Our faculty presently consists of two associate professors, Cristian Micheletti (head) and Alessandro Laio (deputy head), one tenure-track scientist, Giovanni Bussi and one co-opted assistant professor, Alessandra Magistrato from CNR who is responsible for the Biophysics research line of the CNR-IOM Democritos Center for Atomistic Simulations in Trieste.
Main research lines in the Molecular and Statistical Biophysics Group are:
(1) Characterization of dense phases of biopolymers (PI: C. Micheletti)
(2) Elucidating the structure-function relationship in enzymes. (PI: C. Micheletti) Hide
Part of the activity of our group is aimed at developing and applying coarse-grained models for describing the large-scale internal dynamics of proteins and then compare it across superfamilies of enzymes with similar function but different fold.
The long-term objective is to use the dynamics-based comparative scheme to advance the understanding of the structure-function relationship in proteins. The approach is similar in spirit to the classical studies on the sequence-structure relationship. The availability of both sequence and structure comparative (alignment) methods has clarified that, because of either evolutionary conservation or convergence, proteins with different primary chemical sequences can adopt similar native structures.
We have developed a novel set of tools that allows for addressing an analogously challenging question: can proteins with different native fold exhibit similar functionally-oriented movements? What underlying evolutionary mechanisms can we highlight with this scheme. See ref. to learn more about it.
Caption: Corresponding large-scale movements in two different ASP-proteases: HIV-1 Protease (homodimer, 198 amino acids) and Beta-Secretase (monomeric, ~350 amino acids). See Carnevale et al. JACS 2006 and Zen et al. Prot. Sci. 2008 to learn more.
The long-term objective is to use the dynamics-based comparative scheme to advance the understanding of the structure-function relationship in proteins. The approach is similar in spirit to the classical studies on the sequence-structure relationship. The availability of both sequence and structure comparative (alignment) methods has clarified that, because of either evolutionary conservation or convergence, proteins with different primary chemical sequences can adopt similar native structures.
We have developed a novel set of tools that allows for addressing an analogously challenging question: can proteins with different native fold exhibit similar functionally-oriented movements? What underlying evolutionary mechanisms can we highlight with this scheme. See ref. to learn more about it.
Caption: Corresponding large-scale movements in two different ASP-proteases: HIV-1 Protease (homodimer, 198 amino acids) and Beta-Secretase (monomeric, ~350 amino acids). See Carnevale et al. JACS 2006 and Zen et al. Prot. Sci. 2008 to learn more.
(3) Simulating rare events in biological systems (PI: A. Laio)
(4) Molecular Mechanisms of Diseases and Drugs (PI: Dr. A. Magistrato)
(5) Enzymatic and biomimetic catalysis (PI: Dr. A. Magistrato)
(6) Simulation of small ribonucleic acid (RNA) (PI: Dr. G. Bussi)
(7) PLUMED Development (PI: Dr. G. Bussi)