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
Magainin
Protegrin
theta-Defensin
Alamethicin
Melittin
Experimental Methods:
Oriented Circular Dichroism
In-plane Scattering
Diffraction Techniques
Lipid Dynamics by IXS
Anomalous Diffraction
GUV
Peptide-Lipid Interact:
Hydrophobic Matching
Membrane-mediated Protein Interactions
Elasticity Theory and Thermodynamics
Fusion and Lipids:
Stalk
Bending & Lipid Demixing
Chain Volume Conservation
LPS and others
Cholesterol
Gramicidin Problems:
Channel Poperties
Model Studies
Amphipathic Drugs
Curcumin
Green Tea extract
Apoptosis-regualating Proteins
Bax

RECENT PUBLICATIONS
 with Links to PDF files


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

Research Interests

      Lipid molecules of cell membranes play important roles in all sorts of cellular functions, yet their molecular mechanisms are largely unknown, besides the obvious role of forming a hydrophobic barrier surrounding aqueous contents. The fact that each cell maintains its organism-specific lipid compositions and that each type of lipid has its own distinct physical property strongly suggest correlations between the physical properties of lipids and lipid related functions.  The challenge to membrane biophysicists is to show these correlations in the fashion of the standard paradigm, i.e., structure-function relationships.
     We found membran-active proteins and peptides an excellent system for biophysical studies. Most of these proteins are water-soluble, yet they spontaneously bind to the lipid matrix of cell membranes and exert their functions.  We started with the simplest antimicrobial peptides, including gramicidin, alamethicin, melittin, magainin and protegrin, in order to understand the basic principles of molecular interactions with membranes.  The diversity of these peptides exposed different aspects of such interactions, and led us to develop special techniques for investigating the induced structural changes in membrane.  These knowledge and techniques have also been applied to the studies of amphipathic drugs, pore-forming proteins, including apoptosis-regulating Bax, and membrane fusion.
     Because membranes are soft matter, many well-established microscopic structural tools have difficulties.  Over the years, the lab has developed many methods for the structural studies of membranes. Below is our recent structure work: the electron densities of the barrel-stave pore (left), the toroidal pore (middle), and a pre-stalk state of membrane fusion.




All Papers on Mbrn. Biophysics