Podcasts about atomic force

The Sunday service audio from June 23rd, 2024

The reading of this week's lesson.

The Sunday service audio from December 17th, 2023

The reading of this week's lesson.

High-speed atomic force microscopy takes on intrinsically disordered proteins Transcript of this podcastHello and welcome to the NanoLSI podcast. Thank you for joining us today. In this episode we feature the latest research by Toshio Ando at the Kanazawa University NanoLSI, alongside Sonia Longhi at Aix-Marseille University and CNRS in France.The research described in this podcast was published in Nature Nanotechnology in November 2020 Kanazawa University NanoLSI websitehttps://nanolsi.kanazawa-u.ac.jp/en/High-speed atomic force microscopy takes on intrinsically disordered proteinsKanazawa University's pioneering high-speed atomic force microscope technology has now shed light on the structure and dynamics of some of life's most ubiquitous and inscrutable molecules – intrinsically disordered proteins. The study is reported in Nature Nanotechnology.Our understanding of biological proteins does not always correlate with how common or important they are. Half of all proteins, molecules that play an integral role in cell processes, are intrinsically disordered, which means many of the standard techniques for probing biomolecules don't work on them. Now researchers at Kanazawa University in Japan have shown that their home-grown high-speed atomic force microscopy technology can provide information not just on the structures of these proteins but also their dynamics.Understanding how a protein is put together provides valuable clues to its functions. The development of protein crystallography in the 1930s and 1950s brought several protein structures into view for the first time, but it gradually became apparent that a large fraction of proteins lack a single set structure making them intractable to xray crystallography. As they are too thin for electron microscopy, the only viable alternatives for many of these intrinsically disordered proteins are nuclear magnetic resonance imaging and small angle xray scattering. Data collected from these techniques are averaged over ensembles and so give no clear indication of individual protein conformations or how often they occur. Atomic force microscopy on the other hand is capable of nanoscale resolution biological imaging at high-speed, so it can capture dynamics as well as protein structures.So what kind of insights can high-speed AFM offer for these proteins? In this latest work researchers at Kanazawa University alongside collaborators in Japan, France and Italy applied the technique to study several intrinsically disordered proteins. They identified parameters defining the shape, size and chain length of protein regions, as well as a power law relating the protein size to the protein length. Not only that but they got a quantitative description of the effect of the mica surface on protein dimensions. The dynamics of the protein conformations captured thanks to the high-speed capabilities of the technique revealed globules that appear and disappear, and transformations between fully unstructured and loosely folded conformations in segments up to 160 amino acids long.Studies of the measles virus nucleoprotein in particular helped identify not just the shape and dimensions but also characteristics of the order-disorder transitions in the region responsible for molecular recognition, which allows viruses to identify host factors so that they can reproduce. They could also determine larger scale structures of the virus's phosphoprotein that are not accessible to nuclear magnetic resonance (which can only give an indication of distances between amino acids separated by less than 2 nm). The researchers suggest that the formation of certain compact shapes observed may explain the resistance to proteolysis – protein breakNanoLSI Podcast website

The Sunday service audio from June 18th, 2023

The reading of this week's lesson.

"Easy Physics" is a podcast that delves into the bizarre and fascinating world of this amazing science. Join us as we use humor and plain language to explore many foundamental principles, and learn about each one of them in a few minutes. From particles that exist in multiple places at once to the immensity of the cosmos, we'll take a lighthearted look at the most mind-bending concepts in physics.Get amazing T-Shirts on ⁠⁠⁠⁠⁠⁠RevanDesignStore⁠⁠⁠⁠⁠⁠, with free shipping for the US! Hosted on Acast. See acast.com/privacy for more information.

The Sunday service audio from December 18th, 2022

The reading of this week's lesson.

The Sunday service audio from June 19th, 2022

The reading of this week's lesson.

