides",
      "volume": "4",
      "author": "Doig",
      "year": "1995",
      "journal-title": "Protein Sci"
    },
    {
      "key": "10.1006/jmbi.1996.0797_BIB10",
      "doi-asserted-by": "crossref",
      "first-page": "178",
      "DOI": "10.1126/science.1553543",
      "article-title": "Response of a protein structure to cavity-creating mutations and its relatin to the hydrophobic effect",
      "volume": "255",
      "author": "Erikson",
      "year": "1992",
      "journal-title": "Science"
    },
    {
      "key": "10.1006/jmbi.1996.0797_BIB11",
      "doi-asserted-by": "crossref",
      "first-page": "75",
      "DOI": "10.1016/0959-440X(93)90205-Y",
      "article-title": "Principles in protein stability derived from protein engineering experiments",
      "volume": "3",
      "author": "Fersht",
      "year": "1993",
      "journal-title": "Curr. Opin. Struct. Biol"
    },
    {
      "key": "10.1006/jmbi.1996.0797_BIB12",
      "doi-asserted-by": "crossref",
      "first-page": "222",
      "DOI": "10.1006/jmbi.1993.1576",
      "article-title": "Refined crystal structure of the seryl-tRNA synthetase from Thermus thermophilus at 2.5 \u00c5 resolution",
      "volume": "234",
      "author": "Fujinaga",
      "year": "1993",
      "journal-title": "J. Mol. Biol"
    },
    {
      "key": "10.1006/jmbi.1996.0797_BIB13",
      "doi-asserted-by": "crossref",
      "first-page": "425",
      "DOI": "10.1093/protein/7.3.425",
      "article-title": "The effect of engineering surface loops on the thermal stability of Bacillus subtilis neutral protease",
      "volume": "7",
      "author": "Hardy",
      "year": "1994",
      "journal-title": "Protein Eng"
    },
    {
      "key": "10.1006/jmbi.1996.0797_BIB14",
      "doi-asserted-by": "crossref",
      "first-page": "511",
      "DOI": "10.1002/pro.5560050313",
      "article-title": "A stable intermediate in the thermal unfolding process of a chimeric 3-isopropylmalate dehydrogenase between a thermophilic and a mesophilic enzyme",
      "volume": "5",
      "author": "Hayashi-Iwasaki",
      "year": "1996",
      "journal-title": "Protein Sci"
    },
    {
      "key": "10.1006/jmbi.1996.0797_BIB15",
      "doi-asserted-by": "crossref",
      "first-page": "211",
      "DOI": "10.1002/pro.5560030206",
      "article-title": "Do salt bridges stabilize proteins? A continuum electrostatic analysis",
      "volume": "3",
      "author": "Hendsch",
      "year": "1994",
      "journal-title": "Protein Sci"
    },
    {
      "key": "10.1006/jmbi.1996.0797_BIB16",
      "doi-asserted-by": "crossref",
      "first-page": "1295",
      "DOI": "10.1016/S0969-2126(01)00267-2",
      "article-title": "2.0 \u00c5 structure of indole-3-glycerol phosphate synthase from the hyperthermophile Sulfolobus solfataricus",
      "volume": "3",
      "author": "Hennig",
      "year": "1995",
      "journal-title": "Structure"
    },
    {
      "key": "10.1006/jmbi.1996.0797_BIB17",
      "doi-asserted-by": "crossref",
      "first-page": "7077",
      "DOI": "10.1021/bi00146a008",
      "article-title": "Role of proline residues in human lysozyme stability",
      "volume": "31",
      "author": "Herning",
      "year": "1992",
      "journal-title": "Biochemistry"
    },
    {
      "key": "10.1006/jmbi.1996.0797_BIB18",
      "doi-asserted-by": "crossref",
      "first-page": "1031",
      "DOI": "10.1016/S0022-2836(99)80018-7",
      "article-title": "Strength and co-operativity of contributions of surface salt bridges to protein stability",
      "volume": "216",
      "author": "Horovitz",
      "year": "1990",
      "journal-title": "J. Mol. Biol"
    },
    {
      "key": "10.1006/jmbi.1996.0797_BIB19",
      "doi-asserted-by": "crossref",
      "first-page": "2194",
      "DOI": "10.1002/pro.5560031205",
