{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,3,20]],"date-time":"2026-03-20T04:59:06Z","timestamp":1773982746351,"version":"3.50.1"},"reference-count":49,"publisher":"Elsevier BV","issue":"7","license":[{"start":{"date-parts":[[1994,7,1]],"date-time":"1994-07-01T00:00:00Z","timestamp":773020800000},"content-version":"tdm","delay-in-days":0,"URL":"https:\/\/www.elsevier.com\/tdm\/userlicense\/1.0\/"}],"content-domain":{"domain":[],"crossmark-restriction":false},"short-container-title":["Structure"],"published-print":{"date-parts":[[1994,7]]},"DOI":"10.1016\/s0969-2126(00)00065-4","type":"journal-article","created":{"date-parts":[[2004,8,23]],"date-time":"2004-08-23T14:47:34Z","timestamp":1093272454000},"page":"641-649","source":"Crossref","is-referenced-by-count":483,"title":["Volume changes on protein folding"],"prefix":"10.1016","volume":"2","author":[{"given":"Yehouda","family":"Harpaz","sequence":"first","affiliation":[]},{"given":"Mark","family":"Gerstein","sequence":"additional","affiliation":[]},{"given":"Cyrus","family":"Chothia","sequence":"additional","affiliation":[]}],"member":"78","reference":[{"key":"10.1016\/S0969-2126(00)00065-4_BIB1","doi-asserted-by":"crossref","first-page":"1038","DOI":"10.1021\/bi00806a045","article-title":"Thermodynamics of protein denaturation. Effect of pressure on the denaturation of ribonuclease A","volume":"9","author":"Brandts","year":"1970","journal-title":"Biochemistry"},{"key":"10.1016\/S0969-2126(00)00065-4_BIB2","doi-asserted-by":"crossref","first-page":"2436","DOI":"10.1021\/bi00789a002","article-title":"Reversible pressure\u2013temperature denaturation of chymotrypsinogen","volume":"10","author":"Hawley","year":"1971","journal-title":"Biochemistry"},{"key":"10.1016\/S0969-2126(00)00065-4_BIB3","doi-asserted-by":"crossref","first-page":"4217","DOI":"10.1021\/bi00745a028","article-title":"Pressure denaturation of metmyoglobin","volume":"12","author":"Zipp","year":"1973","journal-title":"Biochemistry"},{"key":"10.1016\/S0969-2126(00)00065-4_BIB4","doi-asserted-by":"crossref","first-page":"1","DOI":"10.1016\/S0065-3233(08)60608-7","article-title":"Some factors in the interpretation of protein denaturation","volume":"14","author":"Kauzmann","year":"1959","journal-title":"Adv. Protein Chem"},{"key":"10.1016\/S0969-2126(00)00065-4_BIB5","doi-asserted-by":"crossref","first-page":"763","DOI":"10.1038\/325763a0","article-title":"Thermodynamics of unfolding","volume":"325","author":"Kauzmann","year":"1987","journal-title":"Nature"},{"key":"10.1016\/S0969-2126(00)00065-4_BIB6","doi-asserted-by":"crossref","first-page":"1","DOI":"10.1016\/0022-2836(74)90570-1","article-title":"The interpretation of protein structures: total volume, group volume distributions and packing density","volume":"82","author":"Richards","year":"1974","journal-title":"J. Mol. Biol"},{"key":"10.1016\/S0969-2126(00)00065-4_BIB7","doi-asserted-by":"crossref","first-page":"304","DOI":"10.1038\/254304a0","article-title":"Structural invariants in protein folding","volume":"254","author":"Chothia","year":"1975","journal-title":"Nature"},{"key":"10.1016\/S0969-2126(00)00065-4_BIB8","doi-asserted-by":"crossref","first-page":"535","DOI":"10.1016\/S0022-2836(77)80200-3","article-title":"The protein data bank: a computer-based archival file for macromolecular