A5009717280- Protein Structure and Dynamics
- Enzyme Structure and Function
- Heat shock proteins research
- Protein purification and stability
- RNA and protein synthesis mechanisms
- Hemoglobin structure and function
- Enzyme function and inhibition
- Glycosylation and Glycoproteins Research
- Viral Infectious Diseases and Gene Expression in Insects
- Biochemical and Structural Characterization
- Receptor Mechanisms and Signaling
- Computational Drug Discovery Methods
Institute of Protein Research
2016-2024
Directed stabilization of globular proteins via substitution a minimal number amino acid residues is one the most complicated experimental tasks. This work summarizes our research on effect substitutions protein stability utilizing outputs analysis intrinsic disorder predisposition target proteins. allowed us to formulate basis possible approaches The idea quite simple. To stabilize as whole, needs find its "weakest spot" and it, but question how this weak spot can be found in query protein....
Abstract Enhancing protein stability holds paramount significance in biotechnology, therapeutics, and the food industry. Circular permutations offer a distinctive avenue for manipulating while keeping intra-protein interactions intact. Amidst creation of circular permutants, determining optimal placement new N- C-termini stands as pivotal, albeit largely unexplored, endeavor. In this study, we employed PONDR-FIT’s predictions disorder propensity to guide design permutants GroEL apical domain...
In this study, we have used an approach that allows us to determine in what region of the polypeptide chain protein it is required insert a disulphide bond order stabilize it. our previous paper [Melnik et al., JBSD. 2012] was proposed search for "weak" site protein, possible use programs (for example, PONDR-FIT and IsUnstruct) finding intrinsic disorder regions. We suggested structured globular proteins, such predict not regions disordered under native conditions, but "weakened", feebly...
In most cases, intermediate states of multistage folding proteins are not 'visible' under equilibrium conditions but revealed in kinetic experiments. Time-resolved fluorescence spectroscopy was used denaturation studies. The technique allows for detecting changes the conformation and environment tryptophan residues different structural elements carbonic anhydrase II which its turn has made it possible to study conditions. results experiments using wild-type bovine mutant form with...
Исследован белок Gαo из Drosophila melanogaster.Авторы спроектировали SS-связь в этом белке таким образом, чтобы увеличить его стабильность.Выбор участка полипептидной цепи для введения цистеинового мостика основывался на расчётах программ, которые используются предсказания нативно-развёрнутых белков.В предыдущих работах высказывалось предположение
Abstract Enhancing protein stability holds paramount significance in biotechnology, therapeutics, and the food industry. Circular permutations offer a distinctive avenue for manipulating while keeping intra-protein interactions intact. Amidst creation of circular permutants, determining optimal placement new N- C-termini stands as pivotal, albeit largely unexplored, endeavor. In this study, we employed PONDR-FIT’s predictions disorder propensity to guide design permutants GroEL apical domain...