Thesis final - after defense-7 - Jacobs University

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References 122. Chen, J.; Luo, Q.; Breneman, C.M.; Cramer, S.M. Classification of protein adsorption and recovery at low salt conditions in hydrophobic interaction chromatographic systems. Journal of Chromatography A 2007, 1139, 236-246. 123. Fountoulakis, M. and Takács, B. Design of Protein Purification Pathways: Application to the Proteome ofHaemophilus influenzaeUsing Heparin Chromatography. Protein expression and purification 1998, 14, 113-119. 124. Rose, G.D.; Gierasch, L.; Smith, J.A. Turns in peptides and proteins. Advanced protein chemistry 1985, 37, 109. 125. Miller, S.; Janin, J.; Lesk, A.M.; Chothia, C. Interior and surface of monomeric proteins. Journal of Molecular Biology 1987, 196, 641-656. 126. Fausnaugh, J.L.; Pfannkoch, E.; Gupta, S.; Regnier, F. High-performance hydrophobic interaction chromatography of proteins. Analatyical Biochemistry 1984, 137, 464-472. 127. Katti, A.; Maa, Y.; Horváth, C. Protein surface area and retention in hydrophobic interaction chromatography. Chromatographia 1987, 24, 646-650. 128. Gekko, K. and Hasegawa, Y. Compressibility-structure relationship of globular proteins. Biochemistry (N. Y. ) 1986, 25, 6563-6571. 129. Jungbauer, A.; Machold, C.; Hahn, R. Hydrophobic interaction chromatography of proteins: III. Unfolding of proteins upon adsorption. Journal of Chromatography A 2005, 1079, 221-228. 130. Fogle, J.L.; O’Connell, J.P.; Fernandez, E.J. Loading, stationary phase, and salt effects during hydrophobic interaction chromatography: α-Lactalbumin is stabilized at high loadings. Journal of Chromatography A 2006, 1121, 209-218. 131. Ueberbacher, R.; Haimer, E.; Hahn, R.; Jungbauer, A. Hydrophobic interaction chromatography of proteins: V. Quantitative assessment of conformational changes. Journal of Chromatography A 2008, 1198-1199, 154-163. 129
References 132. Reubsaet, J.L.E. and Vieskar, R. Characterisation of π–π interactions which determine retention of aromatic compounds in reversed-phase liquid chromatography. Journal of Chromatography A 1999, 841, 147-154. 133. Vennapusa, R.R.; Tari, C.; Cabrera, R.; Fernandez-Lahore, M. Surface energetics to assess biomass attachment onto hydrophobic interaction adsorbents in expanded beds. Biotechnology and Bioprocess Engineering 2009, 43, 16-26. 130
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A proteome wide approach to underst
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I also want to mention the efforts
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Dedication To my father Haji Sher A
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Table of Contents 1. Introduction .
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3.3.2.2. Protein distributions on 2
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Chapter 1 1. Introduction 1.1. Intr
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Chapter 1 cell proteome to facilita
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Chapter 1 proteins. It is this diff
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Chapter 1 Salt conc. decreasing (Gr
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Chapter 1 The ions at the start of
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Chapter 1 exposure of hydrophobic r
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Chapter 1 based on the surface hydr
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Chapter 1 1.5. Analysis of the yeas
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Chapter 1 molecular weight impuriti
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Chapter 1 followed by its introduct
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Chapter 1 protein towards purificat
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Chapter 2 EXPERIMENTAL APPROACH
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Chapter 2 Yeast cell proteome and c
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Chapter 2 ligands (Toyopearl-Hexyl,
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Chapter 2 number of spots was count
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Chapter 2 (http://www.matrixscience
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Chapter 3 RESULTS AND DISCUSSION
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Chapter 3 to the retention behavior
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Chapter 3 investigate the hydrophob
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Chapter 3 the interior of the prote
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Chapter 3 A B C Figure 9: The cryst
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Chapter 3 of the comparative analys
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Chapter 3 Figure 11: Represent the
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Chapter 3 Ether, some 2-D gels were
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Chapter 3 Figure 13: Represent 2-D
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Chapter 3 Table 5. List of the iden
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Chapter 3 Table 7. List of the iden
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Chapter 3 amino acids by Cowan-Whit
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Chapter 3 Figure 15 C: Represents t
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Chapter 3 Figure 16 A: Represents t
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Chapter 3 The polarity value for th
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Chapter 3 Figure 17: Represents the
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Chapter 3 Figure 18: Represents the
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Chapter 3 published papers with mod
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Chapter 3 ligands revealed less dif
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Chapter 3 3.2. Influence of the dif
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Chapter 3 Table 10: The chemistry o
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Chapter 3 where approximately 50% o
Page 87 and 88: Chapter 3 3.2.3.2. The electrophore
Page 89 and 90: Chapter 3 Figure 22: Represent 2-D
Page 91 and 92: Chapter 3 Table 12. List of the ide
Page 93 and 94: Chapter 3 Table 14. List of the ide
Page 95 and 96: Chapter 3 r 2 values from the data
Page 97 and 98: Chapter 3 Figure 24 C: Represents t
Page 99 and 100: Chapter 3 approximately 47%. The me
Page 101 and 102: Chapter 3 Figure 25 B: Represents t
Page 103 and 104: Chapter 3 values have been reported
Page 105 and 106: Chapter 3 towards conformational ch
Page 107 and 108: Chapter 3 Figure 28: Represents the
Page 109 and 110: Chapter 3 among the adsorbents were
Page 111 and 112: Chapter 3 3.3. Protein distribution
Page 113 and 114: Chapter 3 3.3.2.2. Protein distribu
Page 115 and 116: Chapter 3 Figure 29 B: Represent th
Page 117 and 118: Chapter 3 When the number of smalle
Page 119 and 120: Chapter 3 and hydrophobic interacti
Page 121 and 122: Chapter 4 CONCLUSIONS
Page 123 and 124: Chapter 4 • The base supports rev
Page 125 and 126: Chapter 4 additional understanding
Page 127 and 128: References 13. Lienqueo, M.E.; Lese
Page 129 and 130: References 32. Salgado, J.C.; Rapap
Page 131 and 132: References 52. B.H.J., H. Accessibl
Page 133 and 134: References 71. Xindu, G. and Regnie
Page 135 and 136: References 91. Alonso-Orgaz, S.; Mo
Page 137: References 112. Gu, Z. and Glatz, C
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Thesis final - after defense-7 - Jacobs University

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