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UV Resonance Raman Investigations of Peptide and Protein Structure and Dynamics
- Source :
- Chemical Reviews. 112:2604-2628
- Publication Year :
- 2012
- Publisher :
- American Chemical Society (ACS), 2012.
-
Abstract
- A study was conducted to demonstrate ultraviolet resonance Raman (UVRR) investigations of peptide and protein structure and dynamics. The tuning of the excitation wavelengths allowed the probing of different chromophoric segments of a macromolecule. Another advantage of deep UV Raman measurements was that there was no interference from molecular relaxed fluorescence, as those chromophores that had their first transition below 260 nm were highly flexible and possessed small fluorescence quantum yields. UVRR was also used in pump-probe measurements to give kinetic information on fast biological processes. It was a powerful technique for studying static protein structure and for studying protein dynamics, such as in protein folding. The rapid development of UVRR was aided by the latest advancements in lasers, optics, and detectors.
- Subjects :
- Models, Molecular
Amyloid
Protein Folding
Molecular Sequence Data
Analytical chemistry
Spectrum Analysis, Raman
medicine.disease_cause
Vibration
Article
Protein Structure, Secondary
symbols.namesake
Protein structure
medicine
Humans
Amino Acid Sequence
Quantitative Biology::Biomolecules
Chemistry
Protein dynamics
Resonance
Bayes Theorem
General Chemistry
Chromophore
Fluorescence
Kinetics
Chemical physics
Isotope Labeling
symbols
Thermodynamics
Muramidase
Protein folding
Peptides
Raman spectroscopy
Ultraviolet
Subjects
Details
- ISSN :
- 15206890 and 00092665
- Volume :
- 112
- Database :
- OpenAIRE
- Journal :
- Chemical Reviews
- Accession number :
- edsair.doi.dedup.....95c26f5e842b602969912c0149fc8d60