structures","volume":"112","author":"Bernstein","year":"1977","journal-title":"J. Mol. Biol"},{"key":"10.1016\/S0969-2126(00)00065-4_BIB9","doi-asserted-by":"crossref","first-page":"345","DOI":"10.1002\/prot.340120407","article-title":"Stereochemical quality of protein structure coordinates","volume":"12","author":"Morris","year":"1992","journal-title":"Proteins"},{"key":"10.1016\/S0969-2126(00)00065-4_BIB10","doi-asserted-by":"crossref","first-page":"62","DOI":"10.1039\/df9674300062","article-title":"Random-close-packed hard-sphere model II. Geometry of random packing of hard spheres","volume":"43","author":"Bernal","year":"1967","journal-title":"Discussions Faraday Soc"},{"key":"10.1016\/S0969-2126(00)00065-4_BIB11","doi-asserted-by":"crossref","first-page":"379","DOI":"10.1016\/0022-2836(71)90324-X","article-title":"The interpretation of protein structures: estimation of static accessibility","volume":"55","author":"Lee","year":"1971","journal-title":"J. Mol. Biol"},{"key":"10.1016\/S0969-2126(00)00065-4_BIB12","series-title":"Proteins, Amino Acids and Peptides as Ions and Dipolar Ions","first-page":"370","author":"Cohn","year":"1943"},{"key":"10.1016\/S0969-2126(00)00065-4_BIB13","doi-asserted-by":"crossref","first-page":"86","DOI":"10.1021\/j150645a021","article-title":"Apparent molal volumes of amino acids, N-acetylamino acids and peptides in aqueous solutions","volume":"88","author":"Mishra","year":"1984","journal-title":"J. Phys. Chem"},{"key":"10.1016\/S0969-2126(00)00065-4_BIB14","first-page":"784","article-title":"Studies in the physical chemistry of amino acids, peptides and related substances. I. The apparent molal volume and the electrostriction of the solvent. J. Am. Chem","volume":"56","author":"Cohn","year":"1934","journal-title":"Soc"},{"key":"10.1016\/S0969-2126(00)00065-4_BIB15","doi-asserted-by":"crossref","first-page":"3129","DOI":"10.1021\/j150658a042","article-title":"Partial molar volumes of \u03b1-amino acids with ionogenic side chains in water","volume":"88","author":"Rao","year":"1984","journal-title":"J. Phys. Chem"},{"key":"10.1016\/S0969-2126(00)00065-4_BIB16","doi-asserted-by":"crossref","first-page":"109","DOI":"10.1007\/BF00646283","article-title":"Solvation of amino acid residues in water and urea\u2013water mixtures: volumes and heat capacities of 20 amino acids in water and 8 molar urea at 25\u00b0 C","volume":"15","author":"Jolicoeur","year":"1986","journal-title":"J. Solution Chem"},{"key":"10.1016\/S0969-2126(00)00065-4_BIB17","doi-asserted-by":"crossref","first-page":"1771","DOI":"10.1021\/ja00869a002","article-title":"Volume changes in protein reactions. II Comparison of ionization reactions in proteins and small molecules","volume":"84","author":"Kauzmann","year":"1962","journal-title":"J. Am. Chem. Soc"},{"key":"10.1016\/S0969-2126(00)00065-4_BIB18","doi-asserted-by":"crossref","first-page":"3117","DOI":"10.1039\/FT9908603117","article-title":"Thermodynamic properties of peptide solutions","volume":"86","author":"Reading","year":"1990","journal-title":"J. Chem. Soc. Faraday Trans"},{"key":"10.1016\/S0969-2126(00)00065-4_BIB19","doi-asserted-by":"crossref","first-page":"537","DOI":"10.1002\/bip.360320509","article-title":"Partial molar volumes of the amino acid side-chains of proteins in aqueous solution: some comments on their estimation using partial molar volumes of amino acids and small peptides","volume":"32","author":"Hedwig","year":"1992","journal-title":"Biopolymers"},{"key":"10.1016\/S0969-2126(00)00065-4_BIB20","doi-asserted-by":"crossref","first-page":"695","DOI":"10.1002\/bip.360240409","article-title":"Aqueous