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  • 1
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    Unknown
    American Association for the Advancement of Science (AAAS)
    Publication Date: 1999-04-30
    Description: The ability of the GroEL chaperonin to unfold a protein trapped in a misfolded condition was detected and studied by hydrogen exchange. The GroEL-induced unfolding of its substrate protein is only partial, requires the complete chaperonin system, and is accomplished within the 13 seconds required for a single system turnover. The binding of nucleoside triphosphate provides the energy for a single unfolding event; multiple turnovers require adenosine triphosphate hydrolysis. The substrate protein is released on each turnover even if it has not yet refolded to the native state. These results suggest that GroEL helps partly folded but blocked proteins to fold by causing them first to partially unfold. The structure of GroEL seems well suited to generate the nonspecific mechanical stretching force required for forceful protein unfolding.〈br /〉〈br /〉〈a href="https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3427652/" target="_blank"〉〈img src="https://static.pubmed.gov/portal/portal3rc.fcgi/4089621/img/3977009" border="0"〉〈/a〉   〈a href="https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3427652/" target="_blank"〉This paper as free author manuscript - peer-reviewed and accepted for publication〈/a〉〈br /〉〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Shtilerman, M -- Lorimer, G H -- Englander, S W -- GM31847/GM/NIGMS NIH HHS/ -- R01 GM031847/GM/NIGMS NIH HHS/ -- New York, N.Y. -- Science. 1999 Apr 30;284(5415):822-5.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉The Johnson Research Foundation, Department of Biochemistry and Biophysics, University of Pennsylvania School of Medicine, Philadelphia, PA 19104, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/10221918" target="_blank"〉PubMed〈/a〉
    Keywords: Adenosine Triphosphate/metabolism ; Adenylyl Imidodiphosphate/metabolism ; Binding Sites ; Chaperonin 10/chemistry/metabolism/physiology ; Chaperonin 60/chemistry/metabolism/*physiology ; Hydrogen/chemistry/metabolism ; Models, Molecular ; Protein Binding ; Protein Conformation ; *Protein Folding ; Protein Structure, Secondary ; Ribulose-Bisphosphate Carboxylase/*chemistry/metabolism
    Print ISSN: 0036-8075
    Electronic ISSN: 1095-9203
    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
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  • 2
    Publication Date: 1992-06-19
    Description: The inability to localize and measure the free energy of protein structure and structure change severely limits protein structure-function investigations. The local unfolding model for protein hydrogen exchange quantitatively related the free energy of local structural stability with the hydrogen exchange rate of concerted sets of structurally related protons. In tests with a number of modified hemoglobin forms, the loss in structural free energy obtained locally from hydrogen exchange results matches the loss in allosteric free energy measured globally by oxygen-binding and subunit dissociation experiments.〈br /〉〈br /〉〈a href="https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3562468/" target="_blank"〉〈img src="https://static.pubmed.gov/portal/portal3rc.fcgi/4089621/img/3977009" border="0"〉〈/a〉   〈a href="https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3562468/" target="_blank"〉This paper as free author manuscript - peer-reviewed and accepted for publication〈/a〉〈br /〉〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Englander, S W -- Englander, J J -- McKinnie, R E -- Ackers, G K -- Turner, G J -- Westrick, J A -- Gill, S J -- R01 GM031847/GM/NIGMS NIH HHS/ -- New York, N.Y. -- Science. 1992 Jun 19;256(5064):1684-7.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Biochemistry and Biophysics, University of Pennsylvania, Philadelphia 19104-6059.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/1609279" target="_blank"〉PubMed〈/a〉
    Keywords: Allosteric Regulation ; Allosteric Site ; Energy Transfer ; Hemoglobins/*metabolism ; Hydrogen/*metabolism ; Ion Exchange ; Molecular Structure
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    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
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  • 3
    Publication Date: 1990-08-17
