ORCID Profile
0000-0002-2726-0983
Current Organisation
University of Nottingham
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Publisher: Royal Society of Chemistry (RSC)
Date: 2002
DOI: 10.1039/B205080N
Publisher: American Chemical Society (ACS)
Date: 19-01-2022
Abstract: Enzyme-based iron-sulfur clusters, exemplified in families such as hydrogenases, nitrogenases, and radical
Publisher: Wiley
Date: 14-02-2023
Abstract: The site‐selective modification of peptides and proteins facilitates the preparation of targeted therapeutic agents and tools to interrogate biochemical pathways. Among the numerous bioconjugation techniques developed to install groups of interest, those that generate C(sp 3 )−C(sp 3 ) bonds are significantly underrepresented despite affording proteolytically stable, biogenic linkages. Herein, a visible‐light‐mediated reaction is described that enables the site‐selective modification of peptides and proteins via desulfurative C(sp 3 )−C(sp 3 ) bond formation. The reaction is rapid and high yielding in peptide systems, with comparable translation to proteins. Using this chemistry, a range of moieties is installed into model systems and an effective PTM‐mimic is successfully integrated into a recombinantly expressed histone.
Publisher: Elsevier BV
Date: 04-2010
Publisher: American Chemical Society (ACS)
Date: 28-08-2009
DOI: 10.1021/JA902662E
Abstract: 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 characterized using LD. We have measured using Couette flow and calculated from first principles the LD of proteins representing prototypical secondary structure classes: a self-assembling fiber and tropomyosin (all-alpha-helical), FtsZ (an alphabeta protein), an amyloid fibril (beta-sheet), and collagen [poly(proline)II helices]. The combination of calculation and experiment allows elucidation of the protein orientation in the Couette flow and the orientation of chromophores within the protein fibers.
Publisher: Royal Society of Chemistry (RSC)
Date: 2007
DOI: 10.1039/B615870F
Abstract: Circular dichroism (CD) is an important technique in the structural characterisation of proteins, and especially for secondary structure determination. The CD of proteins can be calculated from first principles using the so-called matrix method, with an accuracy which is almost quantitative for helical proteins. Thus, for proteins of unknown structure, CD calculations and experimental data can be used in conjunction to aid structure analysis. Linear dichroism (LD) can be calculated using analogous methodology and has been used to establish the relative orientations of subunits in proteins and protein orientation in an environment such as a membrane. However, simple analysis of LD data is not possible, due to overlapping transitions. So coupling the calculations and experiment is an important strategy. In this paper, the use of LD for the determination of protein orientation and how these data can be interpreted with the aid of calculations, are discussed. We review methods for the calculation of CD spectra, focusing on semiempirical and ab initio parameter sets used in the matrix method. Lastly, a new web interface for online CD and LD calculation is presented.
Location: United Kingdom of Great Britain and Northern Ireland
No related grants have been discovered for Jonathan Hirst.