solutions containing amino acids and peptides XX: volumetric behaviour of some terminally substituted amino-acids and peptides at 298.15 K","volume":"24","author":"Leslie","year":"1985","journal-title":"Biopolymers"},{"key":"10.1016\/S0969-2126(00)00065-4_BIB21","doi-asserted-by":"crossref","first-page":"2706","DOI":"10.1021\/j100484a006","article-title":"Compressibility of globular proteins in water at 25\u00b0 C","volume":"83","author":"Gekko","year":"1979","journal-title":"J. Phys. Chem"},{"key":"10.1016\/S0969-2126(00)00065-4_BIB22","doi-asserted-by":"crossref","first-page":"750","DOI":"10.1073\/pnas.80.3.750","article-title":"Adiabatic compressibility of globular proteins","volume":"80","author":"Gavish","year":"1983","journal-title":"Proc. Natl. Acad. Sci. USA"},{"key":"10.1016\/S0969-2126(00)00065-4_BIB23","doi-asserted-by":"crossref","first-page":"224","DOI":"10.1021\/ma60038a014","article-title":"Hydration behaviour of ionic dextran derivatives","volume":"7","author":"Gekko","year":"1974","journal-title":"Macromolecules"},{"key":"10.1016\/S0969-2126(00)00065-4_BIB24","doi-asserted-by":"crossref","first-page":"1817","DOI":"10.1021\/j100534a006","article-title":"On the volume changes upon the protonation of N-alkylcarboxylate ions and N-alkylamines in aqueous solution","volume":"81","author":"Zana","year":"1977","journal-title":"J. Phys. Chem"},{"key":"10.1016\/S0969-2126(00)00065-4_BIB25","doi-asserted-by":"crossref","first-page":"225","DOI":"10.1016\/0022-2836(80)90373-3","article-title":"How different amino acid sequences determine similar protein structures: the structure and evolutionary dynamics of the globins","volume":"136","author":"Lesk","year":"1980","journal-title":"J. Mol. Biol"},{"key":"10.1016\/S0969-2126(00)00065-4_BIB26","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 relation to the hydrophobic effect","volume":"255","author":"Eriksson","year":"1992","journal-title":"Science"},{"key":"10.1016\/S0969-2126(00)00065-4_BIB27","doi-asserted-by":"crossref","first-page":"847","DOI":"10.1006\/jmbi.1993.1630","article-title":"Crystal structural analysis of mutations in the hydrophobic cores of barnase","volume":"234","author":"Buckle","year":"1993","journal-title":"J. Mol. Biol"},{"key":"10.1016\/S0969-2126(00)00065-4_BIB28","doi-asserted-by":"crossref","first-page":"641","DOI":"10.1016\/0022-2836(87)90038-6","article-title":"Interior and surface of monomeric proteins","volume":"196","author":"Miller","year":"1987","journal-title":"J. Mol. Biol"},{"key":"10.1016\/S0969-2126(00)00065-4_BIB29","doi-asserted-by":"crossref","first-page":"7110","DOI":"10.1073\/pnas.89.15.7110","article-title":"Relation between the convergence temperatures Th\u2217 and Ts\u2217 in protein unfolding","volume":"89","author":"Baldwin","year":"1992","journal-title":"Proc. Natl. Acad. Sci. USA"},{"key":"10.1016\/S0969-2126(00)00065-4_BIB30","doi-asserted-by":"crossref","first-page":"3947","DOI":"10.1021\/bi00131a009","article-title":"Use of liquid hydrocarbon and amide transfer data to estimate contributions to thermodynamic functions of protein folding from the removal of nonpolar and polar surfaces from water","volume":"31","author":"Spolar","year":"1992","journal-title":"Biochemistry"},{"key":"10.1016\/S0969-2126(00)00065-4_BIB31","doi-asserted-by":"crossref","first-page":"5154","DOI":"10.1073\/pnas.88.12.5154","article-title":"Isoenthalpic