Skip to main content

Research Repository

Advanced Search

All Outputs (35)

Evaluation of diffusion coefficients by means of an approximate steady-state condition in sedimentation velocity distributions (2015)
Journal Article
Scott, D. J., Harding, S. E., & Winzor, D. J. (2015). Evaluation of diffusion coefficients by means of an approximate steady-state condition in sedimentation velocity distributions. Analytical Biochemistry, 490, https://doi.org/10.1016/j.ab.2015.08.017

This investigation examined the feasibility of manipulating the rotor speed in sedimentation velocity experiments to spontaneously generate an approximate steady-state condition where the extent of diffusional spreading is matched exactly by the boun... Read More about Evaluation of diffusion coefficients by means of an approximate steady-state condition in sedimentation velocity distributions.

Crystal structures of the extracellular domain from PepT1 and PepT2 provide novel insights into mammalian pPeptide transport (2015)
Journal Article
Beale, J. H., Parker, J. L., Samsudin, F., Barrett, A. L., Senan, A., Bird, L. E., …Newstead, S. (2015). Crystal structures of the extracellular domain from PepT1 and PepT2 provide novel insights into mammalian pPeptide transport. Structure, 23(10), https://doi.org/10.1016/j.str.2015.07.016

Mammals obtain nitrogen via the uptake of di- and tri-peptides in the gastrointestinal tract through the action of PepT1 and PepT2, which are members of the POT family of proton-coupled oligopeptide transporters. PepT1 and PepT2 also play an importan... Read More about Crystal structures of the extracellular domain from PepT1 and PepT2 provide novel insights into mammalian pPeptide transport.

A Multilaboratory Comparison of Calibration Accuracy and the Performance of External References in Analytical Ultracentrifugation (2015)
Journal Article
Langowski, J., Zhao, H., Ghirlando, R., Alfonso, C., Arisaka, F., Attali, I., …Schuck, P. (2015). A Multilaboratory Comparison of Calibration Accuracy and the Performance of External References in Analytical Ultracentrifugation. PLoS ONE, 10(5), Article e0126420. https://doi.org/10.1371/journal.pone.0126420

Analytical ultracentrifugation (AUC) is a first principles based method to determine absolute sedimentation coefficients and buoyant molar masses of macromolecules and their complexes, reporting on their size and shape in free solution. The purpose o... Read More about A Multilaboratory Comparison of Calibration Accuracy and the Performance of External References in Analytical Ultracentrifugation.

Concentration dependence of translational diffusion coefficients for globular proteins (2014)
Journal Article
Scott, D. J., Harding, S. E., & Winzor, D. J. (2014). Concentration dependence of translational diffusion coefficients for globular proteins. Analyst, 139(23), https://doi.org/10.1039/c4an01060d

This investigation examines published results of traditional diffusion experiments on ovalbumin and bovine serum albumin to determine the extent to which assumed concentration independence of the translational diffusion coefficient is a reasonable ap... Read More about Concentration dependence of translational diffusion coefficients for globular proteins.

N-terminal Domain of Prion Protein Directs Its Oligomeric Association (2014)
Journal Article
Trevitt, C. R., Hosszu, L. L., Batchelor, M., Panico, S., Terry, C., Nicoll, A. J., …Clarke, A. R. (2014). N-terminal Domain of Prion Protein Directs Its Oligomeric Association. Journal of Biological Chemistry, 289(37), 25497-25508. https://doi.org/10.1074/jbc.m114.566588

The self-association of prion protein (PrP) is a critical step in the pathology of prion diseases. It is increasingly recognized that small non-fibrillar ?-sheet-rich oligomers of PrP may be of crucial importance in the prion disease process. Here, w... Read More about N-terminal Domain of Prion Protein Directs Its Oligomeric Association.

Engineering a reagentless biosensor for single-stranded DNA to measure real-time helicase activity in Bacillus (2014)
Journal Article
Green, M., Gilhooly, N. S., Abedeen, S., Scott, D. J., Dillingham, M. S., & Soultanas, P. (2014). Engineering a reagentless biosensor for single-stranded DNA to measure real-time helicase activity in Bacillus. Biosensors and Bioelectronics, 61, 579-586. https://doi.org/10.1016/j.bios.2014.06.011

Single-stranded DNA-binding protein (SSB) is a well characterized ubiquitous and essential bacterial protein involved in almost all aspects of DNA metabolism. Using the Bacillus subtilis SSB we have generated a reagentless SSB biosensor that can be u... Read More about Engineering a reagentless biosensor for single-stranded DNA to measure real-time helicase activity in Bacillus.

Structure and Catalytic Regulatory Function of Ubiquitin Specific Protease 11 N-Terminal and Ubiquitin-like Domains (2014)
Journal Article
Harper, S., Gratton, H. E., Cornaciu, I., Oberer, M., Scott, D. J., Emsley, J., & Dreveny, I. (2014). Structure and Catalytic Regulatory Function of Ubiquitin Specific Protease 11 N-Terminal and Ubiquitin-like Domains. Biochemistry, 53(18), 2966-2978. https://doi.org/10.1021/bi500116x

The ubiquitin specific protease 11 (USP11) is implicated in DNA repair, viral RNA replication, and TGF? signaling. We report the first characterization of the USP11 domain architecture and its role in regulating the enzymatic activity. USP11 consists... Read More about Structure and Catalytic Regulatory Function of Ubiquitin Specific Protease 11 N-Terminal and Ubiquitin-like Domains.

