Research Topics
Antimicrobial Peptides:
Mechanism of AMP
Energetics of Pore Formation
Toroidal vs. Barrel Stave Model
Observation of Pores
Peptide Orientation Change
Membrane Thinning Effect
Concentration Dependence
Experimental Methods:
Oriented Circular Dichroism
In-plane Scattering
Diffraction Techniques
Lipid Dynamics by IXS
Anomalous Diffraction
Peptide-Lipid Interact:
Hydrophobic Matching
Membrane-mediated Protein Interactions
Elasticity Theory and Thermodynamics
Fusion and Lipids:
Bending & Lipid Demixing
Chain Volume Conservation
LPS and others
Gramicidin Problems:
Channel Poperties
Model Studies
Amphipathic Drugs
Green Tea extract
Apoptosis-regualating Proteins

Huey W. Huang - Sam and Helen Worden Professor Emeritus
Department of Physics & Astronomy - Rice University - phone: 713-348-4899 - fax: 713-348-4150

Thermodynamics for Introductory Physics or Chemistry in 14 Pages

                                                               RECENT PUBLICATIONS  with Links to PDF files

Research Interests

Soft-Matter Physics  A lipid bilayer is a two-molecule-thick, flexible, two-dimensional fluid with many internal degrees of freedom.  Peptide interactions can induce local structural changes in the bilayer.  Elucidation of such structural changes and the associated energetics is the key for understanding the biological consequences of membrane-active peptides.

Highlights of our research include developing the methods of oriented circular dichroism, X-ray and neutron in-plane scattering, anomalous diffraction for membrane structures and method of giant lipid vesicles with peptides.  Highlights of our discoveries include the toroidal pores, membrane-thinning effect, lipid extracting effect, peptide orientation change in membranes, structure of the membrane fusion intermediate state stalk, structure of a pre-stalk intermediate state, crystal structures of barrel-stave pores and toroidal pores. 

      Biology  The lipid bilayer of a cell membrane is the target of membrane-active peptides including antibiotics and beta-amyloid proteins.  Peptide-membrane interactions are the mechanisms of several new structural classes of antibiotics and the key for understanding the amyloid diseases, including Alzheimer’s and type II diabetes.
X-ray electron density of alamethicin pore, melittin pore and the contact state of two bilayers before hemifusion.

 A lipid vesicle exposed to Melittin.          A lipid vesicle exposed to Daptomycin.        Hemifusion between two lipid vesicles.

All Papers on Mbrn. Biophysics