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Internal Stark Effect Measurement of the Electric Field at the Amino Terminus of an α Helix
- Source :
- Science. 257:947-951
- Publication Year :
- 1992
- Publisher :
- American Association for the Advancement of Science (AAAS), 1992.
-
Abstract
- The strengths of electrostatic interactions in biological molecules are difficult to calculate or predict because they occur in complicated, inhomogeneous environments. The electric field at the amino terminus of an alpha helix in water has been determined by measuring the shift in the absorption band for a covalently attached, neutral probe molecule with an electric dipole moment difference between the ground and excited electronic states (an internal Stark effect). The field at the interface between the helix and the solvent is found to be an order of magnitude stronger than expected from the dielectric properties of bulk water. Furthermore, although the total electric dipole moment of the helix increases with length, the electric field at the amino terminus does not.
- Subjects :
- Models, Molecular
Quantitative Biology::Biomolecules
Multidisciplinary
Field (physics)
Protein Conformation
Chemistry
Molecular Sequence Data
Proteins
Water
Dielectric
Electrostatics
Molecular physics
symbols.namesake
Electric dipole moment
Nuclear magnetic resonance
Stark effect
Electric field
Helix
Electrochemistry
symbols
Spectrophotometry, Ultraviolet
Amino Acid Sequence
Amino Acids
Peptides
Alpha helix
Subjects
Details
- ISSN :
- 10959203 and 00368075
- Volume :
- 257
- Database :
- OpenAIRE
- Journal :
- Science
- Accession number :
- edsair.doi.dedup.....6170eb00e57c5cd7deb9706766a8069f
- Full Text :
- https://doi.org/10.1126/science.1502559