Richard J. Law, McCammon Group, LMB, University of California San Diego.

My research interests lie around the area of membrane protein structure determination and simulation from low/medium resolution data, but have also investigated ligand binding in such systems - namely the cys loop ligand gated ion channels.

I am currently in the 2nd year of a post-doctoral position in the McCammon Group. My main interst during my tie here has concerned ion conduction and gating mechanisms in the nicotinic acetlycholine receptor.

Here is a recent workshop that I conducted in CTBP concerning the set up of a membrane protein simulation

Here you can download a couple of short movies of steered ion conduction through a M2 helix pore model of the nicotinic channel (Best to right-click and save).
Ion pulling movie 1
Ion pulling movie 2

The main sublect of investigation towards the end of my Phd was Human Aquaporin-1 either working with 2D crystallography data or by homology modelling against the GlpF crystal structure. I'm then using MD simulation to attempt to answer the question of how aquaporin stabilises a column of water in the pore (as in the spinning model in the corner) without allowing the passage of protons or other charged particles, and how this differs from GlpF channel environment, which facilitates the transport of glycerol.

The Kcsa potassium channel structure has been used as a template for many homology models, and I used it to approach the modeling of twin-domain like potassium channels - specifically using the simpler case of the C.elegans Twk-5 sequence to attack the more complex problem of the H-TWIK-1 structure. To help with the process of homology modeling, I have tried to develop a method of testing alignments and models using a statistical comparison of sequence variability and surface accessibility of residues in the template and model.


	McCammon Group Chemistry and Biochemistry Dept, M/C 0365, Urey Hall, 9500, Gilman Drive, University of California San Diego San Diego, 92093, USA	Tel +1 858 349 6369 Fax +1 858 534 7042 Email:rlaw@mccammon.ucsd.edu
	My research interests lie around the area of membrane protein structure determination and simulation from low/medium resolution data, but have also investigated ligand binding in such systems - namely the cys loop ligand gated ion channels. I am currently in the 2nd year of a post-doctoral position in the McCammon Group. My main interst during my tie here has concerned ion conduction and gating mechanisms in the nicotinic acetlycholine receptor. Here is a recent workshop that I conducted in CTBP concerning the set up of a membrane protein simulation Here you can download a couple of short movies of steered ion conduction through a M2 helix pore model of the nicotinic channel (Best to right-click and save). Ion pulling movie 1 Ion pulling movie 2 The main sublect of investigation towards the end of my Phd was Human Aquaporin-1 either working with 2D crystallography data or by homology modelling against the GlpF crystal structure. I'm then using MD simulation to attempt to answer the question of how aquaporin stabilises a column of water in the pore (as in the spinning model in the corner) without allowing the passage of protons or other charged particles, and how this differs from GlpF channel environment, which facilitates the transport of glycerol. The Kcsa potassium channel structure has been used as a template for many homology models, and I used it to approach the modeling of twin-domain like potassium channels - specifically using the simpler case of the C.elegans Twk-5 sequence to attack the more complex problem of the H-TWIK-1 structure. To help with the process of homology modeling, I have tried to develop a method of testing alignments and models using a statistical comparison of sequence variability and surface accessibility of residues in the template and model.