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Journal Abstract Search


115 related items for PubMed ID: 21117672

  • 1. Protein stability and structure in HIC: hydrogen exchange experiments and COREX calculations.
    Gospodarek AM, Smatlak ME, O'Connell JP, Fernandez EJ.
    Langmuir; 2011 Jan 04; 27(1):286-95. PubMed ID: 21117672
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  • 2. Hydrophobic interaction chromatography selectivity changes among three stable proteins: conformation does not play a major role.
    Jones TT, Fernandez EJ.
    Biotechnol Bioeng; 2004 Aug 05; 87(3):388-99. PubMed ID: 15281113
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  • 9. Loading, stationary phase, and salt effects during hydrophobic interaction chromatography: alpha-lactalbumin is stabilized at high loadings.
    Fogle JL, O'Connell JP, Fernandez EJ.
    J Chromatogr A; 2006 Jul 21; 1121(2):209-18. PubMed ID: 16690064
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  • 10. Changes in solvent exposure reveal the kinetics and equilibria of adsorbed protein unfolding in hydrophobic interaction chromatography.
    Deitcher RW, O'Connell JP, Fernandez EJ.
    J Chromatogr A; 2010 Aug 27; 1217(35):5571-83. PubMed ID: 20630532
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  • 13. Protein instability during HIC: evidence of unfolding reversibility, and apparent adsorption strength of disulfide bond-reduced alpha-lactalbumin variants.
    Deitcher RW, Xiao Y, O'Connell JP, Fernandez EJ.
    Biotechnol Bioeng; 2009 Apr 01; 102(5):1416-27. PubMed ID: 19152385
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  • 16. Structure of a hydrophobically collapsed intermediate on the conformational folding pathway of ribonuclease A probed by hydrogen-deuterium exchange.
    Houry WA, Scheraga HA.
    Biochemistry; 1996 Sep 10; 35(36):11734-46. PubMed ID: 8794754
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  • 17. Structures of multidomain proteins adsorbed on hydrophobic interaction chromatography surfaces.
    Gospodarek AM, Sun W, O'Connell JP, Fernandez EJ.
    J Chromatogr A; 2014 Dec 05; 1371():204-19. PubMed ID: 25456599
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  • 20. Influence of surface modification on protein retention in ion-exchange chromatography. Evaluation using different retention models.
    Bruch T, Graalfs H, Jacob L, Frech C.
    J Chromatogr A; 2009 Feb 06; 1216(6):919-26. PubMed ID: 19111307
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