A5081892612- Protein Structure and Dynamics
- Enzyme Structure and Function
- Monoclonal and Polyclonal Antibodies Research
- RNA and protein synthesis mechanisms
- Mass Spectrometry Techniques and Applications
- Molecular spectroscopy and chirality
- Biosimilars and Bioanalytical Methods
- vaccines and immunoinformatics approaches
- Genomics and Chromatin Dynamics
- nanoparticles nucleation surface interactions
- Diffusion and Search Dynamics
- Cellular Mechanics and Interactions
- Heat shock proteins research
- Microfluidic and Bio-sensing Technologies
- Prion Diseases and Protein Misfolding
- Bacteriophages and microbial interactions
Cadence Design Systems (United States)
2023-2024
University of California, Merced
2018-2023
Institute of Genomics and Integrative Biology
2015
Therapeutic antibody discovery often relies on in-vitro display methods to identify lead candidates. Assessing selected output diversity traditionally involves random colony picking and Sanger sequencing, which has limitations. Next-generation sequencing (NGS) offers a cost-effective solution with increased read depth, allowing comprehensive understanding of diversity. Our study establishes NGS guidelines for drug discovery, demonstrating its advantages in expanding the number unique HCDR3...
Intrinsically disordered proteins (IDPs) fold upon binding to select/recruit multiple partners, morph around the partner's structure, and exhibit allostery. However, we do not know whether these properties emerge passively from disorder, or rather are encoded into IDP's folding mechanisms. A main reason for this gap is lack of suitable methods dissect energetics IDP conformational landscapes without partners. Here introduce such an approach that term molecular LEGO, apply it NCBD, a helical,...
Many proteins comprising of complex topologies require molecular chaperones to achieve their unique three-dimensional folded structure. The E.coli chaperone, GroEL binds with a large number unfolded and partially proteins, facilitate proper folding prevent misfolding aggregation. Although the major structural components are well defined, scaffolds non-native substrates that determine chaperone-mediated have been difficult recognize. Here we performed all-atomistic replica-exchange dynamics...
Many proteins are partially disordered in physiological conditions and only fold, fully or partially, upon binding. Their structural analysis is challenging because the accessible information, typically chemical shifts (CS) from nuclear magnetic resonance experiments, averages over broad ensembles of conformations. We aim to develop a database for such data terms conformational distributions protein backbone rather than individual high-resolution structures.Glutton largest available linking...
Canonical proteins fold and function as conformational switches that toggle between their folded (on) unfolded (off) states, a mechanism also provides the basis for engineering transducers biosensor applications. One of limitations such transducers, however, is relatively narrow operational range, limited to ligand concentrations 20-fold below or above C50. Previously, we discovered certain fast-folding lose/gain structure gradually (downhill folding), which led us postulate operation...
Abstract DNA scanning proteins slide on the assisted by a clamping interface and uniquely recognize their cognate sequence motif. The transcription factors that control cell fate in eukaryotes must forgo these elements to gain access both naked chromatin, so whether or how they scan is unknown. Here we use single-molecule techniques investigate Engrailed homeodomain (enHD) as paradigm of promiscuous recognition open interaction. We find enHD scans fast extensively conventional scanners...