Kanazawa NanoLSI Research Podcast 26 May 2022 Small but mighty: Identifying nanosized molecules using atomic force microscopy In a recent study Mikihiro Shibata and Leonardo Puppulin at the WPI Nano Life Science Institute Kanazawa University (NanoLSI) used advanced atomic force microscopy to accurately recognize tiny cellular biomolecules. Learn more about their research here: WPI Kanazawa Nano Life Science Institutehttps://nanolsi.kanazawa-u.ac.jp/en/research/researchers/Original article:  https://pubs.acs.org/doi/10.1021/acsami.1c17708Transcript of this podcastHello and welcome to the NanoLSI podcast. Thank you for joining us today. In this episode we will feature the latest research published by Mikihiro Shibata and Leonardo Puppulin. They are both members of the nanometrology group at the Kanazawa University NanoLSI.The research described in this podcast was published in the American Chemical Society, Applied Materials  Interfaces, in November 2021.  Small but mighty: Identifying nanosized molecules using atomic force microscopyIn a study recently published in the journal Applied Materials and Interfaces researchers from Kanazawa University use advanced atomic force microscopy to accurately recognize tiny cellular biomolecules. Biologists rely on a wide range of microscopy techniques to visualize biomolecules within biological cells. High-speed atomic force microscopy (HS-AFM) is one such example in which a sharp tip attached to a sensor is used for visualizing cells. Specifically, as the AFM tip scans the surface of a molecule, the pattern of signals it generates enables researchers to visualize the molecule's topography. However, recognizing individual biomolecules using HS-AFM is still in its infancy. Now, researchers at Kanazawa University report on an innovative method to facilitate this by tweaking the structures of AFM tips.The research team, led by Mikihiro Shibata and Leonardo Puppulin at the WPI Nano Life Science Institute Kanazawa University (NanoLSI), characterized a protein found on human cells known as the hepatocyte growth factor receptor (hMET). The researchers first attached aMD4, a synthetic molecule that latches onto hMET, to the HS-AFM tip using different sized linkers. Patterns of connections between this modified tip and single molecules of hMET were subsequently investigated. When hMET on a mica surface (a material typically used in HS-AFM studies) was exposed to the tip, interactions between aMD4 and the external surface of hMET were indeed observed. However, when multiple molecules of aMD4 and hMET were used, it was found that shorter and more flexible linkers enabled aMD4 to interact with two adjacent hMET molecules bringing them closer together. This observation posits practical applications in the laboratory—biologists can potentially mimic the binding of two cell surface proteins together which often leads to the induction of cellular processes. Next, the specificity of this tip for molecule recognition was examined. hMET and its mouse form are very similar in structure. However, the mouse form does not bind to aMD4. Thus, when the aMD4-loaded tips were exposed to both forms of the protein, activity was observed only with the human form. This technique could therefore be useful in the selection of specific biomolecules from a heterogenous mix as is typically seen on the cell surface. Lastly, the modified HS-AFM technique was applied when hMET was bound to a lipid surface mimicking the structural composition of cell membranes (its natural home). Similar interactions were observed in this milieu suggesting

Kanazawa University research: Publication of an insightful reference book on high-speed atomic force microscopy (HS-AFM) for in situ biological applications  Pioneering biophysicist Professor Toshio Ando of the NanoLSI publishes his new book on high-speed atomic force microscopy (HS-AFM) for directly monitoring the dynamics of biomolecules. The book offers easy to understand descriptions of the basic technology and in situ biological applications of liquid HS-AFM. The book is ideal for students from multidisciplinary backgrounds interested in accelerating their research on high speed, in situ monitoring of biomolecules. NanoLSI Podcast where Professor Ando describes the background to the publication of the book and his thoughts about the future of HS-AFM.Link to Nano LSI Podcasthttps://nanolsi.kanazawa-u.ac.jp/en/announcements/nanolsipodcast/Professor Toshio Ando is internationally recognized as the pioneer of high speed atomic force microscopy for biological applications. “I first became aware of atomic force microscopy in the mid-eighties after I returned to Japan following several years in the USA,” says Ando. “I had just moved to Kanazawa University and was looking for new paths to explore. I was interested in directly observing the dynamics of proteins. This is when I decided to pursue research on the development of high speed liquid AFM (HS-AFM). Now, more than 30 years later, I want to share my experiences and insights into the technology and applications of HS-AFM. This book is my way of sharing my knowledge about this subject. It is the first book on this topic and hopefully it will inspire the development of the next generation of scanning probe microscopes for biology.” Professor Ando describes how he started his research on HS-AFMhttps://nanolsi.kanazawa-u.ac.jp/wp-content/uploads/2022/05/background-to-research-on-hs-afm.mp3Professor Ando describes why he decided to write this bookhttps://nanolsi.kanazawa-u.ac.jp/wp-content/uploads/2022/05/writing-the-book.mp3The future of high speed AFMProfessor Ando shares his views about the future of HS-AFMhttps://nanolsi.kanazawa-u.ac.jp/wp-content/uploads/2022/05/evolution-of-hs-afm.mp3Ando envisages continuous evolution in both the performance and applications of HS-AFM. “The scanning speed is an area of research being addressed by many groups globally,” says Ando. “In my group we are developing new methods, that is system operation procedures, and have achieved 40 frames per second (fps). Conventional systems enable around 10 fps. I expect advances in devices used for imaging will enable image rates of 100 fps within 3 to 4 years. So this area of research is still evolving.” Ando also foresees that many proteins that have been “untouched” to-date will be imaged by high performance HS-AFM systems. “I expect many more users of HS-AFM in the future,” says Ando. About the book Professor Ando describes the contents of the book https://nanolsi.kanazawa-u.ac.jp/wp-content/uploads/2022/05/audience-and-contents.mp3‘High Speed Atomic Force Microscopy in Biology” is published by Springer and is available as an eBook or hard cover [1]. The book consists of 18 chapters and more than 300 pages that include practical hints about the preparation of cantilever tips and sample surfaces, for example, to enable first time users to succes

