118 related articles for article (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; 27(1):286-95. PubMed ID: 21117672
[TBL] [Abstract][Full Text] [Related]
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; 87(3):388-99. PubMed ID: 15281113
[TBL] [Abstract][Full Text] [Related]
3. Local and long-range interactions in the molten globule state: A study of chimeric proteins of bovine and human alpha-lactalbumin.
Mizuguchi M; Masaki K; Demura M; Nitta K
J Mol Biol; 2000 May; 298(5):985-95. PubMed ID: 10801363
[TBL] [Abstract][Full Text] [Related]
4. Protein instability during HIC: hydrogen exchange labeling analysis and a framework for describing mobile and stationary phase effects.
Xiao Y; Jones TT; Laurent AH; O'Connell JP; Przybycien TM; Fernandez EJ
Biotechnol Bioeng; 2007 Jan; 96(1):80-93. PubMed ID: 16952152
[TBL] [Abstract][Full Text] [Related]
5. Elucidation of the binding sites of sodium dodecyl sulfate to β-lactoglobulin using hydrogen/deuterium exchange mass spectrometry combined with docking simulation.
Hu W; Liu J; Luo Q; Han Y; Wu K; Lv S; Xiong S; Wang F
Rapid Commun Mass Spectrom; 2011 May; 25(10):1429-36. PubMed ID: 21504009
[TBL] [Abstract][Full Text] [Related]
6. Molten globule structure of equine beta-lactoglobulin probed by hydrogen exchange.
Kobayashi T; Ikeguchi M; Sugai S
J Mol Biol; 2000 Jun; 299(3):757-70. PubMed ID: 10835282
[TBL] [Abstract][Full Text] [Related]
7. Protein instability during HIC: describing the effects of mobile phase conditions on instability and chromatographic retention.
Xiao Y; Freed AS; Jones TT; Makrodimitris K; O'Connell JP; Fernandez EJ
Biotechnol Bioeng; 2006 Apr; 93(6):1177-89. PubMed ID: 16444741
[TBL] [Abstract][Full Text] [Related]
8. 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; 1217(35):5571-83. PubMed ID: 20630532
[TBL] [Abstract][Full Text] [Related]
9. Unfolding and refolding of bovine beta-lactoglobulin monitored by hydrogen exchange measurements.
Ragona L; Fogolari F; Romagnoli S; Zetta L; Maubois JL; Molinari H
J Mol Biol; 1999 Nov; 293(4):953-69. PubMed ID: 10543977
[TBL] [Abstract][Full Text] [Related]
10. 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; 1121(2):209-18. PubMed ID: 16690064
[TBL] [Abstract][Full Text] [Related]
11. Charge state distribution and hydrogen/deuterium exchange of alpha-lactalbumin and beta-lactoglobulin preparations by electrospray ionization mass spectrometry.
Alomirah H; Alli I; Konishi Y
J Agric Food Chem; 2003 Mar; 51(7):2049-57. PubMed ID: 12643672
[TBL] [Abstract][Full Text] [Related]
12. Accessibility changes within diphtheria toxin T domain when in the functional molten globule state, as determined using hydrogen/deuterium exchange measurements.
Man P; Montagner C; Vitrac H; Kavan D; Pichard S; Gillet D; Forest E; Forge V
FEBS J; 2010 Feb; 277(3):653-62. PubMed ID: 20050921
[TBL] [Abstract][Full Text] [Related]
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; 102(5):1416-27. PubMed ID: 19152385
[TBL] [Abstract][Full Text] [Related]
14. Cooperative unfolding of a metastable serpin to a molten globule suggests a link between functional and folding energy landscapes.
Tsutsui Y; Wintrode PL
J Mol Biol; 2007 Aug; 371(1):245-55. PubMed ID: 17568610
[TBL] [Abstract][Full Text] [Related]
15. Limited proteolysis of bovine alpha-lactalbumin: isolation and characterization of protein domains.
Polverino de Laureto P; Scaramella E; Frigo M; Wondrich FG; De Filippis V; Zambonin M; Fontana A
Protein Sci; 1999 Nov; 8(11):2290-303. PubMed ID: 10595532
[TBL] [Abstract][Full Text] [Related]
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; 35(36):11734-46. PubMed ID: 8794754
[TBL] [Abstract][Full Text] [Related]
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; 1371():204-19. PubMed ID: 25456599
[TBL] [Abstract][Full Text] [Related]
18. Comparison of the denaturant-induced unfolding of the bovine and human alpha-lactalbumin molten globules.
Wijesinha-Bettoni R; Dobson CM; Redfield C
J Mol Biol; 2001 Sep; 312(1):261-73. PubMed ID: 11545601
[TBL] [Abstract][Full Text] [Related]
19. Probing subtle differences in the hydrogen exchange behavior of variants of the human alpha-lactalbumin molten globule using mass spectrometry.
Last AM; Schulman BA; Robinson CV; Redfield C
J Mol Biol; 2001 Aug; 311(4):909-19. PubMed ID: 11518539
[TBL] [Abstract][Full Text] [Related]
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; 1216(6):919-26. PubMed ID: 19111307
[TBL] [Abstract][Full Text] [Related]
[Next] [New Search]