      "article-title": "Cavities and packing at protein interfaces",
      "volume": "3",
      "author": "Hubbard",
      "year": "1994",
      "journal-title": "Protein Sci"
    },
    {
      "key": "10.1006/jmbi.1996.0797_BIB20",
      "doi-asserted-by": "crossref",
      "first-page": "613",
      "DOI": "10.1093/protein/7.5.613",
      "article-title": "Intramolecular cavities in globular proteins",
      "volume": "7",
      "author": "Hubbard",
      "year": "1994",
      "journal-title": "Protein Eng"
    },
    {
      "key": "10.1006/jmbi.1996.0797_BIB21",
      "doi-asserted-by": "crossref",
      "first-page": "8635",
      "DOI": "10.1073/pnas.86.22.8635",
      "article-title": "Structure of a bacterial enzyme retgulated by phosphorylation, isocitrate dehydrogenase",
      "volume": "86",
      "author": "Hurley",
      "year": "1989",
      "journal-title": "Proc. Natl Acad. Sci"
    },
    {
      "key": "10.1006/jmbi.1996.0797_BIB22",
      "doi-asserted-by": "crossref",
      "first-page": "8671",
      "DOI": "10.1021/bi00099a026",
      "article-title": "Catalytic mechanism of NADP+-dependent isocitrate dehydrogenase",
      "volume": "30",
      "author": "Hurley",
      "year": "1991",
      "journal-title": "Biochemistry"
    },
    {
      "key": "10.1006/jmbi.1996.0797_BIB23",
      "doi-asserted-by": "crossref",
      "first-page": "725",
      "DOI": "10.1016/0022-2836(91)90508-4",
      "article-title": "Three-dimensional structure of a highly thermostable enzyme, 3-isopropylmalate dehydrogenase from Thermus thermophilus at 22 \u00c5 resolution",
      "volume": "222",
      "author": "Imada",
      "year": "1991",
      "journal-title": "J. Mol. Biol"
    },
    {
      "key": "10.1006/jmbi.1996.0797_BIB24",
      "doi-asserted-by": "crossref",
      "first-page": "11259",
      "DOI": "10.1021/bi00093a001",
      "article-title": "Effect of cavity creating mutations in the hydrophobic core of chymotrypsin inhibitor 2",
      "volume": "32",
      "author": "Jackson",
      "year": "1993",
      "journal-title": "Biochemistry"
    },
    {
      "key": "10.1006/jmbi.1996.0797_BIB25",
      "doi-asserted-by": "crossref",
      "first-page": "745",
      "DOI": "10.1093/oxfordjournals.jbchem.a124975",
      "article-title": "Ligand-induced changes in the conformation of 3-isopropylmalate dehydrogenase from Thermus thermophilus",
      "volume": "118",
      "author": "Kadono",
      "year": "1995",
      "journal-title": "J. Biochem"
    },
    {
      "key": "10.1006/jmbi.1996.0797_BIB26",
      "doi-asserted-by": "crossref",
      "first-page": "275",
      "DOI": "10.1111/j.1432-1033.1994.tb18623.x",
      "article-title": "Hydrophobic interaction at the subunit interface contributes to the thermostability of 3-isopropylmalate dehydrogenase from an extreme thermophile, Thermus thermophilus",
      "volume": "200",
      "author": "Kirino",
      "year": "1994",
      "journal-title": "Eur. J. Biochem"
    },
    {
      "key": "10.1006/jmbi.1996.0797_BIB27",
      "series-title": "From First Map to Final Model",
      "first-page": "59",
      "article-title": "Halloween...masks and bones",
      "author": "Kleywegt",
      "year": "1994"
    },
    {
      "key": "10.1006/jmbi.1996.0797_BIB28",
      "doi-asserted-by": "crossref",
      "first-page": "178",
      "DOI": "10.1107/S0907444993011333",
      "article-title": "Detection, delineation, measurement and display of cavities in macromolecular structures",
      "volume": "50",
      "author": "Kleywegt",
      "year": "1994",
      "journal-title": "Acta Crystallog sect. D"
    },
    {
      "key": "10.1006/jmbi.1996.0797_BIB29",
      "doi-asserted-by": "crossref",
      "first-page": "511",
      "DOI": "10.1006/jmbi.1994.0103",
