A5017372629- Protein Structure and Dynamics
- Alzheimer's disease research and treatments
- Enzyme Structure and Function
- Molecular spectroscopy and chirality
- Metabolomics and Mass Spectrometry Studies
- Drug Transport and Resistance Mechanisms
- Mass Spectrometry Techniques and Applications
- Protein Interaction Studies and Fluorescence Analysis
- Neuroinflammation and Neurodegeneration Mechanisms
- Heat shock proteins research
- Parkinson's Disease Mechanisms and Treatments
- RNA and protein synthesis mechanisms
- Analytical Chemistry and Chromatography
- Bacterial Genetics and Biotechnology
- Complement system in diseases
- Glycosylation and Glycoproteins Research
- Amyotrophic Lateral Sclerosis Research
- Adenosine and Purinergic Signaling
- Neurological diseases and metabolism
- Spectroscopy and Quantum Chemical Studies
- Blood Coagulation and Thrombosis Mechanisms
- Autophagy in Disease and Therapy
- Educational Robotics and Engineering
- Biochemical and Structural Characterization
- Antimicrobial Resistance in Staphylococcus
Eötvös Loránd University
2015-2025
Significance Circular dichroism (CD) spectroscopy is widely used for protein secondary structure analysis. However, quantitative estimation β-sheet–containing proteins problematic due to the huge morphological and spectral diversity of β-structures. We show that parallel/antiparallel orientation twisting β-sheets account observed diversity. Taking into twist β-structures, our method accurately estimates a broad range folds, particularly β-sheet–rich amyloid fibrils. Moreover, can predict...
Circular dichroism (CD) spectroscopy is a widely used method to study the protein secondary structure. However, for decades, general opinion was that correct estimation of β-sheet content challenging because large spectral and structural diversity β-sheets. Recently, we showed orientation twisting β-sheets account observed diversity, developed new estimate accurately structure (PNAS, 112, E3095). BeStSel web server provides Beta Structure Selection analyze CD spectra recorded by conventional...
Circular dichroism (CD) spectroscopy is widely used to characterize the secondary structure composition of proteins. To derive accurate and detailed structural information from CD spectra, we have developed Beta Structure Selection (BeStSel) method (PNAS, 112, E3095), which can handle spectral diversity β-structured The BeStSel webserver provides this with useful accessories community main goal analyze single or multiple protein spectra. Uniquely, on eight components including parallel...
Significance Synaptic pruning is dominant in early ontogenesis when a large number of unnecessary synapses are eliminated, and it maintains synaptic plasticity the mature healthy brain, e.g., memory processes. Its malfunction involved degenerative diseases such as Alzheimer’s disease. C1q, member immune complement system, plays central role selective by microglial phagocytosis. Understanding molecular aspects complement-mediated synapse elimination high importance for developing effective...
Intrinsically disordered proteins lack a stable tertiary structure and form dynamic conformational ensembles due to their characteristic physicochemical properties amino acid composition. They are abundant in nature responsible for large variety of cellular functions. While numerous bioinformatics tools have been developed silico disorder prediction the last decades, there is need experimental methods verify state. CD spectroscopy widely used protein secondary analysis. It usable wide...
Abstract Synaptic functional disturbances with concomitant synapse loss represent central pathological hallmarks of Alzheimer’s disease. Excessive accumulation cytotoxic amyloid oligomers is widely recognized as a key event that underlies neurodegeneration. Certain complement components are crucial instruments widespread because they can tag synapses impairments leading to their engulfment by microglia. However, an exact understanding the affected synaptic functions predispose...
Recent progress in the field of amyloid research indicates that classical view fibrils, being irreversibly formed highly stable structures resistant to perturbating conditions and proteolytic digestion, is getting more complex. We studied thermal stability heat-induced depolymerization fibrils β2-microglobulin (β2m), a protein responsible for dialysis-related amyloidosis. found freshly polymerized β2m at 0.1−0.3 mg/mL concentration completely dissociated monomers upon 10 min incubation 99...
Abstract Protein aggregation and amyloid formation are linked to numerous degenerative diseases, such as Alzheimer's or Parkinson's disease. Additionally, protein plays a crucial role in various biological processes, storage of molecules cell signaling. can form wide range aggregates, from oligomers different sizes non‐specific aggregates highly ordered cross‐β structured fibrils with diverse morphologies. Circular dichroism (CD) spectroscopy is widely used technique study structures...