    Description: The interaction of a protein antigen, horse cytochrome c (cyt c), with a monoclonal antibody has been studied by hydrogen-deuterium (H-D) exchange labeling and two-dimensional nuclear magnetic resonance (2D NMR) methods. The H-exchange rate of residues in three discontiguous regions of the cyt c polypeptide backbone was slowed by factors up to 340-fold in the antibody-antigen complex compared with free cyt c. The protected residues, 36 to 38, 59, 60, 64 to 67, 100, and 101, and their hydrogen-bond acceptors, are brought together in the three-dimensional structure to form a contiguous, largely exposed protein surface with an area of about 750 square angstroms. The interaction site determined in this way is consistent with prior epitope mapping studies and includes several residues that were not previously identified. The hydrogen exchange labeling approach can be used to map binding sites on small proteins in antibody-antigen complexes and may be applicable to protein-protein and protein-ligand interactions in general.〈br /〉〈br /〉〈a href="https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3432411/" target="_blank"〉〈img src="https://static.pubmed.gov/portal/portal3rc.fcgi/4089621/img/3977009" border="0"〉〈/a〉   〈a href="https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3432411/" target="_blank"〉This paper as free author manuscript - peer-reviewed and accepted for publication〈/a〉〈br /〉〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Paterson, Y -- Englander, S W -- Roder, H -- GM 31847/GM/NIGMS NIH HHS/ -- GM 35926/GM/NIGMS NIH HHS/ -- R01 GM031847/GM/NIGMS NIH HHS/ -- S07-RR-05415-28/RR/NCRR NIH HHS/ -- New York, N.Y. -- Science. 1990 Aug 17;249(4970):755-9.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Microbiology, University of Pennsylvania, Philadelphia 19104.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/1697101" target="_blank"〉PubMed〈/a〉
    Keywords: Antibodies, Monoclonal/immunology/metabolism ; Antigen-Antibody Complex ; *Binding Sites, Antibody ; Chemical Phenomena ; Chemistry ; Cytochrome c Group/*immunology ; Deuterium ; Epitopes/immunology ; Hydrogen/*metabolism ; Hydrogen Bonding ; Kinetics ; *Magnetic Resonance Spectroscopy ; Molecular Structure ; Protein Conformation
    Print ISSN: 0036-8075
    Electronic ISSN: 1095-9203
    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
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  • 4
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    Unknown
    American Association for the Advancement of Science (AAAS)
    Publication Date: 1995-07-14
    Description: The hydrogen exchange behavior of native cytochrome c in low concentrations of denaturant reveals a sequence of metastable, partially unfolded forms that occupy free energy levels reaching up to the fully unfolded state. The step from one form to another is accomplished by the unfolding of one or more cooperative units of structure. The cooperative units are entire omega loops or mutually stabilizing pairs of whole helices and loops. The partially unfolded forms detected by hydrogen exchange appear to represent the major intermediates in the reversible, dynamic unfolding reactions that occur even at native conditions and thus may define the major pathway for cytochrome c folding.〈br /〉〈br /〉〈a href="https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3432310/" target="_blank"〉〈img src="https://static.pubmed.gov/portal/portal3rc.fcgi/4089621/img/3977009" border="0"〉〈/a〉   〈a href="https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3432310/" target="_blank"〉This paper as free author manuscript - peer-reviewed and accepted for publication〈/a〉〈br /〉〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Bai, Y -- Sosnick, T R -- Mayne, L -- Englander, S W -- GM31847/GM/NIGMS NIH HHS/ -- R01 GM031847/GM/NIGMS NIH HHS/ -- New York, N.Y. -- Science. 1995 Jul 14;269(5221):192-7.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Johnson Research Foundation, Department of Biochemistry and Biophysics, School of Medicine, University of Pennsylvania, Philadelphia 19104-6059, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/7618079" target="_blank"〉PubMed〈/a〉
    Keywords: Cytochrome c Group/*chemistry ; Guanidine ; Guanidines/chemistry ; Hydrogen/*chemistry ; Hydrogen Bonding ; Protein Conformation ; Protein Denaturation ; *Protein Folding ; Protein Structure, Secondary ; Temperature ; Thermodynamics
    Print ISSN: 0036-8075
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    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
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  • 5
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    Unknown
    American Association for the Advancement of Science (AAAS)
