Article
Site-directed circular dichroism of proteins: 1Lb bands of Trp resolve position-specific features in tear lipocalin.
Analytical biochemistry - 15 Mar 2008
Gasymov Oktay K, Abduragimov Adil R, Glasgow Ben J
Abstract excerpt
The absorption spectra of N-acetyl-L-tryptophanamide in various solvents were resolved into the sums of the (1)L(a) and (1)L(b) components. The relative intensities of the 0-0 transitions of the (1)L(b) bands correlate linearly with the solvent polarity values (E(T)(N)). A novel strategy that uses a set of the experimental (1)L(b) bands was employed to resolve the near-UV circular dichroism (CD) spectra of...
Topics
- Absorption
- Apoproteins
- Circular Dichroism
- Dimethyl Sulfoxide
- Humans
- Lipocalin 1
- Mutagenesis, Site-Directed
- Mutant Proteins
- Mutation
- Peptide Mapping
- Sensitivity and Specificity
- Solvents
- Tryptophan
- Tyrosine
- Ultraviolet Rays
