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                    "firstName": "Dorota",
                    "lastName": "Ksiazek"
                },
                {
                    "creatorType": "author",
                    "firstName": "M. Kamran",
                    "lastName": "Azim"
                },
                {
                    "creatorType": "author",
                    "firstName": "Pawel",
                    "lastName": "Smialowski"
                },
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                    "creatorType": "author",
                    "firstName": "Nediljko",
                    "lastName": "Budisa"
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                    "creatorType": "author",
                    "firstName": "Tad A.",
                    "lastName": "Holak"
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            ],
            "abstractNote": "Green fluorescent protein and its mutants have become valuable tools in molecular biology. They also provide systems rich in photophysical and photochemical phenomena of which an understanding is important for the development of new and optimized variants of GFP. Surprisingly, not a single NMR study has been reported on GFPs until now, possibly because of their high tendency to aggregate. Here, we report the 19F nuclear magnetic resonance (NMR) studies on mutants of the green fluorescent protein (GFP) and cyan fluorescent protein (CFP) labeled with fluorinated tryptophans that enabled the detection of slow molecular motions in these proteins. The concerted use of dynamic NMR and 19F relaxation measurements, supported by temperature, concentration- and folding-dependent experiments provides direct evidence for the existence of a slow exchange process between two different conformational states of CFP. 19F NMR relaxation and line shape analysis indicate that the time scale of exchange between these states is in the range of 1.21.4 ms. Thermodynamic analysis revealed a difference in enthalpy H0 = (18.2 3.8) kJ/mol and entropy TS0 = (19.6 1.2) kJ/mol at T = 303 K for the two states involved in the exchange process, indicating an entropyenthalpy compensation. The free energy of activation was estimated to be approximately 60 kJ/mol. Exchange between two conformations, either of the chromophore itself or more likely of the closely related histidine 148, is suggested to be the structural process underlying the conformational mobility of GFPs. The possibility to generate a series of single-atom exchanges (\"atomic mutations\") like H F in this study offers a useful approach for characterizing and quantifying dynamic processes in proteins by NMR.",
            "publicationTitle": "Journal of the American Chemical Society",
            "publisher": "",
            "place": "",
            "date": "juillet 1, 2002",
            "volume": "124",
            "issue": "27",
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            "partNumber": "",
            "partTitle": "",
            "pages": "7932-7942",
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            "seriesTitle": "",
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            "journalAbbreviation": "J. Am. Chem. Soc.",
            "DOI": "10.1021/ja0257725",
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            "title": "Relation between pH, structure, and absorption spectrum of Cerulean: A study by molecular dynamics and TD DFT calculations",
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                    "firstName": "Germain",
                    "lastName": "Vallverdu"
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                    "firstName": "Fabienne",
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                    "lastName": "Ridard"
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                    "firstName": "Bernard",
                    "lastName": "Lévy"
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            "abstractNote": "",
            "publicationTitle": "Proteins: Structure, Function, and Bioinformatics",
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                    "creatorType": "author",
                    "firstName": "Lars V.",
                    "lastName": "Schäfer"
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                    "firstName": "Gerrit",
                    "lastName": "Groenhof"
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                    "firstName": "Astrid R.",
                    "lastName": "Klingen"
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                    "firstName": "G. Matthias",
                    "lastName": "Ullmann"
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                    "creatorType": "author",
                    "firstName": "Martial",
                    "lastName": "Boggio-Pasqua"
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                    "creatorType": "author",
                    "firstName": "Michael A.",
                    "lastName": "Robb"
                },
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                    "creatorType": "author",
                    "firstName": "Helmut",
                    "lastName": "Grubmüller"
                }
            ],
            "abstractNote": "",
            "publicationTitle": "Angewandte Chemie International Edition",
            "publisher": "",
            "place": "",
            "date": "janvier 15, 2007",
            "volume": "46",
            "issue": "4",
            "section": "",
            "partNumber": "",
            "partTitle": "",
            "pages": "530-536",
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            "journalAbbreviation": "Angewandte Chemie International Edition",
            "DOI": "10.1002/anie.200602315",
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            "url": "http://onlinelibrary.wiley.com/doi/10.1002/anie.200602315/abstract",
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            "shortTitle": "Photoswitching of the Fluorescent Protein asFP595",
            "language": "en",
            "libraryCatalog": "Wiley Online Library",
            "callNumber": "",
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            "extra": "",
            "tags": [
                {
                    "tag": "absorption spectroscopy",
                    "type": 1
                },
                {
                    "tag": "isomerization",
                    "type": 1
                },
                {
                    "tag": "molecular dynamics",
                    "type": 1
                },
                {
                    "tag": "proteins",
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            "creatorSummary": "Moors et al.",
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            "version": 2,
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            "title": "How Is cis−trans Isomerization Controlled in Dronpa Mutants? A Replica Exchange Molecular Dynamics Study",
            "creators": [
                {
                    "creatorType": "author",
                    "firstName": "Samuel L. C.",
                    "lastName": "Moors"
                },
                {
                    "creatorType": "author",
                    "firstName": "Servaas",
                    "lastName": "Michielssens"
                },
                {
                    "creatorType": "author",
                    "firstName": "Cristina",
                    "lastName": "Flors"
                },
                {
                    "creatorType": "author",
                    "firstName": "Peter",
                    "lastName": "Dedecker"
                },
                {
                    "creatorType": "author",
                    "firstName": "Johan",
                    "lastName": "Hofkens"
                },
                {
                    "creatorType": "author",
                    "firstName": "Arnout",
                    "lastName": "Ceulemans"
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            ],
            "abstractNote": "The reversibly photoactivatable green fluorescent protein analog Dronpa holds great promise as a marker for various new cellular imaging applications. Using a replica exchange method which combines both Hamiltonian and temperature exchanges, the ground-state dynamics of Dronpa and two mutants with increased switching kinetics, Val157Gly and Met159Thr, were compared. The dominant chromophore state was found to be the cis isomer in all three proteins. The simulation data suggest that both mutations strongly increase the chromophore flexibility and cis?trans isomerization rate. We identify three key amino acids, Val157, Met159, and Phe173, which are able to impede the bottom hula-twist transition path, depending on their position and rotameric state. We believe our insights will help to understand the switching process and provide useful information for the design of new variants with improved fluorescence properties.",
            "publicationTitle": "Journal of Chemical Theory and Computation",
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            "date": "juin 1, 2008",
            "volume": "4",
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            "PMID": "",
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            "shortTitle": "How Is cis−trans Isomerization Controlled in Dronpa Mutants?",
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]