    Publication Date: 1993-11-05
    Description: 〈br /〉〈br /〉〈a href="https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3432308/" target="_blank"〉〈img src="https://static.pubmed.gov/portal/portal3rc.fcgi/4089621/img/3977009" border="0"〉〈/a〉   〈a href="https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3432308/" target="_blank"〉This paper as free author manuscript - peer-reviewed and accepted for publication〈/a〉〈br /〉〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Englander, S W -- R01 GM031847/GM/NIGMS NIH HHS/ -- New York, N.Y. -- Science. 1993 Nov 5;262(5135):848-9.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Biochemistry and Biophysics, University of Pennsylvania School of Medicine, Philadelphia 19104-6059.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/8235606" target="_blank"〉PubMed〈/a〉
    Keywords: Hydrogen-Ion Concentration ; Magnetic Resonance Spectroscopy ; Mass Spectrometry ; Models, Molecular ; Muramidase/*chemistry ; Myoglobin/*chemistry ; Protein Conformation ; *Protein Folding ; Ribonuclease, Pancreatic/*chemistry
    Print ISSN: 0036-8075
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    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
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  • 6
    Publication Date: 2010-05-08
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Gleick, P H -- Adams, R M -- Amasino, R M -- Anders, E -- Anderson, D J -- Anderson, W W -- Anselin, L E -- Arroyo, M K -- Asfaw, B -- Ayala, F J -- Bax, A -- Bebbington, A J -- Bell, G -- Bennett, M V L -- Bennetzen, J L -- Berenbaum, M R -- Berlin, O B -- Bjorkman, P J -- Blackburn, E -- Blamont, J E -- Botchan, M R -- Boyer, J S -- Boyle, E A -- Branton, D -- Briggs, S P -- Briggs, W R -- Brill, W J -- Britten, R J -- Broecker, W S -- Brown, J H -- Brown, P O -- Brunger, A T -- Cairns, J Jr -- Canfield, D E -- Carpenter, S R -- Carrington, J C -- Cashmore, A R -- Castilla, J C -- Cazenave, A -- Chapin, F S 3rd -- Ciechanover, A J -- Clapham, D E -- Clark, W C -- Clayton, R N -- Coe, M D -- Conwell, E M -- Cowling, E B -- Cowling, R M -- Cox, C S -- Croteau, R B -- Crothers, D M -- Crutzen, P J -- Daily, G C -- Dalrymple, G B -- Dangl, J L -- Darst, S A -- Davies, D R -- Davis, M B -- De Camilli, P V -- Dean, C -- DeFries, R S -- Deisenhofer, J -- Delmer, D P -- DeLong, E F -- DeRosier, D J -- Diener, T O -- Dirzo, R -- Dixon, J E -- Donoghue, M J -- Doolittle, R F -- Dunne, T -- Ehrlich, P R -- Eisenstadt, S N -- Eisner, T -- Emanuel, K A -- Englander, S W -- Ernst, W G -- Falkowski, P G -- Feher, G -- Ferejohn, J A -- Fersht, A -- Fischer, E H -- Fischer, R -- Flannery, K V -- Frank, J -- Frey, P A -- Fridovich, I -- Frieden, C -- Futuyma, D J -- Gardner, W R -- Garrett, C J R -- Gilbert, W -- Goldberg, R B -- Goodenough, W H -- Goodman, C S -- Goodman, M -- Greengard, P -- Hake, S -- Hammel, G -- Hanson, S -- Harrison, S C -- Hart, S R -- Hartl, D L -- Haselkorn, R -- Hawkes, K -- Hayes, J M -- Hille, B -- Hokfelt, T -- House, J S -- Hout, M -- Hunten, D M -- Izquierdo, I A -- Jagendorf, A T -- Janzen, D H -- Jeanloz, R -- Jencks, C S -- Jury, W A -- Kaback, H R -- Kailath, T -- Kay, P -- Kay, S A -- Kennedy, D -- Kerr, A -- Kessler, R C -- Khush, G S -- Kieffer, S W -- Kirch, P V -- Kirk, K -- Kivelson, M G -- Klinman, J P -- Klug, A -- Knopoff, L -- Kornberg, H -- Kutzbach, J E -- Lagarias, J C -- Lambeck, K -- Landy, A -- Langmuir, C H -- Larkins, B A -- Le Pichon, X T -- Lenski, R E -- Leopold, E B -- Levin, S A -- Levitt, M -- Likens, G E -- Lippincott-Schwartz, J -- Lorand, L -- Lovejoy, C O -- Lynch, M -- Mabogunje, A L -- Malone, T F -- Manabe, S -- Marcus, J -- Massey, D S -- McWilliams, J C -- Medina, E -- Melosh, H J -- Meltzer, D J -- Michener, C D -- Miles, E L -- Mooney, H A -- Moore, P B -- Morel, F M M -- Mosley-Thompson, E S -- Moss, B -- Munk, W H -- Myers, N -- Nair, G B -- Nathans, J -- Nester, E W -- Nicoll, R A -- Novick, R P -- O'Connell, J F -- Olsen, P E -- Opdyke, N D -- Oster, G F -- Ostrom, E -- Pace, N R -- Paine, R T -- Palmiter, R D -- Pedlosky, J -- Petsko, G A -- Pettengill, G H -- Philander, S G -- Piperno, D R -- Pollard, T D -- Price, P B Jr -- Reichard, P A -- Reskin, B F -- Ricklefs, R E -- Rivest, R L -- Roberts, J D -- Romney, A K -- Rossmann, M G -- Russell, D W -- Rutter, W J -- Sabloff, J A -- Sagdeev, R Z -- Sahlins, M D -- Salmond, A -- Sanes, J R -- Schekman, R -- Schellnhuber, J -- Schindler, D W -- Schmitt, J -- Schneider, S H -- Schramm, V L -- Sederoff, R R -- Shatz, C J -- Sherman, F -- Sidman, R L -- Sieh, K -- Simons, E