BIOPHYSICAL SOCIETY NEWSLETTER
9
MAY
2014
Viscoelasticity of TauProteins
Leads to StrainRateDepen-
dent Breaking ofMicrotubules
DuringAxonal Stretch Injury:
Predictions from aMathemati-
calModel
byVivekShenoy,
HosseinAhmadzadeh, andDouglas Smith.
UnknownUnknowns: The
Challenge of Systematic and
Statistical Error inMolecular
Dynamics Simulations
, byAlan
Grossfield, whichhighlights
the paper
IndolicidinBinding
Induces Thinning of aLipid
Bilayer
, byRégis Pomès, Chris
Neale, JennyHsu, andChristopher Yip.
DriftingThrough the Beehive
by
BrianRoth, whichhighlights
the article
Attraction of Ro-
tors to the PulmonaryVeins in
Paroxysmal Atrial Fibrillation:
AModeling Study
by Omer
Berenfeld, ConradoCalvo,
MakarandDeo, SharonZlochiver, and JoséMillet.
The Importance of Intrinsic
Order in aDisorderedProtein
Ligand
byNatalieGoto, which
highlights the paper
Confor-
mational Recognition of an
IntrinsicallyDisorderedProtein
byAlfonsoDe Simone, James
Krieger,Giuliana Fusco,Marc
Lewitzky, PhilipSimister, JanMarchant, Carlo
Camilloni, andStephanFeller.
Review
TheReview
Membrane Protein
Structural Validation byOri-
ented Sample Solid StateNMR:
Diacylglycerol Kinase
byTimo-
thyCross,DylanT.Murray,
ConggangLi, F. PhilipGao,
andHuajunQinwas high-
lighted in theApril 15 Issue. Visit thewebsite to
read the full article.
Know theEditors
LeonidBrown
University ofGuelph
Editor inCell Biophysics Section
Q:
What isyour areaof research?
Adiverse group of light-sensitivemembrane
proteins, calledmicrobial rhodopsins, has been
the focus ofmy research formany years. In the
past, it was thought that these proteins exist only
in a small group of halophilicArchaea (Halobac-
teria), but lately it became obvious thatmicrobial
rhodopsins are omnipresent ecologically and
taxonomically, being found inmany bacterial,
fungal, and algal taxa.The range of their functions
expanded substantially as well, from the original
ionpumps andphotosensors to light-gated ion
channels and light-switchable enzymes. Recently,
microbial rhodopsins became very popular in the
neurobiology community for their use in optoge-
netics.
My research onmicrobial rhodopsins startedwith
the prototypical light-drivenprotonpump bacte-
riorhodopsin, which entered almost every bio-
chemistry textbook as the simplest bioenergetics
machine. Later, it expanded to include other ion
pumps andphotosensors,mainly from bacteria
and fungi.We have beenusing a powerful combi-
nation of site-directedmutagenesis withdifferent
types of biophysical techniques,mainly spectro-
scopic, to dissect functionalmechanisms of these
proteins.The types of spectroscopywe employ
include time-resolved laser spectroscopy in the
visible, static and time-resolved infrared spectros-
copy, Raman spectroscopy, and,more recently,
solid-stateNMR (in collaborationwithVladimir
Ladizhansky).The latter development brought us
closer to structural biology and allowed expand-
ing our efforts to othermembrane proteins, such
as aquaporins andGPCRs. I have been blessed
with a number of other great collaborators, who
enriched our researchwith their expertise inmass
spectrometry, ultrafast spectroscopy, low-tempera-
ture spectroscopy,molecularmicrobiology, SAXS,
andEPR.
LeonidBrown
