{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2025,10,5]],"date-time":"2025-10-05T04:10:38Z","timestamp":1759637438371,"version":"build-2065373602"},"reference-count":55,"publisher":"Elsevier BV","issue":"1","license":[{"start":{"date-parts":[[2017,1,1]],"date-time":"2017-01-01T00:00:00Z","timestamp":1483228800000},"content-version":"tdm","delay-in-days":0,"URL":"https:\/\/www.elsevier.com\/tdm\/userlicense\/1.0\/"},{"start":{"date-parts":[[2017,1,1]],"date-time":"2017-01-01T00:00:00Z","timestamp":1483228800000},"content-version":"tdm","delay-in-days":0,"URL":"https:\/\/www.elsevier.com\/legal\/tdmrep-license"},{"start":{"date-parts":[[2017,12,10]],"date-time":"2017-12-10T00:00:00Z","timestamp":1512864000000},"content-version":"am","delay-in-days":343,"URL":"http:\/\/www.elsevier.com\/open-access\/userlicense\/1.0\/"}],"funder":[{"DOI":"10.13039\/100000015","name":"U.S. Department of Energy","doi-asserted-by":"publisher","award":["DE-AC05-00OR22725"],"award-info":[{"award-number":["DE-AC05-00OR22725"]}],"id":[{"id":"10.13039\/100000015","id-type":"DOI","asserted-by":"publisher"}]},{"DOI":"10.13039\/100000015","name":"U.S. Department of Energy","doi-asserted-by":"publisher","award":["DE-AC05-00OR22725"],"award-info":[{"award-number":["DE-AC05-00OR22725"]}],"id":[{"id":"10.13039\/100000015","id-type":"DOI","asserted-by":"publisher"}]}],"content-domain":{"domain":["elsevier.com","sciencedirect.com"],"crossmark-restriction":true},"short-container-title":["Biochimica et Biophysica Acta (BBA) - General Subjects"],"published-print":{"date-parts":[[2017,1]]},"DOI":"10.1016\/j.bbagen.2016.04.024","type":"journal-article","created":{"date-parts":[[2016,5,3]],"date-time":"2016-05-03T22:11:25Z","timestamp":1462313485000},"page":"3513-3519","update-policy":"https:\/\/doi.org\/10.1016\/elsevier_cm_policy","source":"Crossref","is-referenced-by-count":9,"special_numbering":"PB","title":["Microscopic relaxations in a protein sustained down to 160 K in a non-glass forming organic solvent"],"prefix":"10.1016","volume":"1861","author":[{"given":"E.","family":"Mamontov","sequence":"first","affiliation":[],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"H.","family":"O'Neill","sequence":"additional","affiliation":[],"role":[{"role":"author","vocabulary":"crossref"}]}],"member":"78","reference":[{"key":"10.1016\/j.bbagen.2016.04.024_bb0005","doi-asserted-by":"crossref","first-page":"37","DOI":"10.1016\/S0065-3233(08)60197-7","article-title":"Protein hydration and function","volume":"41","author":"Rupley","year":"1991","journal-title":"Adv. Protein Chem."},{"key":"10.1016\/j.bbagen.2016.04.024_bb0010","doi-asserted-by":"crossref","first-page":"16047","DOI":"10.1073\/pnas.212637899","article-title":"Slaving: solvent fluctuations dominate protein dynamics and functions","volume":"99","author":"Fenimore","year":"2002","journal-title":"Proc. Natl. Acad. Sci."},{"key":"10.1016\/j.bbagen.2016.04.024_bb0015","doi-asserted-by":"crossref","first-page":"14408","DOI":"10.1073\/pnas.0405573101","article-title":"Bulk-solvent and hydration-shell fluctuations, similar to alpha- and beta-fluctuations in glasses, control protein motions and functions","volume":"101","author":"Fenimore","year":"2004","journal-title":"Proc. Natl. Acad. Sci."},{"key":"10.1016\/j.bbagen.2016.04.024_bb0020","doi-asserted-by":"crossref","first-page":"5129","DOI":"10.1073\/pnas.0900336106","article-title":"A unified model of protein dynamics","volume":"106","author":"Frauenfelder","year":"2009","journal-title":"Proc. Natl. Acad. Sci."