      "article-title": "The crystal structure of holo-glyceraldehyde-3-phosphate dehydrogenase from the hyperthermophilic bacterium Thermotoga maritima at 2.5 \u00c5 resolution",
      "volume": "246",
      "author": "Kornd\u00f6rfer",
      "year": "1995",
      "journal-title": "J. Mol. Biol"
    },
    {
      "key": "10.1006/jmbi.1996.0797_BIB30",
      "doi-asserted-by": "crossref",
      "first-page": "723",
      "DOI": "10.1128/jb.178.3.723-727.1996",
      "article-title": "Further stabilization of 3-isopropylmalate dehydrogease of an extreme thermophile, Thermus thermophilus, by a supressor mutation method",
      "volume": "178",
      "author": "Kotsuka",
      "year": "1996",
      "journal-title": "J. Bacteriol. (1996)"
    },
    {
      "key": "10.1006/jmbi.1996.0797_BIB31",
      "doi-asserted-by": "crossref",
      "first-page": "85",
      "DOI": "10.1016/0378-1119(95)00494-Q",
      "article-title": "Revision of the amino acid sequence of 3-isopropylmalate dehydrogenase from Salmonella typhimurium by means of X-ray crystallography",
      "volume": "164",
      "author": "Kryger",
      "year": "1995",
      "journal-title": "Gene"
    },
    {
      "key": "10.1006/jmbi.1996.0797_BIB32",
      "doi-asserted-by": "crossref",
      "first-page": "488",
      "DOI": "10.1073/pnas.82.2.488",
      "article-title": "Rapid and efficient site-specific mutagenesis without phenotypic selection",
      "volume": "82",
      "author": "Kunkel",
      "year": "1985",
      "journal-title": "Proc. Natl Acad. Sci. USA"
    },
    {
      "key": "10.1006/jmbi.1996.0797_BIB33",
      "doi-asserted-by": "crossref",
      "first-page": "733",
      "DOI": "10.1002/pro.5560020505",
      "article-title": "Estimation of the maximum change in stability of globular proteins upon mutation of a hydrophobic residue to another of smaller size",
      "volume": "2",
      "author": "Lee",
      "year": "1993",
      "journal-title": "Protein Sci"
    },
    {
      "key": "10.1006/jmbi.1996.0797_BIB34",
      "doi-asserted-by": "crossref",
      "first-page": "378",
      "DOI": "10.1021/bi00001a046",
      "article-title": "Mutational analysis of the catalytic residues lysine 230 and tyrosine 160 in the NADP+-dependent isocitrate dehydrogenase from Escherichia coli",
      "volume": "34",
      "author": "Lee",
      "year": "1995",
      "journal-title": "Biochemistry"
    },
    {
      "key": "10.1006/jmbi.1996.0797_BIB35",
      "doi-asserted-by": "crossref",
      "first-page": "849",
      "DOI": "10.1126/science.3775366",
      "article-title": "Loops in globular proteins",
      "volume": "234",
      "author": "Leszczynski",
      "year": "1986",
      "journal-title": "Science"
    },
    {
      "key": "10.1006/jmbi.1996.0797_BIB36",
      "doi-asserted-by": "crossref",
      "first-page": "4324",
      "DOI": "10.1021/bi00132a025",
      "article-title": "Structural and energetic consequences of disruptive mutations in a protein core",
      "volume": "31",
      "author": "Lim",
      "year": "1992",
      "journal-title": "Biochemistry"
    },
    {
      "key": "10.1006/jmbi.1996.0797_BIB37",
      "doi-asserted-by": "crossref",
      "first-page": "6663",
      "DOI": "10.1073/pnas.84.19.6663",
      "article-title": "Enhanced protein thermostability from site-directed mutations that decrease the entropy of unfolding",
      "volume": "84",
      "author": "Matthews",
      "year": "1987",
      "journal-title": "Proc. Natl Acad. Sci. USA"
    },
    {
      "key": "10.1006/jmbi.1996.0797_BIB38",
      "series-title": "Molecular Replacement",
      "first-page": "87",
      "article-title": "AMoRE",
      "author": "Navaza",
      "year": "1992"
    },
    {
      "key": "10.1006/jmbi.1996.0797_BIB39",
      "doi-asserted-by": "crossref",
      "first-page": "429",
