Introduction

Research Groups

Select Research Group Head Prof. Sir Tom Blundell Prof. Kevin Brindle Dr Bill Broadhurst Dr Guy Brown Dr Mark Carrington Prof. Paul Dupree Prof. Gerard Evan - Head of Dept Prof. Richard Farndale Dr Giorgio Favrin Dr Jenny Gallop Dr Nick Gay Dr Andrew Grace Dr Jules Griffin Dr Brian Hendrich Dr Andrew Hesketh Dr Robin Hesketh Dr Matt Higgins Dr Florian Hollfelder Dr Hee-Jeon Hong Prof. Chris Howe Dr Marko Hyvonen Prof. Steve Jackson Dr Tony Jackson Prof. Richard Jackson Prof. Ernest Laue Prof. Peter Leadlay Dr Kathryn Lilley Dr Karen Lipkow Dr Rick Livesey Prof. Ben Luisi Dr Sarah Lummis Dr Juan Mata Dr John McCafferty Prof. Jim Metcalfe Dr Masanori Mishima Dr Eric Miska Dr Tom Monie Dr Helen Mott Dr Natasha Murzina Dr Daniel Nietlispach Dr Darerca Owen Prof. Steve Oliver Dr Luca Pellegrini Dr Markus Ralser Dr Nick Robinson Prof. George Salmond Dr Deirdre Scadden Dr José Silva Prof. Austin Smith Prof. Chris Smith Dr Nancy Standart Prof. Dame Jean Thomas Dr Aviva Tolkovsky Dr Martin Welch Dr Joyce Wong Dr Nianshu Zhang

Service & Research Support Facilities

Select by Subject or Manager DNA Sequencing Facility . . . . . Mr John Lester _______________________________ Quantitative Proteomics . . . . . Dr Kathryn Lilley _______________________________ Proteomics Core Services . . . . . Dr Mike Deery _______________________________ Protein & Nucleic Acid Chemistry . . . . . Dr Len Packman _______________________________ Metabolomics . . . . . Dr Jules Griffin _______________________________ Baculovirus Facility . . . . . Dr Darerca Owen _______________________________ Biophysics Facility . . . . . Dr Katherine Stott _______________________________ Crystallographic X-ray Facility . . . . . Dr Dima Chirgadze _______________________________ NMR spectroscopy . . . . . Dr Daniel Nietlispach _______________________________ Fermentation Facility . . . . . Dr Nianshu Zhang _______________________________ Bioinformatics & Computational Biology Services . . . . . Dr Jenny Barna _______________________________ Computer & IT Support . . . . . Dr Erik Timmers _______________________________

Past members last known active weblink

Select past member of Department Dr Stephen Bell Prof. Jonathan Blackburn Dr David Brown Dr Pak-Lee Chau Dr Hal Dixon (deceased) Dr Jessica Downs Prof. David Ellar Dr Paul Kemp Dr Simon Lovell Dr Kenji Mizuguchi Dr Massimo Paoli Prof. Richard Perham Dr Peter Reynolds Dr Philip Rubery Dr Gerry Smith Dr Margaret Sunde Prof. Jamie Vandenberg Dr Kira Weissman

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Method development for the Structural Study of Proteins by NMR

Research Grouping: Structural and molecular cell biology

Solution NMR spectroscopy is used to investigate a broad range of biophysical problems including the study of structural aspects of proteins and their complexes, together with the analysis of their dynamical behaviour in solution, their interaction with target molecules and their folding pathways. One of the main interests in our lab is to develop methodology so that NMR can be more efficiently applied to protein systems of higher molecular weight. The approach combines method development with theoretical simulations and experimental verification. In combination with isotope labelling techniques we are designing new methods that make the structural study of proteins > 35 kDa more accessible. Various aspects are currently addressed as new strategies are required to both improve the quality of NMR derived structures and to speed up the slow process of assignment and structure determination. Our second main interest focuses on the development of techniques for the solution study of integral membrane proteins by NMR. As membrane proteins are very hydrophobic and typically only stable in their natural lipid environment this causes problems for structural studies by X-ray. Thus, only a few structures of such proteins are currently available. Detergent stabilization allows membrane proteins to be solubilized. Most helical proteins e.g. the G-Protein Coupled Receptors (GPCR) are, by their size, amenable to study by NMR, but the presence of the detergent aggregate can increase the molecular weight beyond 100kDa, making such systems challenging to study.

Intra-HN(CA)CO NMR experiment which helps to establish the sequential assignment of residues in proteins > 35 kDa.	[1H/15N] TROSY 2D correlation spectrum of a seven-helical rhodopsin protein in detergent micelles (total mass is approximately ~100 kDa).

Lab members
Mark Bostock, Antoine Gautier, Fatima Abdul Hussein, Leena Makani, Simon Quick

References