The biotin-1,4-diaminobutane (Bio-Put), biotin-tryptophan (Bio-Trp) and biotin-3-methylindole (Bio-Sct) systems were investigated by means of Raman spectroscopy. The interaction with Put renders the polar resonance forms of Bio more stabilized. One group of Put is protonated by the COOH group of Bio
Tryptophan-containing peptide helices: interactions involving the indole side chain*
✍ Scribed by Mahalakshmi, R. ;Sengupta, A. ;Raghothama, S. ;Shamala, N. ;Balaram, P.
- Book ID
- 110893920
- Publisher
- John Wiley and Sons
- Year
- 2005
- Tongue
- English
- Weight
- 967 KB
- Volume
- 66
- Category
- Article
- ISSN
- 1397-002X
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## Abstract The mechanisms for the electron transfer between the indole side chain and phenol side chain of peptides involving tryptophan and tyrosine have been studied by __ab initio__ calculation in this work. The solvent effect has been considered by using the conductor‐like screening model (COS
Previous ab initio computations revealed that the conformational building unit of the Ž . right-handed helix f y54Њ, f y45Њ is not an energy minimum on two-Ž Ä 4 . dimensional-type Ramachandran potential energy surfaces E s E , . Theoretical investigations were performed on several single-amino-acid