NanoWorld USC-F1.2-k0.15 Ultra-Short AFM cantilevers [C = 0.15 N/m; fo = 1200 kHz] were used for the high speed imaging.
The HighSpeedScanning webpage is dedicated to presenting information about ultra high frequency AFM probe solutions for High Speed AFM ranging from already commercialized AFM probes such as the ArrowTM UHF and NanoWorld Ultra-Short Cantilever (USC) series to AFM probes that are still under development.
We are aware that these lists are far from complete and we are constantly working on keepting them up to date. If your research institute or company is working with High Speed AFM (HS-AFM) using our AFM probes or if you have published articles with images that were achieved with our High Speed AFM probes annd you find that are missing from our list then please let us know via email: email@example.com if you would like us to add them to the list of references .
Membrane proteins (MPs) reside in the plasma membrane and perform various biological processes including ion transport, substrate transport, and signal transduction.*
Function-related conformational changes in membrane proteins occur in times scales ranging from nanoseconds to seconds.*
Obtaining time-resolved dynamic information of MPs in their membrane environment is still a major challenge.*
Although High Speed Atomic Force Microscopy (HS-AFM) images label-free samples such as DNA, soluble proteins, MPs, and intrinsically disordered proteins at ~1n~m lateral, ~0.1 nm vertical and ~100 ms temporal solution in aqueous environment and at ambient temperature and pressure, its temporal resolution is too slow to characterize many dynamic biological processes.*
In order to overcome this limitation Raghavendar Reddy Sanganna Gari, Joel José Montalvo-Acosta, George R. Heath, Yining Jiang, Xiaolong Gao, Crina M. Nimigean, Christophe Chipot and Simon Scheuring in their article Correlation of membrane protein conformational and functional dynamics use High Speed Atomic Force Microscopy Height Spectroscopy ( HS-AFM-HS) to characterize the microsecond timescale conformational changes of an integral-MP model system, i.e., the outer membrane protein G (OmpG) in a membrane environment.*
The positioning of the AFM tip is guided by HS-AFM imaging immediately before HS-AFM-HS-operation.*
NanoWorld Ultra-Short Cantilevers (USC) of the USC-F1.2-k0.15 type were used for the HS-AFM and HS-AFM-HS presented in the article.*
*Raghavendar Reddy Sanganna Gari, Joel José Montalvo-Acosta, George R. Heath, Yining Jiang, Xiaolong Gao, Crina M. Nimigean, Christophe Chipot and Simon Scheuring Correlation of membrane protein conformational and functional dynamics Nature Communications volume 12, Article number: 4363 (2021) DOI: https://doi.org/10.1038/s41467-021-24660-1
Open Access : The article “Correlation of membrane protein conformational and functional dynamics” by Raghavendar Reddy Sanganna Gari, Joel José Montalvo-Acosta, George R. Heath, Yining Jiang, Xiaolong Gao, Crina M. Nimigean, Christophe Chipot and Simon Scheuring is licensed under a Creative Commons Attribution 4.0 International License, which permits use, sharing, adaptation, distribution and reproduction in any medium or format, as long as you give appropriate credit to the original author(s) and the source, provide a link to the Creative Commons license, and indicate if changes were made. The images or other third party material in this article are included in the article’s Creative Commons license, unless indicated otherwise in a credit line to the material. If material is not included in the article’s Creative Commons license and your intended use is not permitted by statutory regulation or exceeds the permitted use, you will need to obtain permission directly from the copyright holder. To view a copy of this license, visit https://creativecommons.org/licenses/by/4.0/.
Johannes Kepler University in Linz Austria has published a High-Speed Atomic Force Microscopy video of human lectin CLEC4G binding to glycans on a SARS-CoV-2 spike. This video was recorded by Daniel Canena and Peter Hinterdorfer and is, according to the two researchers, the first short film of the active structure the virus uses to attach to cell