ArticleBiophysical journal2015
Protein Conformational Changes Are Detected and Resolved Site Specifically by Second-Harmonic Generation.
Article in Biophysical journal, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 18 papers.
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Who cites it
18 citing papers in PubMed, 42 citations in OpenAlex.
- Quantifying protein unfolding kinetics with a high-throughput microfluidic platform.Cell systems · 2026Article
- Ligand-induced conformations and dynamic allosteric motions of IDO1 affecting the recruitment of a protein signaling partner.Communications chemistry · 2025Article
- Ligand-induced conformational changes in protein molecules detected by sum-frequency generation.Biophysical journal · 2024Article
- Monitoring In Vitro Extracellular Matrix Protein Conformations in the Presence of Biomimetic Bone-Regeneration Scaffolds Using Functionalized Gold-Edge-Coated Triangular Silver Nanoparticles.Nanomaterials (Basel, Switzerland) · 2022Article
- Discovery of fragments inducing conformational effects in dynamic proteins using a second-harmonic generation biosensor.RSC advances · 2021Article
- Using modern approaches to sedimentation velocity to detect conformational changes in proteins.European biophysics journal : EBJ · 2020Article
- Second harmonic generation detection of Ras conformational changes and discovery of a small molecule binder.Proceedings of the National Academy of Sciences of the United States of America · 2019Article
- Angular Mapping of Protein Structure Using Nonlinear Optical Measurements.Biophysical journal · 2019Article
- A hybrid, bottom-up, structurally accurate, Go¯-like coarse-grained protein model.The Journal of chemical physics · 2019Article
- New weapons to penetrate the armor: Novel reagents and assays developed at the NCI RAS Initiative to enable discovery of RAS therapeutics.Seminars in cancer biology · 2019Review
- Engineering a Single-Agent Cytokine/Antibody Fusion That Selectively Expands Regulatory T Cells for Autoimmune Disease Therapy.Journal of immunology (Baltimore, Md. : 1950) · 2018Article
- Identification of inactive conformation-selective interleukin-2-inducible T-cell kinase (ITK) inhibitors based on second-harmonic generation.FEBS open bio · 2018Article
- Ligand-Induced Conformational Changes in HSP90 Monitored Time Resolved and Label Free-Towards a Conformational Activity Screening for Drug Discovery.Angewandte Chemie (International ed. in English) · 2018Article
- Monomeric ephrinB2 binding induces allosteric changes in Nipah virus G that precede its full activation.Nature communications · 2017Article
- Cooperative binding mitigates the high-dose hook effect.BMC systems biology · 2017Article
- Evaluating the Contribution of Transition-State Destabilization to Changes in the Residence Time of Triazole-Based InhA Inhibitors.Journal of the American Chemical Society · 2017Article
- Biophysics in drug discovery: impact, challenges and opportunities.Nature reviews. Drug discovery · 2016Review
- Small Molecules Detected by Second-Harmonic Generation Modulate the Conformation of Monomeric α-Synuclein and Reduce Its Aggregation in Cells.The Journal of biological chemistry · 2015Article
Corrections and comments
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Authors and funding
6 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
We present here a straightforward, broadly applicable technique for real-time detection and measurement of protein conformational changes in solution. This method is based on tethering proteins labeled with a second-harmonic generation (SHG) active dye to supported lipid bilayers. We demonstrate our method by measuring the conformational changes that occur upon ligand binding with three well-characterized proteins labeled at lysine residues: calmodulin (CaM), maltose-binding protein (MBP), and dihydrofolate reductase (DHFR). We also create a single-site cysteine mutant of DHFR engineered within the Met20 catalytic loop region and study the protein's structural motion at this site. Using published x-ray crystal structures, we show that the changes in the SHG signals upon ligand binding are the result of structural motions that occur at the labeled sites between the apo and ligand-bound forms of the proteins, which are easily distinguished from each other. In addition, we demonstrate that different magnitudes of the SHG signal changes are due to different and specific ligand-induced conformational changes. Taken together, these data illustrate the potential of the SHG approach for detecting and measuring protein conformational changes for a wide range of biological applications.
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Registered trials
Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.