Search Results - "Main, Ewan R.G."
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Scalable Geometrically Designed Protein Cages Assembled via Genetically Encoded Split Inteins
Published in Structure (London) (07-05-2019)“…Engineering proteins to assemble into user-defined structures is key in their development for biotechnological applications. However, designing generic rather…”
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Repeat protein engineering: creating functional nanostructures/biomaterials from modular building blocks
Published in Biochemical Society transactions (01-10-2013)“…There is enormous interest in molecular self-assembly and the development of biological systems to form smart nanostructures for biotechnology (so-called…”
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Dissecting and reprogramming the folding and assembly of tandem-repeat proteins
Published in Biochemical Society transactions (01-10-2015)“…Studying protein folding and protein design in globular proteins presents significant challenges because of the two related features, topological complexity…”
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A high-throughput fluorescence chemical denaturation assay as a general screen for protein–ligand binding
Published in Analytical biochemistry (01-04-2011)“…Chemical denaturation of ligand–protein complexes can provide the basis of a label-free binding assay. Here, we show how the technique can be used as a…”
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Mapping the Interactions Present in the Transition State for Unfolding/Folding of FKBP12
Published in Journal of molecular biology (13-08-1999)“…The structure of the transition state for folding/unfolding of the immunophilin FKBP12 has been characterised using a combination of protein engineering…”
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Exploring the “N-Terminal Anchor” Binding Interface of the T3SS Chaperone–Translocator Complexes from P. aeruginosa
Published in Biochemistry (Easton) (18-04-2023)“…The type III secretion system is a large multiprotein complex that many Gram-negative bacteria use for infection. A crucial part of the complex is its…”
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Exploring the ‘N-terminal arm’ & ‘Convex surface’ Binding Interfaces of the T3SS Chaperone-Translocator Complexes from P. Aeruginosa
Published in Journal of molecular biology (01-08-2023)“…[Display omitted] •Major/Minor Translocator-chaperone complexes are crucial for effective T3SS operation.•Specificity of P. aeruginosa major/minor…”
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Context-Dependent Energetics of Loop Extensions in a Family of Tandem-Repeat Proteins
Published in Biophysical journal (05-06-2018)“…Consensus-designed tetratricopeptide repeat proteins are highly stable, modular proteins that are strikingly amenable to rational engineering. They therefore…”
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Decoupling a tandem-repeat protein: Impact of multiple loop insertions on a modular scaffold
Published in Scientific reports (28-10-2019)“…The simple topology and modular architecture of tandem-repeat proteins such as tetratricopeptide repeats (TPRs) and ankyrin repeats makes them straightforward…”
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PyFolding: Open-Source Graphing, Simulation, and Analysis of the Biophysical Properties of Proteins
Published in Biophysical journal (06-02-2018)“…For many years, curve-fitting software has been heavily utilized to fit simple models to various types of biophysical data. Although such software packages are…”
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Fibrous Nanostructures from the Self-Assembly of Designed Repeat Protein Modules
Published in Angewandte Chemie International Edition (21-12-2012)“…Single‐protein‐chain superhelical filaments are obtained from monomeric repeat proteins by controlling the chemistry and solvent exposure at their terminal…”
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Design of Stable α-Helical Arrays from an Idealized TPR Motif
Published in Structure (London) (01-05-2003)“…The tetratrico peptide repeat (TPR) is a 34-amino acid α-helical motif that occurs in over 300 different proteins. In the different proteins, three to sixteen…”
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Programmed Protein Self-Assembly Driven by Genetically Encoded Intein-Mediated Native Chemical Ligation
Published in ACS synthetic biology (20-04-2018)“…Harnessing and controlling self-assembly is an important step in developing proteins as novel biomaterials. With this goal, here we report the design of a…”
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Exploring the Folding Energy Landscape of a Series of Designed Consensus Tetratricopeptide Repeat Proteins
Published in Proceedings of the National Academy of Sciences - PNAS (13-10-2009)“…Repeat proteins contain short, tandem arrays of simple structural motifs (20-40 aa). These stack together to form nonglobular structures that are stabilized by…”
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LcrH, a Class II Chaperone from the Type Three Secretion System, Has a Highly Flexible Native Structure
Published in The Journal of biological chemistry (08-02-2013)“…The type three secretion system is a large and complex protein nano-machine that many Gram-negative pathogens employ to infect host cells. A key structure of…”
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A New Folding Paradigm for Repeat Proteins
Published in Journal of the American Chemical Society (27-07-2005)“…The folding/unfolding transitions of a series of designed consensus tetratricopeptide repeat proteins are quantitatively described by the classical…”
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A recurring theme in protein engineering: the design, stability and folding of repeat proteins
Published in Current opinion in structural biology (01-08-2005)“…Repeat proteins are ubiquitous and are involved in a myriad of essential processes. They are typically non-globular structures that act as diverse scaffolds…”
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The folding and design of repeat proteins: reaching a consensus
Published in Current opinion in structural biology (01-08-2003)“…Although they are widely distributed across kingdoms and are involved in a myriad of essential processes, until recently, repeat proteins have received little…”
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Protein folding: Defining a “standard” set of experimental conditions and a preliminary kinetic data set of two‐state proteins
Published in Protein science (01-03-2005)“…Recent years have seen the publication of both empirical and theoretical relationships predicting the rates with which proteins fold. Our ability to test and…”
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Local and Long-Range Stability in Tandemly Arrayed Tetratricopeptide Repeats
Published in Proceedings of the National Academy of Sciences - PNAS (19-04-2005)“…The tetratricopeptide repeat (TPR) is a 34-aa α-helical motif that occurs in tandem arrays in a variety of different proteins. In natural proteins, the number…”
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