Local dynamic properties of the heme pocket in native and solvent-induced molten-globule-like states of cytochrome c

Biophysical Chemistry

Volumn 97, Issue 2-3, 2002, Pages 121-128

  Militello, V ^a   Leone, M ^a   Cupane, A ^a   Santucci, R ^b   Desideri, A ^b  

^a UNIVERSITY OF PALERMO   (Italy)

^b UNIVERSITY OF ROME TOR VERGATA   (Italy)

Author keywords

Molten globule proteins; Optical absorption spectroscopy; Protein dynamics

Indexed keywords

CYTOCHROME C; HEME; SOLVENT;

ABSORPTION; ARTICLE; DYNAMICS; HEART; HORSE; MOTION; NORMAL DISTRIBUTION; PRIORITY JOURNAL; PROTEIN ANALYSIS; PROTEIN CONFORMATION; PROTEIN STRUCTURE; STRUCTURE ANALYSIS; TEMPERATURE; TEMPERATURE DEPENDENCE;

EQUUS CABALLUS;

EID: 0037134762     PISSN: 03014622     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0301-4622(02)00044-3     Document Type: Article

References (28)

1. Dynamics of carbon monoxide binding to heme proteins
2. Dynamics of ligand binding to heme proteins
3. Ligand binding to heme proteins: Connection between dynamics and function
4. Protein dynamics. Comparative investigation on heme-protein with different physiological roles
5. Structure-dynamics-function relationships in Asian elephant (Elephas maximus) myoglobin. An optical and flash-photolysis study on functionally important motions
6. Heme-protein interactions in cytochrome c peroxidase revealed site-directed mutagenesis and resonance Raman spectra of isotopically labeled hemes
7. Fourier-transform infrared analysis of the interaction of azide with the active site of oxidized and reduced bovine Cu, Zn superoxide dismutase
8. Structural and dynamic properties of the homodimeric hemoglobin from Scapharca inaequivalvis Thr72→Ile mutant: Molecular dynamics simulation, low-temperature visible absorption spectroscopy and resonance Raman spectroscopy studies
9. Protein dynamics in an intermediate state of myoglobin: Optical absorption, resonance Raman spectroscopy and X-ray structure analysis
10. The molten globule state as a clue for understanding the folding and co-operativity of globular-protein structure
11. Molten globule and protein folding
12. Probing the molten globule state of alpha-lactalbumin by limited proteolysis
13. Probing the partly folded states of proteins by limited proteolysis
14. Structure and stability of the molten globule state of guinea-pig alpha-lactalbumin: A hydrogen exchange study
15. Formation of a molten-globule-like state of cytochrome c induced by high concentrations of glycerol
16. Acid-induced folding of proteins
17. Interactions of normal modes with electron traps
18. Investigations of spectral broadening mechanisms in biomolecules
19. Thermal broadening of Soret band in heme complexes and in heme-proteins: Role of the iron dynamics
20. Low-temperature optical absorption spectroscopy: An approach to the study of stereodynamic properties of heme proteins
21. Structural fluctuations of myoglobin derived from normal-modes, Mossbauer, Raman and absorption spectroscopy
22. Anharmonic protein motions and heme deformations in myoglobin cyanide probed by absorption and resonance Raman spectroscopy
23. Heme symmetry, vibronic structure and dynamics in heme proteins: Ferrous nicotinate horse myoglobin and soybean leghemoglobin
24. Investigation of the Stokes and anti-Stokes resonance Raman scattering of cytochrome c
25. Structural and analytical aspects of the electronic spectra of heme proteins
26. Low-temperature optical spectroscopy of low-spin ferric heme proteins
27. Conformational substates in proteins
28. Glass-like behavior of proteins as seen by Mossbauer spectroscopy