---------- Forwarded message ----------
From: Catherine M Bourgeois <cmbourg(a)mit.edu>
Date: Thu, Jan 28, 2016 at 4:20 PM
Subject: Romain Studer - Excitonics Speaker Schedule
To: efrc-faculty <efrc-faculty(a)mit.edu>du>, excitonics-sp <
excitonics-sp(a)mit.edu>
Dear members:
Romain Studer from the European Bioinformatics Institute will be giving a
talk at the center on Feb 9 at 3pm in the RLE Haus/Allen room. Alan is
hosting his visit. Please CLICK HERE
<https://urldefense.proofpoint.com/v2/url?u=http-3A__doodle.com_poll_27rmfh7gn28zrrmn&d=CwMFAg&c=WO-RGvefibhHBZq3fL85hQ&r=CkFdLmRHkAvmxtF7xMV5_62jpYJuWc_IdPQsn0Le_s0&m=qAW4D4jYUflhub89i8X5SO9kX1jL10NxjWpXsyy4PHg&s=V3kusqWSQn3F28jCa-fxMmvNKCK12hyWwLWGYPJ1Ogo&e=>
to let me know all the available times you can meet with him.
Please note two items: 1. Due to other commitments Alan will be taking him
to lunch instead of dinner. Let me know if you can take him to dinner. 2.
The talk is schedule for 3 PM instead of the usual 4 pm talk.
Please respond by Thursday, Feb 4.
Thank you,
Cathy
Molecular evolution meets biophysics: the history of the RubisCO enzyme and
the Fenna-Matthews-Olson (FMO) complex
February 9, 2016 at 3:00pm/36-428*
*Romain Studer, *
*The European Bioinformatics Institute, European Molecular Biology
Laboratory (EMBL-EBI)*
[image: studer_romain_web]
Ancestral sequence reconstruction allows the inference of a protein’s
past characteristics at a particular point during its evolution. The
inferred ancestral sequence can be modelled in 3D, assuming a structural
template exists. Having ancestral structures allows a better understanding
of protein evolution and protein function. Ultimately, the ancestral
sequence can be resurrected in vitro by synthesis and purification and its
properties can be studied using the standard protocols, used its for modern
counterparts. Recent successful studies using ancestral
sequence reconstruction have focused on old proteins (Groussin et al., Biol
Lett. 2013), nuclear receptors (Harms et al., PNAS 2013) or cetacean
myoglobins (Dasmeh P. et al., PLOS Comp Biol 2013). In this talk, I will
give an introduction to methodologies used to infer ancestral sequences and
to identify amino acids under selective pressures. I will present some
studies that successfully used these methods. Finally, I will present my
recent work on RubisCO (Ribulose-1,5-bisphosphate
carboxylase/oxygenase), the main enzyme responsible for the fixation of CO2
in bacteria and plants (Studer RA et al., PNAS 2014) and our current
collaborative project on the Fenna-Matthews-Olson (FMO) complex, which
participate in energy transfer in Bacteria.
*Romain Studer* is a postdoctoral fellow within the lab of Dr. Pedro
Beltrao at the European Bioinformatics Institute (EMBL-EBI) in Cambridge,
UK. He is now studying the evolution of posttranslational modification
(PTM) of amino acids. He did his PhD at University of Lausanne (2005-2009),
under the supervision of Prof. Marc Robinson-Rechavi. He studied the impact
of whole-genome duplications in vertebrates’ evolution and initiated the
development of Selectome, a database of positive selection. In 2010, he
collaborated with Prof. Bernard Rossier (University of Lausanne) to work on
the evolution of sodium regulation. He then received a fellowship grant
from the Swiss National Science Foundation to continue his research at
University College London within the lab of Prof. Christine Orengo
(2010-2013). He conducted several evolutionary projects, on the RubisCO
enzyme and on the coagulation system. His research interest is to study the
evolution of biological systems by integrating knowledge from phylogenetic
inference, structural information and biochemical function.
*please note time change to 3:00 pm instead of 4:30 pm
--
Stéphanie Valleau
PhD student in Chemical Physics
Harvard University CCB,
12 Oxford St. Mailbox 312,
Cambridge, MA, USA
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