In synapses that show signs of local apoptosis and mitochondrial stress undergo neuro-immunological synapse pruning, an increase in the levels presynaptic protein, neuronal-specific septin-3 can be observed. Septin-3 is a member septin GTPase family with ability to form multimers contribute cytoskeleton. However, function remains elusive. Here, we provide evidence capable binding most-studied autophagy protein Atg8 homolog microtubule-associated 1 light chain 3B (LC3B), besides another...
β2-microglobulin- (β2m-) based fibril deposition is the key symptom in dialysis-related amyloidosis. β2m readily forms amyloid fibrils vitro at pH 2.5. However, it not well understood which factors promote this process vivo, because cannot polymerize neutral without additives even elevated concentration. Here we show that lysophosphatidic acid (LPA), an vivo occurring lysophospholipid mediator, promotes formation under physiological conditions through a complex mechanism. In presence of LPA,...
Adsorption of enzymes on solid surfaces may lead to conformational changes that reduce their catalytic conversion activity and are thus detrimental the efficiency biotechnology or biosensing applications. This work is a joint theoretical experimental endeavor in which we identify quantify chymotrypsin undergoes when contact with surface amorphous silica nanoparticles. For this purpose, use circular dichroism spectroscopy, standard molecular dynamics, advanced-sampling methods. Only...
Disordered plant chaperones play key roles in helping plants survive harsh conditions, and they are indispensable for seeds to remain viable. Aside from well-known thoroughly characterized globular chaperone proteins, there a number of intrinsically disordered proteins (IDPs) that can also serve as highly effective protecting agents the cells. One largest groups is group dehydrins, expressed at high levels under different abiotic stress such drought, temperature, or osmotic stress. Dehydrins...
Pancreatic chymotrypsins (CTRs) are digestive proteases that in humans include CTRB1, CTRB2, CTRC, and CTRL. The highly similar CTRB1 CTRB2 the products of gene duplication. A common inversion at CTRB1-CTRB2 locus reverses expression ratio these isoforms favor CTRB2. Carriers allele protected against inflammatory disorder pancreatitis presumably via their increased capacity for CTRB2-mediated degradation harmful trypsinogen. To reveal protective molecular determinants we compared enzymatic...
The 20 residue long Trp-cage miniprotein is an excellent model for both computational and experimental studies of protein folding stability. Recently, great attention emerged to study disease-related misfolding, aggregation, amyloid formation, with the aim revealing their structural thermodynamic background. sensitive environmental structure-modifying effects. It aggregates ease upon structure destabilization, thus it suitable modeling aggregation formation. Here, we characterize formation...
Horizontal transfer of mobile genetic elements within Staphylococci is high biomedical significance as such are frequently responsible for virulence and toxic effects. Staphylococcus-encoded repressor proteins regulate the replication these that located so-called pathogenicity islands. Here, we report structural functional characterization one protein, namely Stl protein encoded by island SaPIbov1. We create a 3D model based on this prediction, investigate different functionalities truncated...
Details of the functional mechanisms intrinsically disordered proteins (IDPs) in living cells is an area not frequently investigated. Here, we dissect molecular mechanism action IDP by detailed structural analyses based on in-cell nuclear magnetic resonance experiment. We show that ID stress protein (IDSP) A. thaliana Early Response to Dehydration (ERD14) capable protecting E. coli under heat stress. The overexpression ERD14 increases viability from 38.9% 73.9% following (50 °C × 15 min)....
Complement component C1q is a protein complex of the innate immune system with well-characterized binding partners that constitutes part classical complement pathway. In addition, was recently described in central nervous as having role synapse elimination both healthy brain and neurodegenerative diseases. However, molecular mechanism C1q-associated phagocytosis still unclear. Here, we designed monomer multimer constructs, which comprised globular interaction recognition parts mouse...
Human ileal bile acid‐binding protein (I‐ BABP ) has a key role in the intracellular transport and metabolic targeting of salts. Similar to other members family lipid‐binding proteins ( iLBP s), disorder–order transitions local unfolding processes are thought mediate ligand entry release human I‐ . To gain insight into stability various regions, temperature response was investigated using NMR , CD fluorescence spectroscopy, as well molecular dynamics MD simulations. A joint analysis thermal...
Although successful in the structural determination of ordered biomolecules, spectroscopic investigation oligopeptides solution is hindered by their complex and rapidly changing conformational ensemble. The measured circular dichroism (CD) spectrum an oligopeptide ensemble average over all microstates, severely limiting its interpretation, contrast to biomolecules. Spectral deconvolution methods estimate secondary structure contributions are still mostly based on databases larger proteins....