In 40% TFE/60% water, thymosin alpha‑1 adopts a structure with an alpha-helix from residues 14 to 26 and two double beta-turns in the N-terminal twelve residues.
In plain wordsIn lab tests in a solvent mixture, thymosin alpha‑1 formed a helix in its later part and turns near its start.
- Peptide
- Thymosin alpha-1
- Outcome
- Not applicableNMR structure of thymosin alpha-1 in 40% TFE
- Study
n: not reported in source
40% TFE/60% water solution- Outcome group
- Receptor activity and mechanism · Pharmacology
Source sentences
We found that the peptide adopts a structured conformation having two stable regions: an alpha-helix region from residues 14 to 26 and two double β-turns in the N-terminal twelve residues which form a distorted helical structure.
1 context sentence(design, population, supporting numbers)
800 MHz NMR structure of the 28-residue peptide thymosin alpha-1 in 40% TFE/60% water (v/v) has been determined.
In this study, Thymosin alpha-1 was a lab tool or a carrier, part of a mix, or the subject of a lab method. This result is not evidence about taking Thymosin alpha-1.