A5048961213- RNA and protein synthesis mechanisms
- Cell Adhesion Molecules Research
- Genomics and Chromatin Dynamics
- DNA and Nucleic Acid Chemistry
- DNA Repair Mechanisms
- RNA Interference and Gene Delivery
- RNA modifications and cancer
- Pesticide Residue Analysis and Safety
- Insect Pest Control Strategies
- Cellular Mechanics and Interactions
- Bacteriophages and microbial interactions
- Mitochondrial Function and Pathology
- Protease and Inhibitor Mechanisms
- Synthetic Organic Chemistry Methods
- Bacterial Genetics and Biotechnology
- Mesoporous Materials and Catalysis
- Insect Resistance and Genetics
- Protein Interaction Studies and Fluorescence Analysis
- Pesticide Exposure and Toxicity
- Porphyrin and Phthalocyanine Chemistry
- S100 Proteins and Annexins
- Plant Virus Research Studies
- RNA Research and Splicing
- Cellular transport and secretion
- Skin and Cellular Biology Research
Massachusetts Institute of Technology
2022
National Heart Lung and Blood Institute
2021
National Institutes of Health
2021
University of Lausanne
2017-2021
Integrin α 5 β 1 structures in resting and active states with ligand fibronectin reveal key interactions for integrin opening.
SMC proteins support vital cellular processes in all domains of life by organizing chromosomal DNA. They are composed ATPase "head" and "hinge" dimerization a connecting coiled-coil "arm." Binding to kleisin subunit creates closed tripartite ring, whose ∼47-nm-long arms act as barrier for DNA entrapment. Here, we uncover another, more active function the bacterial Smc arm. Using high-throughput genetic engineering, resized arm range 6-60 nm found that it was functional only specific length...
Multi-subunit SMC ATPases control chromosome superstructure apparently by catalyzing a DNA-loop-extrusion reaction. proteins harbor an ABC-type ATPase "head" and "hinge" dimerization domain connected coiled coil "arm." Two arms in dimer can co-align, thereby forming rod-shaped particle. Upon ATP binding, heads engage, are thought to separate. Here, we study the shape of Bacillus subtilis Smc-ScpAB electron-spin resonance spectroscopy. Arm separation is readily detected proximal absence...
Pesticides are used extensively in agriculture, and their residues food must be monitored to prevent toxicity. The most abundant protein cow’s milk, β-lactoglobulin (BLG), shows high affinity for diverse hydrophobic ligands its central binding pocket, called the calyx. Several of frequently pesticides hydrophobic. To predict if BLG may an unintended carrier pesticides, we tested ability bind 555 isomers, a total 889 compounds, rigid docking screen. We focused on analysis 60 unique molecules...
Summary Multi-subunit SMC ATPases control chromosome superstructure apparently by catalyzing a DNA-loop-extrusion reaction. proteins harbor an ABC-type ATPase ‘head’ and ‘hinge’ dimerization domain connected coiled coil ‘arm’. Two arms in dimer can co-align, thereby forming rod-shaped particle. Upon ATP binding, heads engage, are thought to separate. Here, we studied the shape of B. subtilis Smc-ScpAB electron-spin resonance spectroscopy. Arm separation was readily detected proximal absence...
Summary Multi-subunit SMC ATPase complexes translocate on chromosomal DNA. They control chromosome structure and DNA topology, presumably by acting as extrusion motors. The SMC-kleisin ring entraps lumen is strongly reduced in size alignment of the arms upon ATP binding divided two engagement head domains. Here, we provide evidence for S MC compartment entrapment K leisin B. subtilis Smc/ScpAB. We show that at Smc hinge dispensable identify an essential site engaged heads which faces...
Molecular mechanics calculations (MM3-92) suggest that a slightly distorted diaxial chair conformation of trans-1,2-bis(trimethylsilyl)cyclohexane is at least 1.26 kcal mol-1 (1 cal = 4.184 J) lower in steric energy than the diequatorial form, and this supported by NOED spectra, magnitudes vic-1H–1H spin coupling constants, low temperature (190 K) 13C NMR spectroscopic measurements, which place free difference between 1.5 1.7 mol-1.