Biophysical Netsletter - May 2014

9

BIOPHYSICAL SOCIETY NEWSLETTER

2014

MAY

Know theEditors LeonidBrown University ofGuelph Editor inCell Biophysics Section

Viscoelasticity of TauProteins Leads to StrainRateDepen- dent Breaking ofMicrotubules DuringAxonal Stretch Injury: Predictions from aMathemati- calModel byVivekShenoy, 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

HosseinAhmadzadeh, andDouglas Smith.

LeonidBrown

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.

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.