},{"key":"10.1016\/j.bbagen.2016.04.024_bb0025","doi-asserted-by":"crossref","first-page":"173","DOI":"10.1016\/j.bbapap.2005.03.010","article-title":"Protein\u2013water displacement distributions","volume":"1749","author":"Doster","year":"2005","journal-title":"Biochim. Biophys. Acta"},{"key":"10.1016\/j.bbagen.2016.04.024_bb0030","doi-asserted-by":"crossref","first-page":"754","DOI":"10.1038\/337754a0","article-title":"Dynamical transition of myoglobin revealed by inelastic neutron-scattering","volume":"337","author":"Doster","year":"1989","journal-title":"Nature"},{"key":"10.1016\/j.bbagen.2016.04.024_bb0035","doi-asserted-by":"crossref","first-page":"916","DOI":"10.1016\/j.bbapap.2011.05.005","article-title":"Coupling of protein and environment fluctuations","volume":"1814","author":"Young","year":"2011","journal-title":"Biochim. Biophys. Acta"},{"key":"10.1016\/j.bbagen.2016.04.024_bb0040","doi-asserted-by":"crossref","first-page":"81","DOI":"10.1016\/j.molstruc.2009.12.020","article-title":"On the behaviour of water hydrogen bonds at biomolecular sites: dependences on temperature and on network dimensionality","volume":"972","author":"Russo","year":"2010","journal-title":"J. Mol. Struct."},{"key":"10.1016\/j.bbagen.2016.04.024_bb0045","doi-asserted-by":"crossref","first-page":"064104","DOI":"10.1088\/0953-8984\/24\/6\/064104","article-title":"Common features in the microscopic dynamics of hydration water on organic and inorganic surfaces","volume":"24","author":"Mamontov","year":"2012","journal-title":"J. Phys. Condens. Matter"},{"key":"10.1016\/j.bbagen.2016.04.024_bb0050","doi-asserted-by":"crossref","first-page":"2504","DOI":"10.1016\/S0006-3495(98)77694-5","article-title":"Enzyme activity below the dynamical transition at 220K","volume":"75","author":"Daniel","year":"1998","journal-title":"Biophys. J."},{"key":"10.1016\/j.bbagen.2016.04.024_bb0055","doi-asserted-by":"crossref","first-page":"2184","DOI":"10.1016\/S0006-3495(99)77058-X","article-title":"Enzyme dynamics and activity: time-scale dependence of dynamical transitions in glutamate dehydrogenase solution","volume":"77","author":"Daniel","year":"1999","journal-title":"Biophys. J."},{"key":"10.1016\/j.bbagen.2016.04.024_bb0060","doi-asserted-by":"crossref","first-page":"1043","DOI":"10.1016\/S0006-3495(99)77269-3","article-title":"Harmonic behavior of trehalose-coated carbon-monoxy-myoglobin at high temperature","volume":"76","author":"Cordone","year":"1999","journal-title":"Biophys. J."},{"key":"10.1016\/j.bbagen.2016.04.024_bb0065","doi-asserted-by":"crossref","first-page":"278","DOI":"10.1016\/S0167-4838(00)00081-9","article-title":"Enzyme activity down to \u2212100 degrees C","volume":"1480","author":"Bragger","year":"2000","journal-title":"Biochim. Biophys. Acta"},{"key":"10.1016\/j.bbagen.2016.04.024_bb0070","doi-asserted-by":"crossref","first-page":"355","DOI":"10.1042\/bj3460355","article-title":"Enzyme activity and dynamics: xylanase activity in the absence of fast anharmonic dynamics","volume":"346","author":"Dunn","year":"2000","journal-title":"Biochem. J."},{"key":"10.1016\/j.bbagen.2016.04.024_bb0075","doi-asserted-by":"crossref","first-page":"97","DOI":"10.1016\/S0165-022X(99)00053-6","article-title":"Cryosolvents useful for protein and enzyme studies below \u2212100 degrees C","volume":"42","author":"Reat","year":"2000","journal-title":"J. Biochem. Biophys. Methods"},{"key":"10.1016\/j.bbagen.2016.04.024_bb0080","doi-asserted-by":"crossref","first-page":"9961","DOI":"10.1073\/pnas.97.18.9961","article-title":"Solvent dependence of dynamic transition in protein solutions","volume":"97","author":"Reat","year":"2000","journal-title":"Proc. Natl. Acad. Sci."