مؤتمر
Single Molecule Studies of Membrane Proteins on Glass Substrates using Atomic Force Microscopy
| العنوان: | Single Molecule Studies of Membrane Proteins on Glass Substrates using Atomic Force Microscopy |
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| المؤلفون: | Chada, Nagaraju, Sigdel, Krishna, Matin, Tina, Sanganna Gari, Raghavendar Reddy, Mao, Chunfeng, Randall, Linda, King, Gavin |
| سنة النشر: | 2014 |
| المجموعة: | Zenodo |
| مصطلحات موضوعية: | Biological Physics, Biochemistry, Atomic force microscope imaging, AFM, Protein Translocation, Bacteriorhodopsin bR, Escherichia coli, Halobacterium salinarum, SecA ATPase motor protein, Single Molecule, Membrane Proteins, Glass Chemical Treatment, Glass Etching, Glass Micro-machining, Protein-protein interactions, Surface roughness of Glass, Surface roughness of Mica, Surface roughness of Lipid bilayer, Midwest Single Molecule Workshop, Lipid Membrane, Purple Membrane, Transmembrane protein, SecYEG, Sec Pathway, Motor Proteins |
| الوصف: | 1) Method for for integration of high resolution biological AFM with other powerful optical techniques 2) Straight-forward cleaning procedure for treatment of glass for Microscopy and Micromachining applications 3) Molecular high resolution imaging of bacteriorhodopsin and Sec translocase on glass supports 4) Direct observation of protein-protein interactions 5) Atomic Force Microscopy measurements of surface roughness of Glass, Mica, Lipid and comparison of several glass chemical treatments for Microscopy READ THE PEER-REVIEWED PUBLICATION HERE ASSOCIATED PEER-REVIEWED PUBLICATION Abstract Since its invention in the mid-1980s, the atomic force microscope (AFM) has become a valuable complementary tool for studying membrane proteins in near-native environments. Historically, mica is the most common substrate utilized for biological AFM. Glass being amorphous, transparent, and optically homogeneous has its own set of advantages over mica and has the potential to broaden the overlap of AFM with techniques that require high quality non-birefringent optical access. The use of silanized glass as an AFM substrates has been reported as a means to fine tune surface chemistry. However, such coatings usually require hours of additional preparation time and can lead to increased surface roughness. In this work, we present a simple technique for preparing borosilicate glass as a substrate for two membrane protein systems: non-crystalline translocons (SecYEG) of the general secretary system from E. coli, and bacteriorhodopsin (BR) from H. salinarum. For both these membrane proteins, quantitative comparisons of the measured protein structures on glass versus mica substrates show agreement. An additional advantage of glass is that lipid coverage is rapid (< 1 minute) and complete (occupying the entire surface). A goal is to study the bacterial export system using recently developed precision measurement techniques such as ultra-stable AFM. |
| نوع الوثيقة: | conference object still image |
| اللغة: | English |
| العلاقة: | https://zenodo.org/record/4016547Test; https://doi.org/10.5281/zenodo.4016547Test; oai:zenodo.org:4016547 |
| DOI: | 10.5281/zenodo.4016547 |
| الإتاحة: | https://doi.org/10.5281/zenodo.4016547Test https://doi.org/10.5281/zenodo.4016546Test https://zenodo.org/record/4016547Test |
| حقوق: | info:eu-repo/semantics/openAccess ; https://creativecommons.org/licenses/by/4.0/legalcodeTest |
| رقم الانضمام: | edsbas.6033C026 |
| قاعدة البيانات: | BASE |
| DOI: | 10.5281/zenodo.4016547 |
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