Outputs (19)

Combined Chemical Modification and Collision Induced Unfolding Using Native Ion Mobility‐Mass Spectrometry Provides Insights into Protein Gas‐Phase Structure (2021)
Journal Article
Al‐jabiry, A., Palmer, M., Langridge, J., Bellamy‐Carter, J., Robinson, D., & Oldham, N. J. (2021). Combined Chemical Modification and Collision Induced Unfolding Using Native Ion Mobility‐Mass Spectrometry Provides Insights into Protein Gas‐Phase Structure. Chemistry - A European Journal, 27(55), 13783-13792. https://doi.org/10.1002/chem.202101857

Native mass spectrometry is now an important tool in structural biology. Thus, the nature of higher protein structure in the vacuum of the mass spectrometer is an area of significant interest. One of the major goals in the study of gas-phase protein... Read More about Combined Chemical Modification and Collision Induced Unfolding Using Native Ion Mobility‐Mass Spectrometry Provides Insights into Protein Gas‐Phase Structure.

Iridoid Sex Pheromone Biosynthesis in Aphids Mimics Iridoid‐Producing Plants (2021)
Journal Article
Partridge, S. J., Withall, D. M., Caulfield, J. C., Pickett, J. A., Stockman, R. A., Oldham, N. J., & Birkett, M. A. (2021). Iridoid Sex Pheromone Biosynthesis in Aphids Mimics Iridoid‐Producing Plants. Chemistry - A European Journal, 27(25), 7231-7234. https://doi.org/10.1002/chem.202001356

Biosynthesis of (1R,4aS,7S,7aR)‐nepetalactol (1) and (4aS,7S,7aR)‐nepetalactone (2) in plants involves iridoid synthase (ISY), an atypical reductive cyclase that catalyses the reduction of 8‐oxogeranial into the reactive enol of (S)‐8‐oxocitronellal,... Read More about Iridoid Sex Pheromone Biosynthesis in Aphids Mimics Iridoid‐Producing Plants.

Decoding Protein Gas‐Phase Stability with Alanine Scanning and Collision‐Induced Unfolding Ion Mobility Mass Spectrometry (2021)
Other
Bellamy‐Carter, J., O'Grady, L., Passmore, M., Jenner, M., & Oldham, N. (2021). Decoding Protein Gas‐Phase Stability with Alanine Scanning and Collision‐Induced Unfolding Ion Mobility Mass Spectrometry

Decoding Protein Gas‐Phase Stability with Alanine Scanning and Collision‐Induced Unfolding Ion Mobility Mass Spectrometry (2020)
Journal Article
Bellamy‐Carter, J., O'Grady, L., Passmore, M., Jenner, M., & Oldham, N. J. (2021). Decoding Protein Gas‐Phase Stability with Alanine Scanning and Collision‐Induced Unfolding Ion Mobility Mass Spectrometry. Analysis & Sensing, 1(1), 63-69. https://doi.org/10.1002/anse.202000019

Native mass spectrometry is a widely used tool in structural biology, providing information on protein structure and interactions through preservation of complexes in the gas phase. Herein, the importance of intramolecular non‐covalent interactions i... Read More about Decoding Protein Gas‐Phase Stability with Alanine Scanning and Collision‐Induced Unfolding Ion Mobility Mass Spectrometry.

Structural basis for chain release from the enacyloxin polyketide synthase (2019)
Journal Article
Kosol, S., Gallo, A., Griffiths, D., Valentic, T. R., Masschelein, J., Jenner, M., …Lewandowski, J. R. (2019). Structural basis for chain release from the enacyloxin polyketide synthase. Nature Chemistry, 11(10), 913-923. https://doi.org/10.1038/s41557-019-0335-5

Modular polyketide synthases and nonribosomal peptide synthetases are molecular assembly lines consisting of several multienzyme subunits that undergo dynamic selfassembly to form a functional mega-complex. N- and C-terminal docking domains are usual... Read More about Structural basis for chain release from the enacyloxin polyketide synthase.

A front-face 'SNi synthase' engineered from a retaining 'double-SN2' hydrolase (2017)
Journal Article
Iglesias-Fernández, J., Hancock, S. M., Lee, S. S., Khan, M., Kirkpatrick, J., Oldham, N. J., …Davis, B. G. (2017). A front-face 'SNi synthase' engineered from a retaining 'double-SN2' hydrolase. Nature Chemical Biology, 13, 874-881. https://doi.org/10.1038/nchembio.2394

SNi or SNi-like mechanisms, in which leaving group departure and nucleophile approach occur on the same ‘front’ face, have been observed previously experimentally and computationally in both the chemical and enzymatic (glycosyltransferase) substituti... Read More about A front-face 'SNi synthase' engineered from a retaining 'double-SN2' hydrolase.

Design of nucleotide-mimetic and non-nucleotide inhibitors of the translation initiation factor eIF4E: Synthesis, structural and functional characterisation (2016)
Journal Article
Soukarieh, F., Nowicki, M. W., Bastide, A., Poyry, T., Jones, C., Dudek, K., …Fischer, P. M. (2016). Design of nucleotide-mimetic and non-nucleotide inhibitors of the translation initiation factor eIF4E: Synthesis, structural and functional characterisation. European Journal of Medicinal Chemistry, 124, 200-217. https://doi.org/10.1016/j.ejmech.2016.08.047

Eukaryotic translation initiation factor 4E (eIF4E) is considered as the corner stone in the cap-dependent translation initiation machinery. Its role is to recruit mRNA to the ribosome through recognition of the 50 - terminal mRNA cap structure (m7 G... Read More about Design of nucleotide-mimetic and non-nucleotide inhibitors of the translation initiation factor eIF4E: Synthesis, structural and functional characterisation.

Acyl hydrolases from trans-AT polyketide synthases target acetyl units on acyl carrier proteins (2016)
Journal Article
Jenner, M., Afonso, J. P., Kohlhaas, C., Karbaum, P., Frank, S., Piel, J., & Oldham, N. J. (in press). Acyl hydrolases from trans-AT polyketide synthases target acetyl units on acyl carrier proteins. Chemical Communications, 52(30), https://doi.org/10.1039/C6CC01453D

Acyl hydrolase (AH) domains are a common feature of trans-AT PKSs. They have been hypothesised to perform a proofreading function by removing acyl chains from stalled sites. This study determines the substrate tolerance of the AH PedC for a range of... Read More about Acyl hydrolases from trans-AT polyketide synthases target acetyl units on acyl carrier proteins.

Ion mobility-mass spectrometry reveals conformational flexibility in the deubiquitinating enzyme USP5 (2015)
Journal Article
Scott, D., Layfield, R., & Oldham, N. J. (2015). Ion mobility-mass spectrometry reveals conformational flexibility in the deubiquitinating enzyme USP5. Proteomics, 15(16), https://doi.org/10.1002/pmic.201400457

Many proteins exhibit conformation flexibility as part of their biological function, whether through the presence of a series of well-defined states or by the existence of intrinsic disorder. Ion mobility spectrometry, in combination with MS (IM–MS),... Read More about Ion mobility-mass spectrometry reveals conformational flexibility in the deubiquitinating enzyme USP5.