Piero Temussi - Curriculum Vitae#

• 1962 PhD “Laurea in Chimica, summa cum laude” University of Naples

• Total publications in Peer reviewed journals: 144 (17 since 2014)
  
• Total: H-factor 45, Citations 7037, i10-index 1764
  
• Since 2014: H-factor 22, Citations 1764, i10-index 52
  

• 2009 - 2010 Exchange Royal Society Grant with NIMR, London
  
• 2005 - 2006 Exchange Royal Society Grant with NIMR, London
  
• 1967 Weizman Institute, Rehovoth (Israel)\Visiting Scientist in Prof. Shneior Lifson’ group
  
• 1965 – 1966 University of Illinois (USA): Nato Fellowship in Prof. Herbert Gutowsky’s group
  

• Reviewer of ca. 20 peer reviewed International journals
  
• Advisory Board Member of Journal Peptide Science
  
• Founder of the Centre of Chemical-Physics Methodologies (CIMCF) in Naples
  
• Founder of the Capri Workshop on Bioactive Peptides
  
• Reviewer of National Grant Agencies in France (ANR) and Italy (MIUR)
  
• Scientific Editor of Frontiers in Biomol. Sciences, PlosOne and Peptide Science
  
• Invited speaker in several International meetings (e.g. Telluride, Ascona meeting in 2012

• 1982 International School of NMR methodologies in Arcavacata di Rende (Italy)
  
• 1983 Meeting of the GDRM in Naples
  
• 1988 Nato School on NMR in Biology in Maratea (Italy)
  
• 1988-2000 Biannual Capri Meetings for Bioactive Peptides
  
• 2001 EMBO workshop in Ravello (Italy)
  
• 2010 Workshop on ‘The Biology of Taste’ in Procida (Italy)
  

• Protein folding: he studied the structural determinants that lead proteins to unfold both at high and low temperature. He is in particular a world-wide expert of the field of cold denaturation. This field is of primary importance to understand the forces which determine protein fold and is relevant to protein folding, misfolding and aggregation (2007-present).

• Molecular Crowding and confinement: He studied and is studying the effects of molecular crowding and confinement on the structure, stability and function of proteins. This field is of primary interest to connect in vitro and in vivo studies and take into account the complexity of the cellular environments (2007-present).

• Structural Bioinformatics: he suggested a model of sweet taste recognition using the homology between the aspartame and sweet receptors. This model is currently the only successful way to explain how the sweet receptor works (2001 and thereafter).

• Structural Biology: he studied the fold determinants of the sweet protein monellin and formulated hypothesis on how sweet proteins interact with the sweet receptor (there is only one). This work was/is of primary relevance in the fields of diabetes, obesity and food perception (1995-2010).

• Biologically active peptides: he did pioneering work studying the structures of a number of important neurotransmitters. Among others, he solved the structure of aspartame and studied the conformation of enkephalins and other opioid peptides. He formulated models of how the peptides could interact with their receptors well before the receptors were identified ('80ies-'90ies).

• Biological nuclear molecular biology: he introduced the field in Italy in the early '70ies. His work promoted the technique in Italy and informed all the following studies ('70ies). He has worked in the field since.

• Cold denaturation
  
• Determinants of the sweet taste of proteins
  
• Crowding and confinement