and isoentropic temperatures and the thermodynamics of protein denaturation","volume":"88","author":"Lee","year":"1991","journal-title":"Proc. Natl. Acad. Sci. USA"},{"key":"10.1016\/S0969-2126(00)00065-4_BIB32","doi-asserted-by":"crossref","first-page":"3795","DOI":"10.1021\/j100895a026","article-title":"Volume changes in hydrocarbon\u2013water systems. Partial molal volumes of alcohol\u2013water solutions","volume":"69","author":"Friedman","year":"1965","journal-title":"J. Phys. Chem"},{"key":"10.1016\/S0969-2126(00)00065-4_BIB33","doi-asserted-by":"crossref","first-page":"38","DOI":"10.1111\/j.1399-3011.1978.tb02865.x","article-title":"Tight packing of protein cores and interfaces","volume":"12","author":"Bello","year":"1978","journal-title":"Int. J. Pept. Protein Res"},{"key":"10.1016\/S0969-2126(00)00065-4_BIB34","doi-asserted-by":"crossref","first-page":"559","DOI":"10.1126\/science.2300815","article-title":"Common features of protein unfolding and dissolution of hydrophobic compounds","volume":"247","author":"Murphy","year":"1990","journal-title":"Science"},{"key":"10.1016\/S0969-2126(00)00065-4_BIB35","doi-asserted-by":"crossref","first-page":"699","DOI":"10.1016\/0022-2836(91)90506-2","article-title":"Solid model compounds and the thermodynamics of protein unfolding","volume":"222","author":"Murphy","year":"1991","journal-title":"J. Mol. Biol"},{"key":"10.1016\/S0969-2126(00)00065-4_BIB36","doi-asserted-by":"crossref","first-page":"601","DOI":"10.1016\/0959-440X(93)90090-8","article-title":"De novo protein design: from molten globules to native-like states","volume":"3","author":"Betz","year":"1993","journal-title":"Curr. Opin. Struct. Biol"},{"key":"10.1016\/S0969-2126(00)00065-4_BIB37","doi-asserted-by":"crossref","first-page":"7133","DOI":"10.1021\/bi00483a001","article-title":"Dominant forces in protein folding","volume":"29","author":"Dill","year":"1990","journal-title":"Biochemistry"},{"key":"10.1016\/S0969-2126(00)00065-4_BIB38","doi-asserted-by":"crossref","first-page":"165","DOI":"10.1016\/0003-9861(79)90563-0","article-title":"Hydrodynamics and protein hydration","volume":"196","author":"Squire","year":"1979","journal-title":"Arch. Biochem. Biophys"},{"key":"10.1016\/S0969-2126(00)00065-4_BIB39","doi-asserted-by":"crossref","first-page":"725","DOI":"10.1016\/0022-2836(87)90250-6","article-title":"Refinement of the C222 1 crystal form of oxidized uteroglobin at 1.34 \u00e5 resolution","volume":"194","author":"Morize","year":"1987","journal-title":"J. Mol. Biol"},{"key":"10.1016\/S0969-2126(00)00065-4_BIB40","doi-asserted-by":"crossref","first-page":"591","DOI":"10.1038\/327591a0","article-title":"The crystal structure of trp aporepressor at 1.8 \u00e5 shows how binding tryptophan enhances DNA affinity","volume":"327","author":"Zhang","year":"1987","journal-title":"Nature"},{"key":"10.1016\/S0969-2126(00)00065-4_BIB41","doi-asserted-by":"crossref","first-page":"181","DOI":"10.1016\/0022-2836(82)90174-7","article-title":"Structure of copper, zinc superoxide dismutase","volume":"160","author":"Tainer","year":"1982","journal-title":"J. Mol. Biol"},{"key":"10.1016\/S0969-2126(00)00065-4_BIB42","doi-asserted-by":"crossref","first-page":"941","DOI":"10.1016\/0022-2836(91)80185-W","article-title":"Crystal structure of uncleaved ovalbumin at 1.95 \u00e5 