},{"key":"10.1016\/j.bbagen.2016.04.024_bb0085","doi-asserted-by":"crossref","first-page":"2728","DOI":"10.1016\/S0006-3495(00)76511-8","article-title":"Molecular dynamics of solid-state lysozyme as affected by glycerol and water: a neutron scattering study","volume":"79","author":"Tsai","year":"2000","journal-title":"Biophys. J."},{"key":"10.1016\/j.bbagen.2016.04.024_bb0090","doi-asserted-by":"crossref","first-page":"2339","DOI":"10.1016\/S0006-3495(01)75880-8","article-title":"The inverse relationship between protein dynamics and thermal stability","volume":"81","author":"Tsai","year":"2001","journal-title":"Biophys. J."},{"key":"10.1016\/j.bbagen.2016.04.024_bb0095","doi-asserted-by":"crossref","first-page":"1157","DOI":"10.1016\/S0006-3495(02)75239-9","article-title":"Effect of the environment on the protein dynamical transition: a neutron scattering study","volume":"83","author":"Paciaroni","year":"2002","journal-title":"Biophys. J."},{"key":"10.1016\/j.bbagen.2016.04.024_bb0100","doi-asserted-by":"crossref","first-page":"397","DOI":"10.1016\/S0301-0104(03)00102-2","article-title":"Protein dynamics on the picosecond timescale as affected by the environment: a quasielastic neutron scattering study","volume":"292","author":"Paciaroni","year":"2003","journal-title":"Chem. Phys."},{"key":"10.1016\/j.bbagen.2016.04.024_bb0105","doi-asserted-by":"crossref","first-page":"3152","DOI":"10.1016\/S0006-3495(04)74363-5","article-title":"The influence of solvent composition on global dynamics of human butyrylcholinesterase powders: a neutron-scattering study","volume":"86","author":"Gabel","year":"2004","journal-title":"Biophys. J."},{"key":"10.1016\/j.bbagen.2016.04.024_bb0110","doi-asserted-by":"crossref","first-page":"3836","DOI":"10.1529\/biophysj.103.035519","article-title":"Fast dynamics and stabilization of proteins: binary glasses of trehalose and glycerol","volume":"86","author":"Cicerone","year":"2004","journal-title":"Biophys. J."},{"key":"10.1016\/j.bbagen.2016.04.024_bb0115","doi-asserted-by":"crossref","first-page":"1388","DOI":"10.1039\/B416103C","article-title":"Temperature and timescale dependence of protein dynamics in methanol: water mixtures","volume":"7","author":"Tournier","year":"2005","journal-title":"Phys. Chem. Chem. Phys."},{"key":"10.1016\/j.bbagen.2016.04.024_bb0120","doi-asserted-by":"crossref","first-page":"289","DOI":"10.1529\/biophysj.106.081752","article-title":"Controlling the protein dynamical transition with sugar-based bioprotectant matrices: a neutron scattering study","volume":"91","author":"Cornicchi","year":"2006","journal-title":"Biophys. J."},{"key":"10.1016\/j.bbagen.2016.04.024_bb0125","doi-asserted-by":"crossref","first-page":"200","DOI":"10.1016\/j.chemphys.2007.08.001","article-title":"The impact of kosmotropes and chaotropes on bulk and hydration shell water dynamics in a model peptide solution","volume":"345","author":"Russo","year":"2008","journal-title":"Chem. Phys."},{"key":"10.1016\/j.bbagen.2016.04.024_bb0130","doi-asserted-by":"crossref","first-page":"205101","DOI":"10.1063\/1.3138765","article-title":"Dynamics of a protein and its surrounding environment: a quasielastic neutron scattering study of myoglobin in water and glycerol mixtures","volume":"130","author":"Jansson","year":"2009","journal-title":"J. Chem. Phys."