      "DOI": "10.1016/0022-2836(77)90078-X",
      "article-title": "Reversible thermal unfolding of thermostable phosphoglycerate kinase. Thermostability associated with mean zero enthalpy change",
      "volume": "116",
      "author": "Nojima",
      "year": "1977",
      "journal-title": "J. Mol. Biol"
    },
    {
      "key": "10.1006/jmbi.1996.0797_BIB40",
      "doi-asserted-by": "crossref",
      "first-page": "331",
      "DOI": "10.1146/annurev.bb.13.060184.001555",
      "article-title": "Fluctuations in protein structure from X-ray diffraction",
      "volume": "13",
      "author": "Petsko",
      "year": "1984",
      "journal-title": "Annu. Rev. Biophys. Bioeng"
    },
    {
      "key": "10.1006/jmbi.1996.0797_BIB41",
      "doi-asserted-by": "crossref",
      "DOI": "10.1126/science.3381086",
      "article-title": "Amino acid preferences for specific locations at the ends of \u03b1-helices",
      "volume": "240",
      "author": "Richardson",
      "year": "1988",
      "journal-title": "Science"
    },
    {
      "key": "10.1006/jmbi.1996.0797_BIB42",
      "doi-asserted-by": "crossref",
      "first-page": "381",
      "DOI": "10.1146/annurev.bb.22.060193.002121",
      "article-title": "Hydrogen bonding, hydrophobicity, packing, and protein folding",
      "volume": "22",
      "author": "Rose",
      "year": "1993",
      "journal-title": "Annu. Rev. Biomol. Struct"
    },
    {
      "key": "10.1006/jmbi.1996.0797_BIB43",
      "doi-asserted-by": "crossref",
      "first-page": "1157",
      "DOI": "10.1016/S0969-2126(94)00118-9",
      "article-title": "The crystal structure of citrate synthase from the thermophilic archeon Thermoplasma acidophilum",
      "volume": "2",
      "author": "Russell",
      "year": "1994",
      "journal-title": "Structure"
    },
    {
      "key": "10.1006/jmbi.1996.0797_BIB44",
      "doi-asserted-by": "crossref",
      "first-page": "296",
      "DOI": "10.1038/342296a0",
      "article-title": "Capping and \u03b1-helix stability",
      "volume": "342",
      "author": "Serrano",
      "year": "1989",
      "journal-title": "Nature"
    },
    {
      "key": "10.1006/jmbi.1996.0797_BIB45",
      "doi-asserted-by": "crossref",
      "first-page": "205",
      "DOI": "10.1017/S0033583500004674",
      "article-title": "Mutational studies of protein structures and their stabilities",
      "volume": "25",
      "author": "Shortle",
      "year": "1992",
      "journal-title": "Quart. Rev. Biophys"
    },
    {
      "key": "10.1006/jmbi.1996.0797_BIB46",
      "doi-asserted-by": "crossref",
      "first-page": "9310",
      "DOI": "10.1021/bi00087a008",
      "article-title": "Structure of isocitrate dehydrogenase with isocitrate, nicotinamide adenine dinucleotide phosphate, and calcium at 2.5-\u00c5 resolution",
      "volume": "32",
      "author": "Stoddard",
      "year": "1993",
      "journal-title": "Biochemistry"
    },
    {
      "key": "10.1006/jmbi.1996.0797_BIB47",
      "doi-asserted-by": "crossref",
      "first-page": "62",
      "DOI": "10.1006/jmbi.1995.0599",
      "article-title": "Contribution of hydrophobic residues to the stability of human lysozyme",
      "volume": "254",
      "author": "Takano",
      "year": "1995",
      "journal-title": "J. Mol. Biol"
    },
    {
      "key": "10.1006/jmbi.1996.0797_BIB48",
      "doi-asserted-by": "crossref",
      "first-page": "1471",
      "DOI": "10.1093/protein/7.12.1471",
      "article-title": "The effect of ion pairs on the thermal stability of d-glyceraldehyde 3-phosphate dehydrogenase from the hyperthermophilic bacterium Thermotoga maritima",
      "volume": "7",
      "author": "Tomschy",
      "year": "1994",
      "journal-title": "Protein Eng"
    },
    {
      "key": "10.1006/jmbi.1996.0797_BIB49",
      "doi-asserted-by": "crossref",
