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PROBING PROTEIN-STRUCTURE BY SOLVENT PERTURBATION OF NMR-SPECTRA - A COMPARISON WITH PHOTOCHEMICALLY INDUCED DYNAMIC NUCLEAR-POLARIZATION TECHNIQUES APPLIED TO NATIVE ALPHA-LACTALBUMIN
- Source :
- European journal of biochemistry, 227 (1995): 78–86. doi:10.1111/j.1432-1033.1995.tb20361.x, info:cnr-pdr/source/autori:IMPROTA, S; MOLINARI, H; PASTORE, A; CONSONNI, R; ZETTA, L/titolo:PROBING PROTEIN-STRUCTURE BY SOLVENT PERTURBATION OF NMR-SPECTRA-A COMPARISON WITH PHOTOCHEMICALLY INDUCED DYNAMIC NUCLEAR-POLARIZATION TECHNIQUES APPLIED TO NATIVE ALPHA-LACTALBUMIN/doi:10.1111%2Fj.1432-1033.1995.tb20361.x/rivista:European journal of biochemistry (Print)/anno:1995/pagina_da:78/pagina_a:86/intervallo_pagine:78–86/volume:227
- Publication Year :
- 1995
-
Abstract
- We have suggested elsewhere the use of surface mapping by spin label probes (Esposito et al., 1992). According to this approach, soluble nitroxides are added to a protein solution. Resonances of protons that are accessible to the nitroxide are broadened and bleached out of the spectrum, while resonances in the protein interior remain unaffected. This approach is, in principle, complementary to another technique, photochemically induced dynamic nuclear polarization, which maps the position of aromatic protons on the protein surface. A detailed comparison between the two techniques is necessary for a confident use of the more recent suggested nitroxide perturbation approach. In the present study, we show that the results obtained by the two techniques for the native state of bovine alpha-lactalbumin are fully consistent and may therefore be combined for the study of protein surfaces.
- Subjects :
- Lactalbumin
Nitroxide mediated radical polymerization
Magnetic Resonance Spectroscopy
PHOTO-CIDNP
Chemistry
TEMPOL
Photochemistry
Protein Conformation
Analytical chemistry
Nuclear magnetic resonance spectroscopy
Biochemistry
SURFACE MAPPING
NMR
NMR spectra database
Protein structure
Chemical physics
Native state
Solvents
Animals
Protein folding
Cattle
Spin label
Subjects
Details
- Language :
- English
- Database :
- OpenAIRE
- Journal :
- European journal of biochemistry, 227 (1995): 78–86. doi:10.1111/j.1432-1033.1995.tb20361.x, info:cnr-pdr/source/autori:IMPROTA, S; MOLINARI, H; PASTORE, A; CONSONNI, R; ZETTA, L/titolo:PROBING PROTEIN-STRUCTURE BY SOLVENT PERTURBATION OF NMR-SPECTRA-A COMPARISON WITH PHOTOCHEMICALLY INDUCED DYNAMIC NUCLEAR-POLARIZATION TECHNIQUES APPLIED TO NATIVE ALPHA-LACTALBUMIN/doi:10.1111%2Fj.1432-1033.1995.tb20361.x/rivista:European journal of biochemistry (Print)/anno:1995/pagina_da:78/pagina_a:86/intervallo_pagine:78–86/volume:227
- Accession number :
- edsair.doi.dedup.....57a8bb7e442350f693e30e7f2b326fca
- Full Text :
- https://doi.org/10.1111/j.1432-1033.1995.tb20361.x