has offered his bacteriorhodopsin project as a
resource. If anybody else has been assigned a membrane protein, please feel
free to contact me at "email@example.com".
Added by: Roy Lancasterroylanc on Su Mar 26 19:53:49 BST 1995
I'll do an essay on protein translocation (to cover the role of signal peptides unless someone else wants that). Any suggestions/help welcome, mail me at:
Added by: Mia Unson (firstname.lastname@example.org) on Fri Mar 31 21:24:03 BST 1995
Hi since I have a G-protein I thought is would be nice to do hypertext pages
on how to determine the E, G, and R regions of this protein from
secondary structure calculations. I will probably have the pages done by
the end of the first week in May
Added by: FRED-G on Mo Apr 3 00:58:34 BST 1995
I will try to contribute something about multi-phosphorylated peptides.
Added by: 4cms on Mo Apr 3 02:12:08 BST 1995
I'm interested in the question of symmetry in protein association. Any co- investigators or tips would be welcome. Does anyone have a protein that, in the crystal, forms nearly but not quite symmetrical associations?
Added by: Steve Durbin 1HC1 (email@example.com) on Wed Apr 5 16:23:12 BST 1995
I am working on the structure of membrane-spanning transport proteins, one amino acid transport protein in particular. I have a sequence and have modeled several putative secondary structures. I have identified foour MSD's and am now working on the orientation of these alpha structures within the membrane. I have many resources available to me and would like someone to help. Our project involves analysis of patient DNA, modeling of putative mutant structures, assignment of domains, analysis of energy reduction models, etc. Persons who possess mutant forms of this particular protein are usually afflicted with cystinuria or suffer from cystine stones in the kidneys. I have access to a SGI workstation with LOOK, AMBER and MIDASplus at UCSF. I have worked out secondary structures at EMBL. I really need other persons to help me analyze the structures of this as-yet unnamed protein. Please email me for more info: firstname.lastname@example.org
Added by: Jeremy Bruce (email@example.com) on Fri Apr 7 03:38:03 BST 1995
I am interested in the project about DNA binding proteins.
Added by: SolomonT on Sat Apr 8 15:21:44 BST 1995
It has occurred to me th of us undergraduates could actually take our individual protein
and predict all attributes of its structure including how the
structure contributes to function as a senior research project for their undergraduate degree.
I am in the process of checking to see if my university will alllow me to take this approach to
my senior research project. Has any body else checked on the possibility of doing a seniro research project in this way?
Added by: FredG (FAGROTT@INDYVAX.IUPUI.EDU) on Mo Apr 17 18:30:38 BST 1995
I have previously volunteered to work on poly proline helices.
Any help would be greatly appreciated.
If there is anyone out there with proteins containing poly
proline helices, i would appreciate any information you could offer
//even if it is as little as the name of your protein//.
Added by: JeffreyB (firstname.lastname@example.org on Tue Apr 18 09:49:49 BST 1995
I would like to take a look at how sequence motifs/fingerprints relate to function and structure.
My project will also incorporate a description of the resources available on the web - eg PROSITE,
PRINTS, BLOCKS et al.
Added by: Emer Brizzolara on Wed Apr 19 22:13:24 BST 1995
I will try to construct a page for Serine Proteases on the Protein Family page.
I would like to include modelling the active site/substrate in 3-D (Rasmol, etc).
Added by: 2alp (Bill Chestnut) on Fri Apr 28 05:14:27 BST 1995
I came across a protein "ribonuclease inhibitor" which
has horse-shoe like shape, with alpha,beta structures alternating.
SCOP has classified it as alpha/beta protein.
Are there any structures similar in sequence or structure to
that? This protein source is from porcine.
Added by: email@example.com on Fri Apr 28 18:13:22 BST 1995
I will create an HTML document designed to explore signal transduction in CheY and a related bacterial protein that I study called DctD. These proteins are regulated by phosphorylation, often involving a cascade in which the phosphate moves through several proteins. CheY is one of the best studied cases to date, and DctD is dear to my own heart. An exercise will be posted for modeling DctD structure after CheY structure. The material will be posted on http://www.bmb.psu.edu/pps/ In addition I will post an article on using global statistical analysis of DNAse 1 footprinting to extract cooperativity and intrinsic binding energies for a two-site system (same http address).
Added by: B. Tracy Nixon on Tue May 9 23:17:25 BST 1995
I did my graduate work on the incorporation of selenomethionine in
recombinant proteins and the application of the anomalous scattering
of Se for MAD phasing in X-ray crystallography. For my project, I will
review the "process" from growing bacteria to solving structures would
be discussed along with structures that have utilized SeMet thus far.
Please send me comments about what you would like to see in such a review.
Added by: John Horton on Wed May 10 19:12:29 BST 1995
This is a test. I'm really pleased how well this course has gone.
Please feel freee to keep using
Peter MR (from a strange address!)
Added by: PeterMR on Mo Ju 26 15:30:00 BST 1995
I would like to apply chaos theory to analyse the differences between folded and unfolded proteins. I'm planning to use techniques developed for time series analysis so I would need
experimental data, I'm thinking on time-resolved fluorescence spectroscopy or stopped-flow CD measurements (sampling time in the order of ms or less if possible). I don't have any
particular preference. All data are welcomed. Paper in Nature promissed :-) if results are OK.
Added by: J.M. Zaldivar (firstname.lastname@example.org) on Wed May 22 15:07:21 BST 1996