resolution","volume":"221","author":"Stein","year":"1991","journal-title":"J. Mol. Biol"},{"key":"10.1016\/S0969-2126(00)00065-4_BIB43","doi-asserted-by":"crossref","first-page":"477","DOI":"10.1016\/0022-2836(92)90665-7","article-title":"Three-dimensional structure of the bifunctional enzyme phosphoribosylanthranilate isomerase indoleglycerolphosphate synthase from Escherichia coli refined at 2.0 \u00e5 resolution","volume":"223","author":"Wilmanns","year":"1992","journal-title":"J. Mol. Biol"},{"key":"10.1016\/S0969-2126(00)00065-4_BIB44","doi-asserted-by":"crossref","first-page":"535","DOI":"10.1107\/S0108768191001970","article-title":"Structure and molecular model refinement of Aspergillus oryzae (taka) \u03b1-amylase: an application of the stimulated-annealing method","volume":"47","author":"Swift","year":"1991","journal-title":"Acta Crystallogr. B"},{"key":"10.1016\/S0969-2126(00)00065-4_BIB45","doi-asserted-by":"crossref","first-page":"289","DOI":"10.1002\/prot.340050406","article-title":"The structure of aconitase","volume":"5","author":"Robbins","year":"1989","journal-title":"Proteins"},{"key":"10.1016\/S0969-2126(00)00065-4_BIB46","doi-asserted-by":"crossref","first-page":"495","DOI":"10.1016\/0022-2836(92)90935-D","article-title":"The x-ray structure refinement and comparison of three forms of mitochondrial aspartate aminotransferase","volume":"225","author":"Mcphalen","year":"1992","journal-title":"J. Mol. Biol"},{"key":"10.1016\/S0969-2126(00)00065-4_BIB47","doi-asserted-by":"crossref","first-page":"171","DOI":"10.1016\/0022-2836(87)90635-8","article-title":"The structure of holo-glyceraldehyde-3-phosphate dehydrogenase from Bacillus stearothermophilus at 1.8 \u00e5 resolution","volume":"193","author":"Skarzynski","year":"1987","journal-title":"J. Mol. Biol"},{"key":"10.1016\/S0969-2126(00)00065-4_BIB48","doi-asserted-by":"crossref","first-page":"233","DOI":"10.1016\/0022-2836(91)90887-C","article-title":"Structural mechanism for glycogen phosphorylase: control by phosphorylation and AMP","volume":"218","author":"Barford","year":"1991","journal-title":"J. Mol. Biol"},{"key":"10.1016\/S0969-2126(00)00065-4_BIB49","doi-asserted-by":"crossref","first-page":"497","DOI":"10.1107\/S0108768186097835","article-title":"The refined structure of beef liver catalase at 2.5 \u00e5 resolution","volume":"42","author":"Fita","year":"1986","journal-title":"Acta Crystsllogr. B"}],"container-title":["Structure"],"original-title":[],"language":"en","link":[{"URL":"https:\/\/api.elsevier.com\/content\/article\/PII:S0969212600000654?httpAccept=text\/xml","content-type":"text\/xml","content-version":"vor","intended-application":"text-mining"},{"URL":"https:\/\/api.elsevier.com\/content\/article\/PII:S0969212600000654?httpAccept=text\/plain","content-type":"text\/plain","content-version":"vor","intended-application":"text-mining"}],"deposited":{"date-parts":[[2019,2,4]],"date-time":"2019-02-04T14:54:31Z","timestamp":1549292071000},"score":1,"resource":{"primary":{"URL":"https:\/\/linkinghub.elsevier.com\/retrieve\/pii\/S0969212600000654"}},"subtitle":[],"short-title":[],"issued":{"date-parts":[[1994,7]]},"references-count":49,"journal-issue":{"issue":"7","published-print":{"date-parts":[[1994,7]]}},"alternative-id":["S0969212600000654"],"URL":"https:\/\/doi.org\/10.1016\/s0969-2126(00)00065-4","relation":{},"ISSN":["0969-2126"],"issn-type":[{"value":"0969-2126","type":"print"}],"subject":[],"published":{"date-parts":[[1994,7]]}}}