Anomalous Small Angle X-Ray Scattering Simulations: Proof of Concept for Distance Measurements for Nanoparticle-Labelled Biomacromolecules in Solution (2014)
Journal Article
Pinfield, V. J., & Scott, D. J. (2014). Anomalous Small Angle X-Ray Scattering Simulations: Proof of Concept for Distance Measurements for Nanoparticle-Labelled Biomacromolecules in Solution. PLoS ONE, 9(4), Article e95664. https://doi.org/10.1371/journal.pone.0095664

Anomalous small angle X-ray scattering can in principle be used to determine distances between metal label species on biological molecules. Previous experimental studies in the past were unable to distinguish the label-label scattering contribution f... Read More about Anomalous Small Angle X-Ray Scattering Simulations: Proof of Concept for Distance Measurements for Nanoparticle-Labelled Biomacromolecules in Solution.

Synthesis of ?-glucan in mycobacteria involves a hetero-octameric complex of trehalose synthase TreS and Maltokinase Pep2 (2013)
Journal Article
Roy, R., Usha, V., Kermani, A., Scott, D. J., Hyde, E. I., Besra, G. S., …Fütterer, K. (2013). Synthesis of α-glucan in mycobacteria involves a hetero-octameric complex of trehalose synthase TreS and Maltokinase Pep2. ACS Chemical Biology, 8(10), https://doi.org/10.1021/cb400508k

Recent evidence established that the cell envelope of Mycobacterium tuberculosis, the bacillus causing tuberculosis (TB), is coated by an ?-glucan-containing capsule that has been implicated in persistence in a mouse infection model. As one of three... Read More about Synthesis of ?-glucan in mycobacteria involves a hetero-octameric complex of trehalose synthase TreS and Maltokinase Pep2.

Crystal structure of signal regulatory protein gamma (SIRP?) in complex with an antibody Fab fragment (2013)
Journal Article
Nettleship, J. E., Ren, J., Scott, D. J., Rahman, N., Hatherley, D., Zhao, Y., …Owens, R. J. (2013). Crystal structure of signal regulatory protein gamma (SIRPγ) in complex with an antibody Fab fragment. BMC Structural Biology, 13, Article 13. https://doi.org/10.1186/1472-6807-13-13

BACKGROUND Signal Regulatory Protein γ (SIRPγ) is a member of a closely related family of three cell surface receptors implicated in modulating immune/inflammatory responses. SIRPγ is expressed on T lymphocytes where it appears to be involved in t... Read More about Crystal structure of signal regulatory protein gamma (SIRP?) in complex with an antibody Fab fragment.

The lipidome and proteome of oil bodies from Helianthus annuus (common sunflower) (2013)
Journal Article
Furse, S., Liddell, S., Ortori, C. A., Williams, H., Neylon, D. C., Scott, D. J., …Gray, D. A. (2013). The lipidome and proteome of oil bodies from Helianthus annuus (common sunflower). Journal of Chemical Biology, 6(2), 63-76. https://doi.org/10.1007/s12154-012-0090-1

In this paper we report the molecular profiling, lipidome and proteome, of the plant organelle known as an oil body (OB). The OB is remarkable in that it is able to perform its biological role (storage of triglycerides) whilst resisting the physical... Read More about The lipidome and proteome of oil bodies from Helianthus annuus (common sunflower).

DnaB proteolysis in vivo regulates oligomerization and its localization at oriC in Bacillus subtilis (2010)
Journal Article
Grainger, W. H., Machón, C., Scott, D. J., & Soultanas, P. (2010). DnaB proteolysis in vivo regulates oligomerization and its localization at oriC in Bacillus subtilis. Nucleic Acids Research, 38(9), https://doi.org/10.1093/nar/gkp1236

Initiation of bacterial DNA replication at oriC is mediated by primosomal proteins that act cooperatively to melt an AT-rich region where the replicative helicase is loaded prior to the assembly of the replication fork. In Bacillus subtilis, the dnaD... Read More about DnaB proteolysis in vivo regulates oligomerization and its localization at oriC in Bacillus subtilis.

RepD-mediated recruitment of PcrA helicase at the Staphylococcus aureus pC221 plasmid replication origin, oriD (2010)
Journal Article
Mach?n, C., Thomson, N., Lynch, G., Scott, D. J., Thomas, C., & Soultanas, P. (2010). RepD-mediated recruitment of PcrA helicase at the Staphylococcus aureus pC221 plasmid replication origin, oriD. Nucleic Acids Research, 38(6), https://doi.org/10.1093/nar/gkp1153

Plasmid encoded replication initiation (Rep) proteins recruit host helicases to plasmid replication origins. Previously, we showed that RepD recruits directionally the PcrA helicase to the pC221 oriD, remains associated with it, and increases its pro... Read More about RepD-mediated recruitment of PcrA helicase at the Staphylococcus aureus pC221 plasmid replication origin, oriD.