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All Outputs (36)

Rational design of peptide-based building blocks for nanoscience and synthetic biology (2009)
Journal Article
Armstrong, C., Boyle, A., Bromley, E., Mahmoud, Z., Smith, L., Thomson, A., & Woolfson, D. (2009). Rational design of peptide-based building blocks for nanoscience and synthetic biology. Faraday Discussions, 143, 305-317

The rational design of peptides that fold to form discrete nanoscale objects, and/or self-assemble into nanostructured materials is an exciting challenge. Such efforts test and extend our understanding of sequence-to-structure relationships in protei... Read More about Rational design of peptide-based building blocks for nanoscience and synthetic biology.

The Tumbleweed: towards a synthetic protein motor (2009)
Journal Article
Bromley, E., Kuwada, N., Zuckermann, M., Donadini, R., Samii, L., Blab, G., …Linke, H. (2009). The Tumbleweed: towards a synthetic protein motor. HFSP journal, 3(3), 204-212

Biomolecular motors have inspired the design and construction of artificial nanoscale motors and machines based on nucleic acids, small molecules, and inorganic nanostructures. However, the high degree of sophistication and efficiency of biomolecular... Read More about The Tumbleweed: towards a synthetic protein motor.

Flow Linear Dichroism of Some Prototypical Proteins (2009)
Journal Article
Bulheller, B., Rodger, A., Hicks, M., Dafforn, T., Serpell, L., Marshall, K., …Hirst, J. (2009). Flow Linear Dichroism of Some Prototypical Proteins. Journal of the American Chemical Society, 131(37), 13305-13314

Flow linear dichroism (LD) spectroscopy provides information on the orientation of molecules in solution and hence on the relative orientation of parts of molecules. Long molecules such as fibrous proteins can be aligned in Couette flow cells and cha... Read More about Flow Linear Dichroism of Some Prototypical Proteins.

Designed alpha-Helical Tectons for Constructing Multicomponent Synthetic Biological Systems (2009)
Journal Article
Bromley, E., Sessions, R., Thomson, A., & Woolfson, D. (2009). Designed alpha-Helical Tectons for Constructing Multicomponent Synthetic Biological Systems. Journal of the American Chemical Society, 131(3), 928-930. https://doi.org/10.1021/ja804231a

One possible route to develop new synthetic-biological systems is to assemble discrete nanoscale objects from programmed peptide-based building blocks. We describe an algorithm to design such blocks based on the coiled-coil protein-folding motif. The... Read More about Designed alpha-Helical Tectons for Constructing Multicomponent Synthetic Biological Systems.

Peptide and protein building blocks for synthetic biology: From programming biomolecules to self-organized biomolecular systems (2008)
Journal Article
Bromley, E., Channon, K., Moutevelis, E., & Woolfson, D. (2008). Peptide and protein building blocks for synthetic biology: From programming biomolecules to self-organized biomolecular systems. ACS Chemical Biology, 3(1), 38-50. https://doi.org/10.1021/cb700249v

There are several approaches to creating synthetic-biological systems. Here, we describe a molecular-design approach. First, we lay out a possible synthetic-biology space, which we define with a plot of complexity of components versus divergence from... Read More about Peptide and protein building blocks for synthetic biology: From programming biomolecules to self-organized biomolecular systems.

Synthetic biology through biomolecular design and engineering (2008)
Journal Article
Channon, K., Bromley, E., & Woolfson, D. (2008). Synthetic biology through biomolecular design and engineering. Current Opinion in Structural Biology, 18(4), 491-498

Synthetic biology is a rapidly growing field that has emerged in a global, multidisciplinary effort among biologists, chemists, engineers, physicists, and mathematicians. Broadly, the field has two complementary goals: To improve understanding of bio... Read More about Synthetic biology through biomolecular design and engineering.

Electrostatic control of thickness and stiffness in a designed protein fiber (2008)
Journal Article
Papapostolou, D., Bromley, E., Bano, C., & Woolfson, D. (2008). Electrostatic control of thickness and stiffness in a designed protein fiber. Journal of the American Chemical Society, 130(15), 5124-5130. https://doi.org/10.1021/ja0778444

Attempts to design peptide-based fibers from first principles test our understanding of protein folding and assembly, and potentially provide routes to new biomaterials. Several groups have presented such designs based on a-helical and beta-strand bu... Read More about Electrostatic control of thickness and stiffness in a designed protein fiber.