},{"key":"10.1016\/j.bbagen.2016.04.024_bb0135","doi-asserted-by":"crossref","first-page":"184512","DOI":"10.1063\/1.3407428","article-title":"Study of the relaxational and vibrational dynamics of bioprotectant glass-forming mixtures by neutron scattering and molecular dynamics simulation","volume":"132","author":"Magazu","year":"2010","journal-title":"J. Chem. Phys."},{"key":"10.1016\/j.bbagen.2016.04.024_bb0140","doi-asserted-by":"crossref","first-page":"207","DOI":"10.1007\/s10867-009-9177-5","article-title":"Study of solvent\u2013protein coupling effects by neutron scattering","volume":"36","author":"Varga","year":"2010","journal-title":"J. Biol. Phys."},{"key":"10.1016\/j.bbagen.2016.04.024_bb0145","doi-asserted-by":"crossref","first-page":"380","DOI":"10.1021\/jz201435q","article-title":"Apparent decoupling of the dynamics of a protein from the dynamics of its aqueous solvent","volume":"3","author":"Chu","year":"2012","journal-title":"J. Phys. Chem. Lett."},{"key":"10.1016\/j.bbagen.2016.04.024_bb0150","doi-asserted-by":"crossref","first-page":"11573","DOI":"10.1039\/c2cp41443k","article-title":"Water\u2013protein dynamic coupling and new opportunities for probing it at low to physiological temperatures in aqueous solutions","volume":"14","author":"Mamontov","year":"2012","journal-title":"Phys. Chem. Chem. Phys."},{"key":"10.1016\/j.bbagen.2016.04.024_bb0155","doi-asserted-by":"crossref","first-page":"5336","DOI":"10.1039\/c3sm50492a","article-title":"Solvent effects on protein fast dynamics: implications for biopreservation","volume":"9","author":"Garcia Sakai","year":"2013","journal-title":"Soft Matter"},{"key":"10.1016\/j.bbagen.2016.04.024_bb0160","doi-asserted-by":"crossref","first-page":"291","DOI":"10.1007\/s10867-009-9184-6","article-title":"Mean-squared atomic displacements in hydrated lysozyme, native and denatured","volume":"36","author":"Mamontov","year":"2010","journal-title":"J. Biol. Phys."},{"key":"10.1016\/j.bbagen.2016.04.024_bb0165","doi-asserted-by":"crossref","first-page":"148","DOI":"10.1021\/tx00020a004","article-title":"The molecular mechanism of the carbon disulfide mediated cross-linking of proteins","volume":"4","author":"Amarnath","year":"1991","journal-title":"Chem. Res. Toxicol."},{"key":"10.1016\/j.bbagen.2016.04.024_bb0170","doi-asserted-by":"crossref","first-page":"254","DOI":"10.1021\/tx00026a017","article-title":"Covalent cross-linking of proteins by carbon disulfide","volume":"5","author":"Valentine","year":"1992","journal-title":"Chem. Res. Toxicol."},{"key":"10.1016\/j.bbagen.2016.04.024_bb0175","doi-asserted-by":"crossref","first-page":"71","DOI":"10.1006\/taap.1993.1130","article-title":"Covalent cross-linking of erythrocyte spectrin by carbon disulfide in vivo","volume":"121","author":"Valentine","year":"1993","journal-title":"Toxicol. Appl. Pharmacol."},{"key":"10.1016\/j.bbagen.2016.04.024_bb0180","doi-asserted-by":"crossref","first-page":"96","DOI":"10.1021\/tx00043a013","article-title":"Carbon disulfide mediated protein cross-linking by N,N-diethyldithiocarbamate","volume":"8","author":"Valentine","year":"1995","journal-title":"Chem. Res. Toxicol."},{"key":"10.1016\/j.bbagen.2016.04.024_bb0185","doi-asserted-by":"crossref","first-page":"95","DOI":"10.1006\/taap.1996.8028","article-title":"CS2-mediated cross-linking of erythrocyte spectrin and neurofilament protein: dose response and temporal relationship to the formation of axonal swellings","volume":"142","author":"Valentine","year":"1997","journal-title":"Toxicol. Appl. Pharmacol."},{"key":"10.1016\/j.bbagen.2016.04.024_bb0190","doi-asserted-by":"crossref","first-page":"7328","DOI":"10.1021\/ja050432f","article-title":"Dithiocarbamate assembly on gold","volume":"127","author":"Zhao","year":"2005","journal-title":"J. Am. Chem. Soc."