L -- Singer, B H -- Singer, M F -- Skyrms, B -- Sleep, N H -- Smith, B D -- Snyder, S H -- Sokal, R R -- Spencer, C S -- Steitz, T A -- Strier, K B -- Sudhof, T C -- Taylor, S S -- Terborgh, J -- Thomas, D H -- Thompson, L G -- Tjian, R T -- Turner, M G -- Uyeda, S -- Valentine, J W -- Valentine, J S -- Van Etten, J L -- van Holde, K E -- Vaughan, M -- Verba, S -- von Hippel, P H -- Wake, D B -- Walker, A -- Walker, J E -- Watson, E B -- Watson, P J -- Weigel, D -- Wessler, S R -- West-Eberhard, M J -- White, T D -- Wilson, W J -- Wolfenden, R V -- Wood, J A -- Woodwell, G M -- Wright, H E Jr -- Wu, C -- Wunsch, C -- Zoback, M L -- Howard Hughes Medical Institute/ -- New York, N.Y. -- Science. 2010 May 7;328(5979):689-90. doi: 10.1126/science.328.5979.689.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/20448167" target="_blank"〉PubMed〈/a〉
    Keywords: *Climate Change ; Politics ; Public Policy ; Research/standards ; Research Personnel
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    Electronic ISSN: 1095-9203
    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
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  • 7
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    Unknown
    American Association for the Advancement of Science (AAAS)
    Publication Date: 1982-09-10
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Englander, S W -- New York, N.Y. -- Science. 1982 Sep 10;217(4564):984.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/7112115" target="_blank"〉PubMed〈/a〉
    Keywords: *National Institutes of Health (U.S.) ; *Research Support as Topic ; United States
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    Electronic ISSN: 1095-9203
    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
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  • 8
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    Unknown
    American Association for the Advancement of Science (AAAS)
    Publication Date: 1987-05-01
    Description: A large number of proteins were tested for the property of intrinsic phosphorescence in deoxygenated aqueous solution at room temperature. The majority of proteins exhibit phosphorescence under normal solution conditions. Phosphorescence lifetimes from 0.5 millisecond to 2 seconds were observed in three-fourths of the proteins tested. The lifetime appears to correlate with relative isolation of the tryptophan indole side chain from solvent. With few exceptions, proteins in general can be expected to display a phosphorescence lifetime greater than 30 microseconds. This widespread characteristic of proteins has been largely overlooked because long-lived phosphorescence is highly sensitive to quenching by low levels of dissolved oxygen in solution. Protein phosphorescence offers a new time domain and a far wider dynamic range than has been used before for photoluminescence experimentation.〈br /〉〈br /〉〈a href="https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3438914/" target="_blank"〉〈img src="https://static.pubmed.gov/portal/portal3rc.fcgi/4089621/img/3977009" border="0"〉〈/a〉   〈a href="https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3438914/" target="_blank"〉This paper as free author manuscript - peer-reviewed and accepted for publication〈/a〉〈br /〉〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Vanderkooi, J M -- Calhoun, D B -- Englander, S W -- AM 11295/AM/NIADDK NIH HHS/ -- GM 34448/GM/NIGMS NIH HHS/ -- GM 36393/GM/NIGMS NIH HHS/ -- R01 GM031847/GM/NIGMS NIH HHS/ -- New York, N.Y. -- Science. 1987 May 1;236(4801):568-9.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/3576185" target="_blank"〉PubMed〈/a〉
    Keywords: Fluorescence ; *Luminescence ; *Luminescent Proteins ; Oxygen/pharmacology ; Solutions ; Spectrophotometry ; Temperature ; Time Factors ; Tryptophan
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    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
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  • 9
    Electronic Resource
    Electronic Resource
    s.l. : American Chemical Society
    Biochemistry 19 (1980), S. 5819-5825 
    ISSN: 1520-4995
    Source: ACS Legacy Archives
    Topics: Biology , Chemistry and Pharmacology
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  • 10
    Electronic Resource
    Electronic Resource
    s.l. : American Chemical Society
    Biochemistry 22 (1983), S. 1526-1532 
    ISSN: 1520-4995
    Source: ACS Legacy Archives
    Topics: Biology , Chemistry and Pharmacology
    Type of Medium: Electronic Resource
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