MagicWand: A single, designed peptide that assembles to stable, ordered alpha-helical fibers (2008)
Journal Article
Gribbon, C., Channon, K., Zhang, W., Banwell, E., Bromley, E., Chaudhuri, J., …Woolfson, D. (2008). MagicWand: A single, designed peptide that assembles to stable, ordered alpha-helical fibers. Biochemistry, 47(39), 10365-10371

We describe a straightforward single-peptide design that self-assembles into extended and thickened nano-to-mesoscale fibers of remarkable stability and order. The basic chassis of the design is the well-understood dimeric a-helical coiled-coil motif... Read More about MagicWand: A single, designed peptide that assembles to stable, ordered alpha-helical fibers.

Mechanisms of structure formation in particulate gels of beta-lactoglobulin formed near the isoelectric point (2006)
Journal Article
Bromley, E., Krebs, M., & Donald, A. (2006). Mechanisms of structure formation in particulate gels of beta-lactoglobulin formed near the isoelectric point. The European Physical Journal E, 21(2), 145-152

Particulate gels are known to be formed by bovine beta-lactoglobulin near the isoelectric point when partial unfolding is allowed to occur under heating. The aggregation process of the protein has been investigated within the context of a nucleation... Read More about Mechanisms of structure formation in particulate gels of beta-lactoglobulin formed near the isoelectric point.

Optical microscopy of growing insulin amyloid spherulites on surfaces in vitro (2006)
Journal Article
Rogers, S., Krebs, M., Bromley, E., van der Linden, E., & Donald, A. (2006). Optical microscopy of growing insulin amyloid spherulites on surfaces in vitro. Biophysical Journal, 90(3), 1043-1054

Amyloid fibrils are often found arranged into large ordered spheroid structures, known as spherulites, occurring in vivo and in vitro. The spherulites are predominantly composed of radially ordered amyloid fibrils, which self-assemble from protein in... Read More about Optical microscopy of growing insulin amyloid spherulites on surfaces in vitro.

The binding of thioflavin-T to amyloid fibrils: localisation and implications (2005)
Journal Article
Krebs, M., Bromley, E., & Donald, A. (2005). The binding of thioflavin-T to amyloid fibrils: localisation and implications. Journal of Structural Biology, 149(1), 30-37. https://doi.org/10.1016/j.jsb.2004.08.002

Amyloid fibrils are a polymeric form of protein, involving a continuous P-sheet with the strands perpendicular to the long axis of the fibril. Although typically implicated in diseases such as Alzheimer's disease and the transmissible spongiform ence... Read More about The binding of thioflavin-T to amyloid fibrils: localisation and implications.

Aggregation across the length-scales in beta-lactoglobulin (2005)
Journal Article
Bromley, E., Krebs, M., & Donald, A. (2005). Aggregation across the length-scales in beta-lactoglobulin. Faraday Discussions, 128, 13-27

The protein beta-lactoglobulin (BLG) has been widely studied, in large part because of its importance to the food industry. Following denaturation during heating, under different conditions of pH it has been found to form either particulate (around t... Read More about Aggregation across the length-scales in beta-lactoglobulin.

The mechanism of amyloid spherulite formation by bovine insulin (2005)
Journal Article
Krebs, M., Bromley, E., Rogers, S., & Donald, A. (2005). The mechanism of amyloid spherulite formation by bovine insulin. Biophysical Journal, 88(3), 2013-2021

The formation of amyloid-containing spherulite-like structures has been observed in some instances of amyloid diseases, as well as in amyloid fibril-containing solutions in vitro. In this article we describe the structure and kinetics of bovine insul... Read More about The mechanism of amyloid spherulite formation by bovine insulin.

L55P transthyretin accelerates subunit exchange and leads to rapid formation of hybrid tetramers (2005)
Journal Article
Keetch, C., Bromley, E., McCammon, M., Wang, N., Christodoulou, J., & Robinson, C. (2005). L55P transthyretin accelerates subunit exchange and leads to rapid formation of hybrid tetramers. Journal of Biological Chemistry, 280(50), 41667-41674

Transthyretin is a tetrameric protein associated with the commonest form of systemic amyloid disease. Using isotopically labeled proteins and mass spectrometry, we compared subunit exchange in wild-type transthyretin with that of the variant associat... Read More about L55P transthyretin accelerates subunit exchange and leads to rapid formation of hybrid tetramers.

Confocal microscopy of a dense particle system (2002)
Journal Article
Bromley, E., & Hopkinson, I. (2002). Confocal microscopy of a dense particle system. Journal of Colloid and Interface Science, 245(1), 75-80

We report experiments utilizing confocal microscopy to determine the position of cornflour starch granules in a paste, as a function of distance from a wall. The granules have an average diameter of 15 mum. If a solvent is chosen such as to approxima... Read More about Confocal microscopy of a dense particle system.