Explore the significance of sonocytology, atomic force microscopy (AFM), and other nanoprobes to measure the sounds/songs from the cell, abiotic matierals, and to bioengineer cells beyond Earth from AFM sound pioneer Dr. James Gimzewski, Distinguished Professor of Chemistry at the UCLA and Director of the Nano & Pico Characterization Core. Topics include nanomechanical analysis of cells from cancer patients, quantifying intracellular frequencies, applications of AFM for eukaryotic/prokaryotic cells, piezoelectric actuators, data vibration/math acoustic analysis, microgravity (uG) experiments, and future research opportunities. References www.scienceabc.com/pure-sciences/how-do-our-cells-produce-sound.html Cross, Sarah E et al. “Nanomechanical analysis of cells from cancer patients.” Nature nanotechnology vol. 2,12 (2007): 780-3. https://doi.org/10.1038/nnano.2007.388 Kirmizis, Dimitrios, and Stergios Logothetidis. “Atomic force microscopy probing in the measurement of cell mechanics.” International journal of nanomedicine vol. 5 137-45. 7 Apr. 2010, doi:10.2147/ijn.s5787 --- This episode is sponsored by · Anchor: The easiest way to make a podcast. https://anchor.fm/app Support this podcast: https://anchor.fm/frontierspace/support

The Sunday service audio from December 19th, 2021

The reading of this week's lesson.

The text of this week's lesson.

Nick is joined by Racing Post journalist Maddy Playle to discuss the day's national and International racing news. Amongst topics discussed today are the comeback run of Tarnawa, featuring an interview with her rider Colin Keane, and the perceived exodus of good horses from the UK, highlighted by the departure of Prix Robert Papin winner Atomic Force to continue his career in Hong Kong. Bloodstock agent Alastair Donald offers some fresh perspective and explains why opportunities for this horse may be greater overseas. Nick and Maddy also examine whether geldings should be allowed in some of the key Group One races in Europe as well as considering the sluggish return of full crowds on Irish racecourses. Later in this edition, James Willoughby casts his expert eye over another tumultuous week in the TRC Global Rankings.

Nick is joined by Racing Post journalist Maddy Playle to discuss the day's national and International racing news. Amongst topics discussed today are the comeback run of Tarnawa, featuring an interview with her rider Colin Keane, and the perceived exodus of good horses from the UK, highlighted by the departure of Prix Robert Papin winner Atomic Force to continue his career in Hong Kong. Bloodstock agent Alastair Donald offers some fresh perspective and explains why opportunities for this horse may be greater overseas. Nick and Maddy also examine whether geldings should be allowed in some of the key Group One races in Europe as well as considering the sluggish return of full crowds on Irish racecourses. Later in this edition, James Willoughby casts his expert eye over another tumultuous week in the TRC Global Rankings.

The Sunday service audio from June 20th, 2021

In this episode Pranoti sits down with Pablo Ares, assistant Professor in the Condensed Matter Physics Department at the Autonomous University of Madrid at the time of recording, to take a deeper dive into Pablo‘s research journey. This vintage episode of the Under the Microscope podcast was originally released on 16.06.2021.

