Fluorescence lifetime measurements on some tryptophan-containing diketopiperazines
β Scribed by Donald B. Bivin; Mikhail I. Khoroshev
- Book ID
- 108043509
- Publisher
- Elsevier Science
- Year
- 1994
- Tongue
- English
- Weight
- 663 KB
- Volume
- 78
- Category
- Article
- ISSN
- 1010-6030
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The tryptophan fluorescence of two membrane proteins (outer membrane protein A and lactose permease), a 21-residue hydrophobic peptide, three soluble proteins (rat serum albumin, ribonuclease Tt, and azurin), and N-acetyltryptophanamide (NATA) was investigated by time-resolved measurements extended
done using an empirical energy program for peptides (ECEPP). The resulting low-energy conformations were analyzed for the presence of hydrogen bonds, the distances between carbonyl groups and the indole ring, the distances between the N-terminal amino group and the indole ring, the dihedral angle be