Two-dimensional infrared correlation spectroscopy study of the aggregation of cytochrome c in the presence of dimyristoylphosphatidylglycerol

Biophysical Journal

Volumn 81, Issue 1, 2001, Pages 305-312

  Paquet, Marie Josée ^a   Laviolette, Mario ^a   Pézolet, Michel ^a   Auger, Michèle ^a  

^a UNIVERSITÉ LAVAL   (Canada)

Author keywords

[No Author keywords available]

Indexed keywords

CYTOCHROME C; DIMYRISTOYLPHOSPHATIDYLGLYCEROL;

ARTICLE; ENZYME STRUCTURE; INFRARED SPECTROSCOPY; MOLECULAR INTERACTION; PROTEIN AGGREGATION; PROTEIN TERTIARY STRUCTURE; TEMPERATURE;

EID: 0034957763     PISSN: 00063495     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0006-3495(01)75700-1     Document Type: Article

References (52)

1. Thermal denaturation of globular proteins: Fourier transform-infrared studies of the amide III spectral region
2. Quantitative studies of the structure of proteins in solution by Fourier-transform infrared spectroscopy
3. Probing conformational changes in the nicotinic acetylcholine receptor by Fourier transform infrared difference spectroscopy
4. Structure and dynamics of lipid-associated states of apocytochrome c
5. High-resolution three-dimensional structure of horse heart cytochrome c
6. Examination of the secondary structure of proteins by deconvolved FTIR spectra
7. Precision in condensed phase vibrational spectroscopy
8. Deconvolution, derivation, and smoothing of spectra using Fourier transforms
9. Electrophoretic and dynamic light scattering study of the interaction of cytochrome c with dimyristoylphosphatidylglycerol, dimyristoylphosphatidylcholine, and intramembranously mixed liposomes
10. Ferricytochrome c. I. General features of the horse and bonito proteins at 2.8 Å resolution
11. Protein secondary structures in water from second-derivative amide I infrared spectra
12. Entrapping intermediates of thermal aggregation in α-helical proteins with low concentration of guanidine hydrochloride
13. Determination of the secondary structure content of proteins in aqueous solutions from their amide I and amide II infrared bands. Comparison between classical and partial least-squares methods
14. 1 in aqueous solution
15. Characterization of biological samples by two-dimensional infrared spectroscopy: Simulation of frequency, bandwith, and intensity changes
16. Determination of soluble and membrane protein structure by Fourier transform infrared spectroscopy I. Assignments and model compounds
17. The effects of chain length and thermal denaturation on helix-forming peptides: A mode-specific analysis using 2D FT-IR
18. Introduction to spectral deconvolution
19. Investigation of secondary and tertiary structural changes of cytochrome c in complexes with anionic lipids using amide hydrogen exchange measurements: An FTIR study
20. Protein surface-distribution and protein-protein interactions in the binding of peripheral proteins to charged lipid membranes
21. Cooperative binding of hexadecyltrimethylammonium chloride and sodium dodecyl sulfate to cytochrome c and the resultant change in protein conformation
22. 2+-binding proteins
23. The use and misuse of FTIR spectroscopy in the determination of protein structure
24. Conformation of magainin-2 and related peptides in aqueous solution and membrane environments probed by Fourier transform infrared spectroscopy
25. A study of the amide III band by FT-IR spectrometry of the secondary structure of albumin, myoglobin, and γ-globulin
26. Fourier transforms in the computation of self-deconvoluted and first-order derivative spectra of overlapped band contours
27. Novel use of a static modification of two-dimensional correlation analysis. Part II: Heterospectral correlations of protein Raman, FT-IR, and circular dichroism spectra
28. Effect of lipids on the thermal stability and conformational changes of proteins: Ribonuclease A and cytochrome c
29. Membrane binding induces destabilization of cytochrome c structure
30. Apocytochrome c interaction with phospholipid membranes studied by Fourier-transform infrared spectroscopy
31. Two-dimensional FY-IR spectroscopy: A powerful method to study the secondary structure of proteins using H-D exchange
32. Two-dimensional infrared spectroscopy
33. Two-dimensional infrared (2D-IR) spectroscopy: Theory and applications
34. Novel use of a static modification of two-dimensional correlation analysis. Part I: Comparison of the secondary structure sensitivity of electronic circular dichroism, FT-IR, and Raman spectra of proteins
35. Structural and kinetic description of cytochrome c unfolding induced by the interaction with lipid vesicles
36. Protein secondary structure from Fourier transform infrared and/or circular dichroism spectra
37. Estimation of globular protein secondary structure from circular dichroism
38. Infrared amide I' band of the coiled coil
39. Studies on the lipid dependency and mechanism of the translocation of the mitochondrial precursor protein apocytochrome c across model membranes
40. Surface plasmon resonance studies of complex formation between cytochrome c and bovine cytochrome c oxidase incorporated into a supported planar lipid bilayer. I. Binding of cytochrome c to cardiolipin/phosphatidylcholine membranes in the absence of oxidase
41. Unfolding and refolding of cytochrome c driven by the interaction with lipid micelles
42. Protein secondary structure from Fourier transform infrared spectroscopy: A data base analysis
43. Membrane location of apocytochrome c and cytochrome c determined from lipid-protein spin exchange interactions by continuous wave saturation electron spin resonance
44. Polymerization mechanism of polypeptide chain aggregation
45. Conformational changes of melittin upon insertion into phospholipid monolayer and vesicle
46. Structure, stability, and receptor interaction of cholera toxin as studied by Fourier-transform infrared spectroscopy
47. New insight into protein secondary structure from resolution-enhanced infrared spectra
48. Determination of protein secondary structure by Fourier transform infrared spectroscopy: A critical assessment
49. Conformation change of cytochrome c. I. Ferrocytochrome c structure refined at 1.5 Å resolution
50. Two-dimensional Fourier transform near-infrared spectroscopy study of heat denaturation of ovalbumin in aqueous solutions
51. Fast events in protein folding: Helix melting and formation in a small peptide
52. Calorimetric studies of the interactions of cytochrome c with dioleoylphosphatidylglycerol extruded vesicles: Ionic strength effects