},{"key":"10.1016\/j.bbagen.2016.04.024_bb0195","doi-asserted-by":"crossref","first-page":"8660","DOI":"10.1021\/la801254b","article-title":"Assembly of dithiocarbamate-anchored monolayers on gold surfaces in aqueous solutions","volume":"24","author":"Zhu","year":"2008","journal-title":"Langmuir"},{"key":"10.1016\/j.bbagen.2016.04.024_bb0200","doi-asserted-by":"crossref","first-page":"2904","DOI":"10.1021\/la902839r","article-title":"Kinetic dispersion in redox-active dithiocarbamate monolayers","volume":"26","author":"Eckermann","year":"2010","journal-title":"Langmuir"},{"key":"10.1016\/j.bbagen.2016.04.024_bb0205","doi-asserted-by":"crossref","first-page":"17718","DOI":"10.1021\/la303032f","article-title":"Antibody oriented immobilization on gold using the reaction between carbon disulfide and amine groups and its application in immumosensing","volume":"28","author":"Niu","year":"2012","journal-title":"Langmuir"},{"key":"10.1016\/j.bbagen.2016.04.024_bb0210","doi-asserted-by":"crossref","first-page":"085109","DOI":"10.1063\/1.3626214","article-title":"A time-of-flight backscattering spectrometer at the spallation neutron source, BASIS","volume":"82","author":"Mamontov","year":"2011","journal-title":"Rev. Sci. Instrum."},{"key":"10.1016\/j.bbagen.2016.04.024_bb0215","doi-asserted-by":"crossref","first-page":"1321","DOI":"10.1016\/j.bpj.2009.12.4284","article-title":"Dynamics of biological macromolecules: not a simple slaving by hydration water","volume":"98","author":"Khodadadi","year":"2010","journal-title":"Biophys. J."},{"key":"10.1016\/j.bbagen.2016.04.024_bb0220","doi-asserted-by":"crossref","first-page":"3","DOI":"10.1016\/j.bbapap.2009.06.019","article-title":"The protein\u2013solvent glass transition","volume":"1804","author":"Doster","year":"2010","journal-title":"Biochim. Biophys. Acta"},{"key":"10.1016\/j.bbagen.2016.04.024_bb0225","doi-asserted-by":"crossref","first-page":"1566","DOI":"10.1016\/j.bpj.2012.08.046","article-title":"Dynamics of protein and its hydration water: neutron scattering studies on fully deuterated GFP","volume":"103","author":"Nickels","year":"2012","journal-title":"Biophys. J."},{"key":"10.1016\/j.bbagen.2016.04.024_bb0230","doi-asserted-by":"crossref","first-page":"12","DOI":"10.1016\/j.chemphys.2013.02.026","article-title":"Temperature dependence of the internal dynamics of a protein in an aqueous solvent: decoupling from the solvent viscosity","volume":"424","author":"Mamontov","year":"2013","journal-title":"Chem. Phys."},{"key":"10.1016\/j.bbagen.2016.04.024_bb0235","doi-asserted-by":"crossref","first-page":"572","DOI":"10.1038\/284572a0","article-title":"Correlation of IR spectroscopic, heat capacity, diamagnetic susceptibility and enzymatic measurements on lysozyme powder","volume":"284","author":"Careri","year":"1980","journal-title":"Nature"},{"key":"10.1016\/j.bbagen.2016.04.024_bb0240","doi-asserted-by":"crossref","first-page":"7088","DOI":"10.1073\/pnas.81.22.7088","article-title":"A consistent picture of protein dynamics","volume":"81","author":"Parak","year":"1984","journal-title":"Proc. Natl. Acad. Sci."},{"key":"10.1016\/j.bbagen.2016.04.024_bb0245","doi-asserted-by":"crossref","first-page":"423","DOI":"10.1038\/357423a0","article-title":"Crystalline ribonuclease-A loses function below the dynamic transition at 220K","volume":"357","author":"Rasmussen","year":"1992","journal-title":"Nature"},{"key":"10.1016\/j.bbagen.2016.04.024_bb0250","doi-asserted-by":"crossref","first-page":"9668","DOI":"10.1073\/pnas.90.20.9668","article-title":"Thermal motions and function of bacteriorhodopsin in purple membranes \u2014 effects of temperature and hydration studied by neutron-scattering","volume":"90","author":"Ferrand","year":"1993","journal-title":"Proc. Natl. Acad. Sci."