The University of Sheffield
Department of Chemistry

Barbara CianiDr. Barbara Ciani

Lecturer in Biophysical Chemistry

Room: C72

Tel: +44-(0)114-22-29438

Fax: +44-(0)114-22-29346

email:

 


 

General  Research Teaching

Biographical Sketch

Dr. Ciani obtained a Laurea in Chemistry at University "La Sapienza", Rome in 1997. This was followed by a DPhil in Biochemistry at the University of Sussex in Brighton in 2001, after which she became a Postdoctoral Research Associate at the University of Nottingham (2001-2003) and subsequently at the University of Manchester (2004-2008). In 2008 she was appointed as a Lecturer in Biophysical Chemistry at the University of Sheffield.

Research Keywords

Coiled coils, leucine zippers, de novo design, amyloid, ESCRT complex, circular dichroism, NMR.

Teaching Keywords

Analytical Chemistry; Biophysical Chemistry

Selected Publications:

  • Molecular basis of coiled-coil oligomerization-state specificity, B. Ciani, S. Bjelic, S. Honnappa, H. Jawhari, R. Jaussi, A. Payapilly, T. Jowitt, M. O. Steinmetz and R. A. Kammerer, Proc. Natl. Acad. Sci. USA 2010, 107, 19850-19855.
  • Atomic models of de novo designed cc beta-met amyloid-like fibrils, M. O. Steinmetz, Z. Gattin, R. Verel, B. Ciani, T. Stromer, J. M. Green, P. Tittmann, C. Schulze-Bdese, H. Gross, W. F. van Gunsteren, B. H. Meier, L. C. Serpell, S. A. Muller and R. A. Kammerer, J. Mol. Biol. 2008, 376, 898-912.
  • Electrostatic contributions to the stability of the GCN4 leucine zipper structure, W. M. Matousek, B. Ciani, C. A. Fitch, B. Garcia-Moreno, R. A. Kammerer and A. T. Alexandrescu, J. Mol. Biol. 2007, 374, 206-219.
  • Structure of the extracellular domain of tie receptor tyrosine kinases and localization of the angiopoietin-binding epitope, P. R. Macdonald, P. Progias, B. Ciani, S. Patel, U. Mayer, M. O. Steinmetz and R. A. Kammerer, J. Biol. Chem. 2006, 281, 28408-28414.
  • Structural and functional studies of mutations affecting the UBA domain of SQSTM1 (p62) which cause Paget's disease of bone, R. Layfield, B. Ciani, S. H. Ralston, L. J. Hocking, P. W. Sheppard, M. S. Searle and J. R. Cavey, Biochem. Soc. Trans. 2004, 32, 728-730.

Research Interests

Protein-protein interactions are essential to ensure correct function of all living organisms. One of the means for regulating protein-protein interactions is through coiled coil domains.

Coiled coils are oligomerisation domains present in a large variety of proteins that play major roles in almost all biological processes. The most attractive feature of coiled coils is that their multimerisation properties can be `programmed´ by their amino acid sequences.

Research in our lab focuses specifically in two main areas:

Research Barbara Ciani

  1. Protein designers are trying to learn how natural coiled coil systems can be exploited to create novel functional self-assembled structures for medicine and material science applications. We are interested in the elucidation of molecular features that control coiled coil oligomerisation specificity using simple leucine zipper domains as model systems.
  2. Diseases such as cancer and neurodegeneration are caused by malfunction of cellular pathways involved in degradation of non-functional proteins. We want to understand how coiled coil motifs regulate the assembly of specific protein complexes that work in the transport of cargo destined for degradation.

Our lab has expertise in:

• Protein engineering and cloning
• High-level recombinant peptide and protein expression for structural studies
• De novo and rational design of α- helical and β-hairpin peptides
• Protein stability and protein-protein interaction measurements
• Characterisation of peptides that undergo self-assembly

Teaching Section

Biological Chemistry

Undergraduate Courses Taught

  • Thermochemistry (Year 1)
    This segment further evolves the concepts of classical thermodynamics. Thermodynamics provides us with the means to predict the direction of chemical change. In this segment we develop the essential tools that can help us to predict whether reactions are spontaneous or not, including, most importantly, the concept of free energy.
  • Separation Science (Year 2)
    This course introduces selected separation techniques to enable you to choose suitable techniques for specific separation problems based on physical principles and practical consideration.
  • Biophysical Chemistry (Year 4)
    This lecture course provides an overview of the classical methods employed to investigate the structure of biopolymers and their interactions. 

Tutorial & Workshop Support

  • First Year General Tutorials.
  • Second Year Physical Chemistry Tutorials.
  • Third Year Literature Review.
  • Fourth Year Workshops (Biophysical Chemistry).

Laboratory Teaching

  • Second Year Demonstrating
  • Third Year Advandced Physical Chemistry
  • Fourth Year Research Project