      "first-page": "122",
      "DOI": "10.1038/nsb0295-122",
      "article-title": "Are buried salt bridges important for protein stability and conformational specificity",
      "volume": "2",
      "author": "Waldburger",
      "year": "1995",
      "journal-title": "Nature Struct. Biol"
    },
    {
      "key": "10.1006/jmbi.1996.0797_BIB50",
      "doi-asserted-by": "crossref",
      "first-page": "105",
      "DOI": "10.1016/S0167-4838(96)00157-4",
      "article-title": "Purification catalytic properties and thermostability of 3-isopropylmalate dehydrogenase from E. coli",
      "volume": "1337",
      "author": "Wallon",
      "year": "1996",
      "journal-title": "Biochim. Biophys. Acta, (1997)"
    },
    {
      "key": "10.1006/jmbi.1996.0797_BIB51",
      "series-title": "Biosynthesis and Molecular Regulation of Amino Acids in Plants",
      "first-page": "69",
      "article-title": "Pressure points in the biosynthetic pathway for branched amino-acids",
      "author": "Wittenbach",
      "year": "1992"
    },
    {
      "key": "10.1006/jmbi.1996.0797_BIB52",
      "doi-asserted-by": "crossref",
      "first-page": "449",
      "DOI": "10.1093/oxfordjournals.jbchem.a123220",
      "article-title": "Purification, catalytic properties and thermal stability of threo-ds-3-isopropylmalate dehydrogenase coded by leuB gene from an extreme thermophile, Thermus thermophilus strain HB8",
      "volume": "108",
      "author": "Yamada",
      "year": "1990",
      "journal-title": "J. Biochem"
    },
    {
      "key": "10.1006/jmbi.1996.0797_BIB53",
      "doi-asserted-by": "crossref",
      "first-page": "1147",
      "DOI": "10.1016/S0969-2126(01)00251-9",
      "article-title": "The structure of Pyrococcus furiosus glutamate dehydrogenase reveals a key role for ion-pair networks in maintaining enzyme stability at extreme temperatures",
      "volume": "3",
      "author": "Yip",
      "year": "1995",
      "journal-title": "Structure"
    },
    {
      "key": "10.1006/jmbi.1996.0797_BIB54",
      "doi-asserted-by": "crossref",
      "first-page": "84",
      "DOI": "10.1002/pro.5560040111",
      "article-title": "Modeling substrate binding in Thermus thermophilus isopropylmalate dehydrogenase",
      "author": "Zhang",
      "year": "1995",
      "journal-title": "Protein Sci"
    }
  ],
  "container-title": "Journal of Molecular Biology",
  "original-title": [],
  "language": "en",
  "link": [
    {
      "URL": "https://api.elsevier.com/content/article/PII:S0022283696907974?httpAccept=text/xml",
      "content-type": "text/xml",
      "content-version": "vor",
      "intended-application": "text-mining"
    },
    {
      "URL": "https://api.elsevier.com/content/article/PII:S0022283696907974?httpAccept=text/plain",
      "content-type": "text/plain",
      "content-version": "vor",
      "intended-application": "text-mining"
    }
  ],
  "deposited": {
    "date-parts": [
      [
        2023,
        4,
        4
      ]
    ],
    "date-time": "2023-04-04T14:16:26Z",
    "timestamp": 1680617786000
  },
  "score": 1,
  "resource": {
    "primary": {
      "URL": "https://linkinghub.elsevier.com/retrieve/pii/S0022283696907974"
    }
  },
  "subtitle": [],
  "short-title": [],
  "issued": {
    "date-parts": [
      [
        1997,
        3
      ]
    ]
  },
  "references-count": 54,
  "journal-issue": {
    "issue": "5",
    "published-print": {
      "date-parts": [
        [
          1997,
          3
        ]
      ]
    }
  },
  "alternative-id": [
    "S0022283696907974"
  ],
  "URL": "http://dx.doi.org/10.1006/jmbi.1996.0797",
  "relation": {},
  "ISSN": [
    "0022-2836"
  ],
  "subject": [],
  "container-title-short": "Journal of Molecular Biology",
  "published": {
    "date-parts": [
      [
        1997,
        3
      ]
    ]
  }
}