This episode's guest is Pablo Ares, who was an assistant Professor in the Condensed Matter Physics Department at the Autonomous University of Madrid at the time of recording. This vintage episode of the Under the Microscope podcast was originally released on 14.06.2021.

The text of this week's lesson.

The reading of this week's lesson.

This episode is also available as a blog post: http://imfrom.earth/2021/04/18/42-scientists-find-strong-evidence-for-new-mystery-sub-atomic-force-of-nature-bbc-news-youtube/ --- Send in a voice message: https://anchor.fm/imfromearth/message Support this podcast: https://anchor.fm/imfromearth/support

Professor Mark MacLachlan is an overseas-based principal investigator at the NanoLSI WPI Kanazawa University and faculty at the University of British Columbia. Here, he describes his research on the development of AFM tips functionalized with innovative cellulose nanocrystals for ultra-low invasive insights into the chemical composition of living cells. The Kanazawa University NanoLSI Podcast offers updates of the latest news and research at the WPI-NanoLSI Kanazawa University. The Nano Life Science Institute (NanoLSI) at Kanazawa University was established in 2017 as part of the World Premier International (WPI) Research Center Initiative of the Ministry of Education, Culture, Sports, Science and Technology (MEXT). Researchers at the NanoLSI are combining their cutting-edge expertise in scanning probe microscopy to establish ‘nano-endoscopic techniques' to directly image, analyze, and manipulate biomolecules for insights into mechanisms governing life phenomena such as diseases.Further informationWPI-NanoLSI Kanazawa University website  https://nanolsi.kanazawa-u.ac.jp/en/

The Sunday service audio from December 20th, 2020

The Sunday service audio from December 20th, 2020

The reading of this week's lesson.

The text of this week's lesson.

The reading of this week's lesson.

Link to bioRxiv paper: http://biorxiv.org/cgi/content/short/2020.08.10.242719v1?rss=1 Authors: Kubo, S., Kato, S., Nakamura, K., Kodera, N., Takada, S. Abstract: High-speed atomic force microscopy (HS-AFM) is a scanning probe microscopy that can capture structural dynamics of biomolecules in real time at single molecule level near physiological condition. Albeit much improvement of the instruments, while scanning one frame of HS-AFM movies, biomolecules often change their conformations largely. Thus, the obtained frame images can be hampered by the time-difference, the asynchronicity, in the data acquisition. Here, to resolve this data asynchronicity in the HS-AFM movie, we developed Kalman filter and smoother methods, some of the sequential Bayesian filtering approaches. The Kalman filter/smoother methods use alternative steps of a short time-propagation by a linear dynamical system and a correction by the likelihood of AFM data acquired pixel by pixel. We first tested the method using a toy model of a diffusing cone, showing that the Kalman smoother method outperforms to reproduce the ground-truth movie, compared to that mimics the raw AFM movie, and the Kalman filter result. We then applied the Kalman smoother to a synthetic movie for conformational change dynamics of a motor protein, i.e., dynein, confirming the superiority of the Kalman smoother. Finally, we applied the Kalman smoother to two real HS-AFM movies, FlhAc and centralspindlin, reducing distortion and noise in the AFM movies. The method is general and can be applied to any HS-AFM movies. Copy rights belong to original authors. Visit the link for more info

The Sunday service audio from June 21st, 2020

The Sunday service audio from June 21st, 2020

The reading of this week's lesson.

The text of this week's lesson.

The reading of this week's lesson.

The Sunday service audio from December 22nd, 2019

The Sunday service audio from December 22nd, 2019

The text of this week's lesson.

The reading of this week's lesson.

I read from atomic force microscope to atom smasher. The word of the episode is "atomic theory". https://en.wikipedia.org/wiki/Atomic_theory dictionarypod@gmail.com https://www.facebook.com/thedictionarypod/ https://twitter.com/dictionarypod https://www.instagram.com/dictionarypod/ https://www.patreon.com/spejampar 917-727-5757

The reading of this week's lesson.

The Sunday service audio from June 23rd, 2019

The Sunday service audio from June 23rd, 2019

The text of this week's lesson.

The reading of this week's lesson.

The reading of this week's lesson.

