Conformational flexibility of lysozyme in the folded and unfolded states



    • 野田, 康夫 ノダ, ヤスオ



Conformational flexibility of lysozyme in the folded and unfolded states


野田, 康夫


ノダ, ヤスオ




博士 (理学)








  1. CONTENTS / p1 (0003.jp2)
  2. Summary / p4 (0006.jp2)
  3. Chapter I General Introduction / p6 (0008.jp2)
  4. I-1 Proteins adopt a specific folded three-dimensional,tertiary structure. / p6 (0008.jp2)
  5. I-2 Proteins are both unfolding and refolding at equilibrium. / p10 (0012.jp2)
  6. I-3 The exchange reaction of peptide NH hydrogen is especially suitable to the study of fluctuations in the backbone structure. / p13 (0015.jp2)
  7. I-4 Reference / p15 (0017.jp2)
  8. Chapter II NMR Spectroscopy / p19 (0021.jp2)
  9. II-1 2D NMR provides well-resolved protein ¹H NMR spectra. / p19 (0021.jp2)
  10. II-2 COSY and NOESY spectra of proteins are interpreted by the method of sequential assignment. / p27 (0029.jp2)
  11. II-3 The superior resolution of COSY spectra can be exploited for obtaining more complete data on the kinetics of the hydrogen-deuterium exchange of amides in a protein. / p29 (0031.jp2)
  12. II-4 Reference / p32 (0034.jp2)
  13. Chapter III Conformational Flexibility of a Polypeptide Chain and Residual Substructures in the Unfolded State of Protein / p35 (0037.jp2)
  14. Section 1 Probing the Conformational State of Unfolded Lysozyme by Limited Proteolysis / p35 (0037.jp2)
  15. III-1-1 Synopsis / p35 (0037.jp2)
  16. III-1-2 Introduction / p36 (0038.jp2)
  17. III-1-3 The trypsin susceptibility of an individual cleavage site is defined as a hydrolytic rate constant of the peptide bond. / p38 (0040.jp2)
  18. III-1-4 Susceptible peptide bonds to trypsin concentrate in the C-terminal region of lysozyme. / p46 (0048.jp2)
  19. Section 2 Local Structure in Unfolded Lysozyme and Correlation with Secondary Structures in the Native Conformation / p49 (0051.jp2)
  20. III-2-1 Synopsis / p49 (0051.jp2)
  21. III-2-2 Introduction / p50 (0052.jp2)
  22. III-2-3 There remain residual secondary structures in TMAP-lysozyme. / p51 (0053.jp2)
  23. III-2-4 Lysozyme fragments of helix-forming propensity just correspond to the helical segments in native lysozyme. / p53 (0055.jp2)
  24. III-3 Reference / p60 (0062.jp2)
  25. Chapter IV Conformational Flexibility of Protein in the Folded State―HD Exchange Behavior of Amide Hydrogen― / p62 (0064.jp2)
  26. IV-1 Synopsis / p62 (0064.jp2)
  27. IV-2 Introduction / p63 (0065.jp2)
  28. IV-3 Peek assignment of the COSY spectrum for the cross-linked lysozyme was carried out by sequence-specific methods. / p67 (0069.jp2)
  29. IV-4 Exchange behavior of individual amide hydrogens is classified into two groups. / p73 (0075.jp2)
  30. IV-5 Activation enthalpies were determined for individual amide hydrogens by Arrhenius plots of exchange rates. / p80 (0082.jp2)
  31. IV-6 Discussion / p83 (0085.jp2)
  32. IV-7 Reference / p94 (0096.jp2)
  33. Chapter V Conclusion / p96 (0098.jp2)
  34. Chapter VI Acknowledgment / p101 (0103.jp2)
  35. Local Structures in Unfolded Lysozyme and Correlation with Secondary Structures in the Native Conformation:Helix-Forming or-Breaking Propensity of Peptide Segments / p497 (0105.jp2)
  36. Specificity of Trypsin Digestion and Conformational Flexibility at Different Sites of Unfolded Lysozyme / p217 (0112.jp2)
  37. A Two-Dimensional NMR Study of Exchange Behavior of Amide Hydrogens in a Lysozyme Derivative with an Extra Cross-Link Between Glu35 and Trp108―Quenching of Cooperative Fluctuations and Effects on the Protein Stability / p131 (0117.jp2)


    • 8000001093195
  • DOI(NDL)
  • 本文言語コード
    • eng
  • NDL書誌ID
    • 000000318499
  • データ提供元
    • 機関リポジトリ
    • NDLデジタルコレクション