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Research Interests
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Research Interests

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Amyloid diseases, or amyloidoses, are disorders that involve the accumulation of protein aggregates within human organs over a person's lifespan. The most notorious subset of the amyloidoses are neurodegenerative diseases, such as Alzheimer's and Parkinson's disease. The cost of these neurodegenerative diseases to the US government exceeds $200 billion a year. Estimating the cost of systemic amyloidoses, where solid protein deposits accumulate in other organs, is difficult. The systemic amyloidoses are more challenging to diagnose than those that present as dementias and so the true cost of amyloid disease to the US and global economies is likely to be a gross underestimate. The true toll of these diseases is difficult to assess. However, estimates from Alzheimer's Research UK indicate that if we are able to delay the onset of these diseases by only 5 years, the number of deaths could be halved.

Amyloidoses involve a process whereby fully functional proteins undergo a structural change that results in the formation of solid deposits. What happens in the early stages before solid protein aggregates appear has been the focus of much research. Hence, my passion has revolved around understanding proteins; their structure, functions and dynamic behaviors. This journey has traversed many stops, from method development to increase accuracy in structural determinations to investigation of changes in that structure using molecular dynamics simulations. Currently, I have been investigating the dynamic behaviors and conformational propensities of small peptide systems and 807 proteins of different topologies: the Dynameomics Initiative. This opportunity has allowed me to perform more in-depth surveys of structured and unstructured protein dynamics to gain further understanding of protein behavior across protein fold space. And, as more evidence of the functional roles of intrinsically disordered proteins (IDPs) and regions (IDRs) within signalling networks has accrued, my work has begun to incorporate studies of these fascinating moieties and consideration of the possibility to categorize them into dynamic domain families and in the role of failures in such systems in the onset of human disease.
  • Protein structure and dynamics
  • Intrinsically disordered proteins
  • Protein interactions and associated conformational changes in signalling networks relevant to autophagy and neurodegeneration
  • Post-translational modifications and SNP induced conformational changes of proteins implicated in amyloid diseases


View Clare-Louise Towse's profile on LinkedIn

Clare-Louise Towse


PhD Chemistry
University of Nottingham Computational Chemistry Group Structural Biology & Biophysics Group

MPhil Chemistry

University of Manchester
NMR Research Group

MChem (Hons) Chemistry University of Leicester

I have an experimental background, in industry as well as in academia. Currently, I use molecular dynamic simulations to gain further understanding of protein structure and dynamics at the atomic level.  My experiences as both an experimentalist and as a modeller has made me very passionate about the complementary nature of both approaches.

Current Projects

As a senior postdoctoral research fellow withinin the Daggett lab my main focus is the Dynameomics initiative: a dataset of MD simulations of 807 protein domains that represent 97% of all known protein folds. I am currently characterizing the conformational entropies across our Dynameomics database and determining relationships with spectroscopic observables.
Due to my interest in IDPs, I have initiated work within the group to examine the presence of disorder across our dataset and have identified a number of targets with known and predicted IDRs. This interesting find is now being examined in greater detail to understand and compare the dynamics and conformational preferences with those of ordered proteins.

  • Conformational entropy of structured and unstructured proteins
  • Dynamics of intrinsically disordered regions across protein fold space

Poster presented at 2012 GRC on Intrinsically Disordered Proteins


  1. Clare-Louise Towse, Jiri Vymetal, Jiri Vondrasek and Valerie Daggett, (manuscript in progress)
  2. Clare-Louise Towse and Valerie Daggett, "Simulating Protein Folding Pathways", Reviews in Computational Chemistry (accepted)
  3. Clare-Louise Towse and Valerie Daggett, "When a Domain is not a Domain, and why it is important to properly filter proteins in databases", BioEssays, 34, 1060-1069 (2012) [DOI: 10.1002/bies.201200116]
  4. Clare-Louise Towse and Valerie Daggett, "Molecular Dynamics Simulations", In Gordon C. K. Roberts (Ed.), Encyclopedia of Biophysics, Volume 1, Springer, New York, Oct 2012 [ISBN 978-3-642-16711-9]
  5. Ping Chen, Clare-Louise Evans (Clare-Louise Towse), Jonathan D. Hirst and Mark S. Searle, "Structural Insights into the Two Sequential Folding Transition States of the PB1 domain of NBR1 from Φ Value Analysis and Biased Molecular Dynamics Simulations", Biochemistry, (2010) [DOI: 10.1021/bi1016793]
  6. Clare-Louise Evans, Jed E. Long, Thomas R. A. Gallagher, Jonathan D. Hirst, Mark S. Searle, "Conformation and dynamics of the three-helix bundle UBA domain of p62 from experiment and simulation", Proteins: Structure, Function and Bioinformatics, 71, 227-40 (2008) [DOI: 10.1002/prot.21692]
  7. Clare-Louise Evans, Gareth A. Morris, and Adrian L. Davis, "A New Method for Variable Temperature Gradient Shimming", Journal of Magnetic Resonance, 154, 325-328 (2002) [DOI: 10.1006/jmre.2001.2497]

Dec 2012 BioEssays Cover

"When a Domain is not a Domain"
BioEssays Cover
Dec 2012 Volume 34