Tue, 20 Oct 2009 12:00:00 +0100 https://edoc.ub.uni-muenchen.de/11479/ https://edoc.ub.uni-muenchen.de/11479/1/Erdmann_Matthias.pdf Erdmann, Matthias ddc:530, ddc

A wide range of applications: companies that specialise in scanning probe microscopy use different types of tip to create atomic resolution images.

Transcript -- How it works and what it can do. A close look at it's probe, using an electron microscope.

Transcript -- A wide range of applications: companies that specialise in scanning probe microscopy use different types of tip to create atomic resolution images.

How it works and what it can do. A close look at it's probe, using an electron microscope.

Transcript -- A wide range of applications: companies that specialise in scanning probe microscopy use different types of tip to create atomic resolution images.

A wide range of applications: companies that specialise in scanning probe microscopy use different types of tip to create atomic resolution images.

Transcript -- How it works and what it can do. A close look at it's probe, using an electron microscope.

How it works and what it can do. A close look at it's probe, using an electron microscope.

The object of this thesis is the development of theoretical and experimental methods for the controlled manipulation of surfaces at the nanometer scale, including the design, construction and experimental demonstration of an atomic force microscope (AFM) based manipulator. The transfer function description of an AFM system not only offers a theoretical dynamic characterization but, additionally, it is appropriate for the analysis of stability and controllability of different system configurations, i.e. different inputs and outputs. In this thesis, transfer functions are derived that correspond to a realistic model of the AFM sensor, including all its resonance modes and the tip-sample interaction. This theoretical description is then validated using the frequency response along an AFM cantilever. Different experimental and control techniques have been combined in the NanoManipulator system to optimize AFM lithography. Optical video microscopy allows a fast recognition of the sample and exact positioning of the AFM tip in the particular region of interest, while UV-laser ablation offers the possibility of noncontact manipulation of a wide range of materials, including biological specimens. Two different control approaches have been implemented in the NanoManipulator system: (i) automated control using a vector-scan module, and (ii) interactive control based on the use of a haptic interface. Using the NanoManipulator, the two different standard AFM lithography techniques based on dynamic methods (namely dynamic and modulated plowing) are compared by performing nanopatterning on thin resist films. The results reflect that modulated plowing, where the AFM tip is in permanent contact with the resist surface while the force is being modulated, offers the highest reliability, minimizing undesired side effects. The isolation and extraction of localized regions of human metaphase chromosomes represents a promising alternative to standard methods for the analysis of genetic material. The NanoManipulator is an excellent tool for such application, as it is here illustrated by comparing AFM based mechanical dissection and noncontact ablation on side by side chromosomes. The results are analyzed in situ using AFM imaging, revealing the high precision of mechanical dissection. Acoustical force nanolithography is a novel method for AFM based lithography where the cantilever is actuated using an acoustic wave coupled through the sample surface. The influence of acoustic wave frequency and magnitude, along with the preloading force of the cantilever are studied in detail. Acoustical force nanolithography can be used as a stand alone method or as a complement for the fine adjustment of manipulation forces.

In the past 25 years many techniques have been developed to characterize cell adhesion and to quantify adhesion forces. Atomic force microscopy (AFM) has been used to measure forces in the pico-newton range, an experimental technique known as force spectroscopy. We modified such an AFM to measure adhesion forces between live cells or between cells and surfaces. This strategy required functionalizing the surface of the sensors for immobilizing the cell. We used Dictyostelium discoideum cells which respond to starvation by surface expression of the adhesion molecule csA and consequent aggregation to measure the adhesion force of a single csA-csA bond. Relevant experimental parameters include the duration of contact between the interacting surfaces, the force against which this contact is maintained, the number and specificity of interacting adhesion molecules and the constituents of the medium in which the interaction occurs. This technology also permits the measurement of the viscoelastic properties of single cells or cell layers. Copyright (C) 2002 S, Karger AG, Basel.

We have imaged adsorbed fluid lipid bilayers by atomic force microscopy. The patches were formed by rupture of phospholipid vesicles onto magnesium fluoride. We show that the membrane patches are fluid but can be stably imaged at scan rates higher than 6 p d s . At lower scan rates the tip penetrates through the layer. The penetrating tip does not destroy the fluid patches, and the previous image can be restored after increasing the scanning velocity. The dynamic forces that possibly explain the effect are discussed.