Hydration of apomyoglobin in native, molten globule, and unfolded states by using microwave dielectric spectroscopy

Biophysical Journal

Volumn 82, Issue 1, 2002, Pages 418-425

  Kamei, Takashi ^a   Oobatake, Motohisa ^b   Suzuki, Makoto ^a  

^a TOHOKU UNIVERSITY   (Japan)

^b MEIJO UNIVERSITY   (Japan)

Author keywords

[No Author keywords available]

Indexed keywords

APOMYOGLOBIN;

ARTICLE; HYDRATION; HYDROPHOBICITY; PH; PROTEIN FOLDING; PROTEIN SECONDARY STRUCTURE; SPECTROSCOPY; THERMODYNAMICS;

EID: 0036215851     PISSN: 00063495     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0006-3495(02)75406-4     Document Type: Article

References (14)

1. Phase diagram for acidic conformational states of apomyoglobin
2. Thermodynamic puzzle of apomyoglobin unfolding
3. Thermodynamic study of the apomyoglobin structure
4. Comparison of myoglobins from harbor seal, porpoise, and sperm whale
5. Structural characterization of the molten globule and native states of apomyoglobin by solution x-ray scattering
6. Thermodynamic stability of the molten globule states of apomyoglobin
7. Cold denaturation of the molten globule states of apomyoglobin and a profile for protein folding
8. Further observations on the electrical properties of hemoglobin-bound water
9. Coupling of protein surface hydrophobicity change to ATP hydrolysis by myosin motor domain
10. Hydrophobic hydration analysis on amino acid solution by the microwave dielectric method
11. Hydration study of proteins in solution by microwave dielectric analysis
12. Erklärung der dielektrischen nachwirkungsvorgänge auf grund maxwellscher vorstellungen