},{"key":"10.1016\/j.bbagen.2016.04.024_bb0255","doi-asserted-by":"crossref","first-page":"205","DOI":"10.1038\/35004622","article-title":"Ligand binding and conformational motions in myoglobin","volume":"404","author":"Ostermann","year":"2000","journal-title":"Nature"},{"key":"10.1016\/j.bbagen.2016.04.024_bb0260","doi-asserted-by":"crossref","first-page":"241","DOI":"10.1038\/35051719","article-title":"Improving enzymes by using them in organic solvents","volume":"409","author":"Klibanov","year":"2001","journal-title":"Nature"},{"key":"10.1016\/j.bbagen.2016.04.024_bb0265","doi-asserted-by":"crossref","first-page":"1287","DOI":"10.1098\/rstb.2004.1505","article-title":"What can we learn by studying enzymes in non-aqueous media?","volume":"359","author":"Halling","year":"2004","journal-title":"Philos. Trans. R. Soc. Lond. B"},{"key":"10.1016\/j.bbagen.2016.04.024_bb0270","doi-asserted-by":"crossref","first-page":"1299","DOI":"10.1098\/rstb.2004.1506","article-title":"Characteristics of nearly dry enzymes in organic solvents: implications for biocatalysis in the absence of water","volume":"359","author":"Clark","year":"2004","journal-title":"Philos. Trans. R. Soc. Lond. B"},{"key":"10.1016\/j.bbagen.2016.04.024_bb0275","doi-asserted-by":"crossref","first-page":"3232","DOI":"10.1021\/acs.jpcb.6b00866","article-title":"Protein-style dynamical transition in a non-biological polymer and a non-aqueous solvent","volume":"120","author":"Mamontov","year":"2016","journal-title":"J. Phys. Chem. B"}],"container-title":["Biochimica et Biophysica Acta (BBA) - General Subjects"],"original-title":[],"language":"en","link":[{"URL":"https:\/\/api.elsevier.com\/content\/article\/PII:S0304416516301301?httpAccept=text\/xml","content-type":"text\/xml","content-version":"vor","intended-application":"text-mining"},{"URL":"https:\/\/api.elsevier.com\/content\/article\/PII:S0304416516301301?httpAccept=text\/plain","content-type":"text\/plain","content-version":"vor","intended-application":"text-mining"}],"deposited":{"date-parts":[[2025,10,5]],"date-time":"2025-10-05T03:52:14Z","timestamp":1759636334000},"score":1,"resource":{"primary":{"URL":"https:\/\/linkinghub.elsevier.com\/retrieve\/pii\/S0304416516301301"}},"subtitle":[],"short-title":[],"issued":{"date-parts":[[2017,1]]},"references-count":55,"journal-issue":{"issue":"1","published-print":{"date-parts":[[2017,1]]}},"alternative-id":["S0304416516301301"],"URL":"https:\/\/doi.org\/10.1016\/j.bbagen.2016.04.024","relation":{},"ISSN":["0304-4165"],"issn-type":[{"type":"print","value":"0304-4165"}],"subject":[],"published":{"date-parts":[[2017,1]]},"assertion":[{"value":"Elsevier","name":"publisher","label":"This article is maintained by"},{"value":"Microscopic relaxations in a protein sustained down to 160K in a non-glass forming organic solvent","name":"articletitle","label":"Article Title"},{"value":"Biochimica et Biophysica Acta (BBA) - General Subjects","name":"journaltitle","label":"Journal Title"},{"value":"https:\/\/doi.org\/10.1016\/j.bbagen.2016.04.024","name":"articlelink","label":"CrossRef DOI link to publisher maintained version"},{"value":"article","name":"content_type","label":"Content Type"},{"value":"\u00a9 2016 Elsevier B.V. All rights reserved.","name":"copyright","label":"Copyright"}]}}