Mark Howard's profile
What I do
Use high resolution liquid state nuclear magnetic resonance (NMR) spectroscopy to answer biological question regarding the structure and operation of biological molecules. These molecules can be small, as in integrin specific peptides or large as in multi-domain ER proteins.
Affiliations
Current affiliations
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- Position
- Lecturer in Biomolecular NMR Spectroscopy
- Company
- BSc PhD CSci CChem MRSC
- Further information
Location
- City:
- None chosen
- Hub:
- None chosen
Interests
NMR spectroscopy and protein biochemistry related to structure, interactions and function.
Out of work: Guitar playing!
Projects
Using NMR spectroscopy in biomolecular structure determination and interaction studies.
Using NMR to understand structure/function in integrin based cell signalling
Studying structure/function relationships in endoplasmic reticulum (ER) proteins
The effects of modifications on protein structure and function
Publications
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Alanen H, Williamson R, Howard M, Hatahet F, Salo K, Kauppila A, Kellokumpu S, Ruddock L. ERp27, a new non-catalytic endoplasmic reticulum-located human protein disulfide isomerase family member, interacts with ERp57. The Journal of biological chemistry (44) , 33727-38 (Epub 28 Aug 2006) PubMed ID:(16940051)
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DiCara D, Rapisarda C, Sutcliffe J, Violette S, Weinreb P, Hart I, Howard M, Marshall J. Structure-function analysis of Arg-Gly-Asp helix motifs in alpha v beta 6 integrin ligands. The Journal of biological chemistry (13) , 9657-65 (Epub 23 Jan 2007) PubMed ID:(17244604)
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Povey J, Smales C, Hassard S, Howard M. Comparison of the effects of 2,2,2-trifluoroethanol on peptide and protein structure and function. Journal of structural biology (2) , 329-38 (Epub 02 Aug 2006) PubMed ID:(16979904)
Contact
- email:
- m.j.howard [ at ] kent.ac.uk
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