Center for Single Molecule Biophysics

Auerbach Lab :
We study ligand-gated ion channels that mediate neuron-neuron and nerve-muscle transmission. Transmitter molecules coax these receptors to change from a closed- to an open-channel conformation. A major goal of our lab is to understand the molecular details of this 'gating' reaction, as well as the other reactions that drive the synaptic response, for example transmitter binding and desensitization. We measure single-channel kinetics to probe the energy landscapes of these reactions (using wild-type and mutant receptors), and relate these results regarding reaction mechanism to the physiological response of the synapse.

Sachs Lab :
My scientific interests span the range of organs to molecules, and the development of new technical methods. For the last twenty years, I have focused on the area of cell mechanics and the mechanisms by which mechanical forces are transduced into cellular signals such as voltage, Ca2+ and cell volume and the cytoskeleton, the research has a broad reach. We discovered mechanosensitive ion channels in 1983, and have since then studied the biophysics and cell biology. Our methodology has includes patch clamp, high resolution light microscopy, real time fluorescence microscopy, high speed digital microscopy, TIRF, digital image analysis, high voltage EM, EM tomography, AFM, molecular biology, natural product and recombinant protein biochemistry and 2DNMR structures. We have discovered the only specific inhibitor of mechanosensitive ion channels - a small peptide in tarantula venom, and have demonstrated some clinical applications for brain tumors and cardiac arrhythmias.

Zhou Lab :
Our group's research focuses on developing and utilizing statistical mechanics theories, bioinformatic, and simulation methods to explain and predict the behavior of biologically interesting macromolecules. The current research program aimed at the understanding of the molecular mechanisms and bioinformatic studies of protein folding, stability, and binding. The long-term goal of the proposed research is to elucidate the relations between the sequence, structure, and function of proteins and to uncover the molecular mechanism associated with solute-assisted protein denaturation and stabilization. This will be accomplished by designing simple (yet realistic) models and by developing statistical mechanics theories.

Qin Lab :
Noxious stimuli such as protons (H+), temperature (temp) etc. applied to endorgans activate nociceptors. Injury leads to the release of prostaglandins such as prostaglandin E2 (PGE2), serotonin (5-HT), nerve growth factor (NGF) etc. from damaged cells, Bradykinin (BK) from blood vessels and substance P (sP) from nociceptors. These agents either activate nociceptors directly or senstitize them to subsequent stimuli by parallel activation of intracellular kinases by G-protein coupled receptors and tyrosine kinase receptors. Primary nociceptive afferents (C-fibers, Ad-fibers) of dorsal root ganglion (DRG) neurons synapse on second order neurons (S) in the spinal dorsal horn (magnified in inset). Here, glutamate (Glu) and sP released from primary afferent terminals (A) activate glutamate receptors (NMDA R, AMPA R, mGluRs) and neurokinin-1 (NK-1) receptors, respectively, located post-synaptically on spinal neurons. These synapses are negatively modulated by spinal inhibitory interneurons (I), which employ enkephalins (Enk) or gamma-amino-butyric acid (GABA) as neurotransmitters. Spinal neurons convey nociceptive information to the brain and brainstem. Activation of descending noradrenergic and/or serotonergic systems, which originate in the brain and brainstem, leads to the activation of spinal inhibitory interneurons (I) thereby resulting in antinociception. (From http://encref.springer.de/mp/0002.htm)

Bianco Lab :
The work in my laboratory focuses on DNA motor protein complexes or DNA nano-machines. These machines are frequently coupled to, or powered by, DNA helicases. DNA helicases are ubiquitous enzymes whose primary function is to unwind DNA duplexes into their component single strands, a process that is coupled to the hydrolysis of nucleoside 5'-triphosphates. Our work is aimed at understanding DNA helicase mechanism(s) and how these mechanisms contribute to and are adapted to the processes of replication, recombination, DNA repair and transcription.