Alanine substitutions at Pro4, Lys18, Lys19, Pro27, Leu28, Pro29 and Ile34 of Tbeta4 weakened the affinity of the actin-Tbeta4 complex.
In plain wordsIn lab tests, changing single amino acids in thymosin beta‑4 weakened how tightly it bound actin.
- Peptide
- Thymosin beta-4 (human)
- Outcome
- DecreaseActin binding affinity of Tbeta4 alanine mutants
- Study
n: not reported in source
purified MgATP-actin monomers with Tbeta4 mutants- Comparator
- Wild-type Tbeta4
- Outcome group
- Receptor activity and mechanism · Pharmacology
Source sentences
All these mutations weaken the affinity of the actin-Tbeta4 complex
2 context sentences(design, population, supporting numbers)
Pro4, Lys18, Lys19, Pro27, Leu28, Pro29, and Ile34 were substituted by alanine residues.
We have used site-directed mutagenesis to investigate the contributions of widely distributed residues in the thymosin beta-4 (Tbeta4) sequence to the formation and stability of the actin-Tbeta4 complex.
In this study, Thymosin beta-4 (human) 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 beta-4 (human).