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Search theses and dissertations gathered from participating repositories worldwide. Every result links back to the library that holds it. No account is needed.
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Showing 1 to 20 of 29 for “"Cryoem"”.
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Protein Loop Length Estimation From Medium Resolution Cryoem Images
… PDB (Protein Databank). Cryoelectron Microscopy (cryoEM) is an important biophysical technique that produces 3D subnanometer resolution images of molecules not amenable to past approaches like x-ray crystallography or nuclear magnetic resonance. De novo modeling is becoming a promising approach to …
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Hardware developments to improve image quality for cryoEM of biological specimens
Several advances in cryoEM hardware have been integral in transforming the technique into a standard technique for high-resolution macromolecular structure determination. We are now entering an era where we can experimentally determine or predict the structure of almost the entire proteome. Efforts …
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De Novo Protein Structure Modeling from Cryoem Data Through a Dynamic Programming Algorithm in the Secondary Structure Topology Graph
… determination, Electron Cryorricroscopy (CryoEM) is able to produce volumetric maps of proteins that are poorly soluble, large and hard to crystallize. Furthermore, it studies the proteins in their native environment. Unfortunately, the volumetric maps generated by current advances in …
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Machine learning for understanding protein sequence and structure
… Recent advances in cryo-electron microscopy (cryoEM) has enabled high resolution experimental measurement of proteins in their native states. However, this technology remains expensive and low throughput. At the same time, ever growing protein databases offer new opportunities for …
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The physical origins of specimen movement in electron cryomicroscopy and how to eliminate it
Electron cryomicroscopy (cryoEM) is an important imaging technique for determining the atomic structures of biological macromolecules and complexes. Success in determining a structure by cryoEM depends on being able to prepare a thin frozen specimen of the molecules of interest on a small metal …
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Advances In Computer Aided Protein Structure Determination From Sparse Cryo Electron Microscopy Data
Single-particle cryo-electron microscopy (cryoEM) has become a powerful tool for determining macromolecular structures. Thanks to recent advances in direct electron detectors and motion correction algorithms it can frequently deliver electron density maps in the range of 3-5Å resolution. To obtain …
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INSIGHTS INTO POLYMERISATION OF FTSZ AND OTHER CYTOMOTIVE FILAMENTS
… crystallography and electron cryomicroscopy (cryoEM) that FtsZ switches conformation when it polymerises into filaments. I then show using cryoEM that this conformational switch is likely needed for recognition of filaments by the widely conserved filament cross-linking protein ZapA. I also …
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NON-FOULING AFFINITY PLATFORMS FOR PROTEIN IMMOBILIZATION IN ELECTRON MICROSCOPY
… for the preparation of a purified sample for cryoEM analysis from an E. coli expression system. The selective and reversible capture of his-tag T7 bacteriophage, RplL, and GroEL from crude lysates, as well as purified nanodisc-solubilized his-malFGK2, on these NTA-modified grids with an …
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Replaying Life's Tape With Intraclonal Germinal Center Evolution
… scanning (DMS) and cryo-electron microscopy (CryoEM). DMS elucidated that chIgY B cells must avoid ~13 deleterious mutations in order to make one affinityincreasing mutations. CryoEM revealed that central paratope of clone 2.1 is largely optimal in its ability to bind chIgY, but it can be …
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Recruitment and Mechanism of the Bacterial Type IV Pilus Motors
… with the structure used for this analysis. CryoEM analysis revealed PilT, but not PilB, has preferences for conformation that are obscured by crystal lattice formation. The physiologic importance of these conformations was validated, allowing for the proposal of the most comprehensive model …
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The Interaction of Cofilin with the Actin Filament
… much more elusive. As of yet, there are only cryoEM models of cofilin-bound F-actin: where the binding occurs at a 1:1 ratio), which are not high enough resolution and do not show molecular interactions. The focus of this research is to build a model of how cofilin binds F-actin and understand …
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Structural and Dynamic Proximal Proteomic Analysis of TRPV2 Ion Channel Activation
… channel opening, cryogenic-electron microscopy (cryoEM) was used to determine the structures of TRPV2 upon pharmacological activation. Using this cutting-edge structural technique, we were able to elucidate high resolution structures of TRPV2 bound to the pharmacological activators 2-APB and CBD, …
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The role of RNA modifications in mitochondrial translation
… details of its structure were investigated by cryoEM, revealing the persistence of a late stage assembly containing the anti-association MALSU1:SMCR7L:mtACP complex and unfolded interfacial rRNA. Pseudouridine (Ψ), the most common RNA modification found in cells, is also present in mtRNAs. …
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The study of ancient viral class II envelope fusion proteins within the viral retroelements of Nematoda and the nuclear plasmids of Dictyostelium
… as a member of the genus Semotivirus. A 3.76 Å cryoEM reconstruction of the encoded membrane fusion machinery of the A. ceylanicum retroelement shows that it is a phleboviral homologue and class II fusion protein. Biophysical and biochemical characterization indicate this ancient class II fusion …
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Prosthecobacter BtubAB form bacterial mini microtubules
… structure of the in vitro BtubAB filament using cryoEM and cryoET, revealing a hollow tube that consists of four protofilaments. A closer look showed that BtubAB filaments have many conserved microtubule features including: an overall polarity, similar longitudinal contacts, M-loops in lateral …
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Investigating complex I dynamics and ROS production in ischaemia-reperfusion injury
… with the Hirst laboratory we combined cryoEM derived structural information from their lab with in vivo data from a myocardial infarction model that enabled us to identify the RET-blocking mechanism caused by this mutation and to confirm RET derived ROS as major cause for IR injury. In …
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Structural and functional role of the extracellular loops and C-terminal domain of the voltage-gated sodium ion channel
… determined by cryogenic electron microscopy (cryoEM), the wild-type residues that correspond to some of these mutants form a complex salt bridge at the interface between the DII and DIII turret loops. Furthermore, adjacent aromatic residues could potentially form cation-π interactions with the …
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Computational Development for Secondary Structure Detection From Three-Dimensional Images of Cryo-Electron Microscopy
… and 39 β-sheets computationally detected from cryoEM density maps at 4.4-7.4Å resolutions. <em>StrandTwister</em> appears to detect the traces of β-strands on major β-sheets quite accurately, particularly at the central area of a β-sheet.</p> <p>β-barrel is a structure feature that is formed by …
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Integration of Structural Methods to Characterize the Dynamics of Macromolecular Complexes
Our understanding of the mechanism of protein function has been continuously adapted to be consistent with new experimental and theoretical findings. Eventually, the idea of a relationship between the structure and function of proteins emerged. As the methods available to probe structure became …
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Novel Structures of RAD51 Reveal Mechanisms in DNA Damage Repair and Genomic Stability
The RAD51 protein contributes to the maintenance of genomic stability by promoting the repair of DNA double-strand breaks and the protection of DNA replication forks. RAD51 functions alongside the tumour suppressor protein BRCA2 to catalyse DNA strand-exchange reactions which form an integral part …
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