Dear Kishore,
Tetrapeptides to hexapeptides are shown to form beta sheets. In fact, these peptides make the amyloid fibrils which are formed of beta sheets. But I'm not sure whether a tripeptide will make beta sheet or not. You might find the following reference useful:
http://www.nature.com/nature/journal/v447/n7143/full/nature05695.html
There are ways where you can design peptides which should form beta sheet. For that you might find the following references useful:
http://www.pnas.org/content/99/5/2754.long
http://www.ncbi.nlm.nih.gov/pubmed/11880628
Best wishes,
Jogender
thank You Jogender Singh .i hope i may be able to figure out the good idea from this.
Hello Kishore,
Surely all polypeptides (including di and tripeptides) can form beta sheets under appropriate conditions as also noted by Dobson. Here is a reference which you may be interested in
Street, A. G., & Mayo, S. L. (1999). Intrinsic β-sheet propensities result from van der Waals interactions between side chains and the local backbone. Proceedings of the National Academy of Sciences of the United States of America, 96(16), 9074-9076.
Regards,
Anant Dave
so can i create the beta sheet just by changing the solvent condition and i want to know exactly at what temperature and solvent condition this is possible
?
Yes indeed! This is the principle of amyloid fibril formation which lead to pathological conditions such as Alzheimer's disease. In these conditions, the protein that remains usually correctly folded or unfolded, can undergo protein misfolding due to stresses imposed by the environmental conditions such as solvent composition. However, the optimum conditions for the self-assembly polypeptides vary greatly and you will have to look into literature for the data on the self-assembly of sequences which are closer to yours.
I recommend visiting the "Amyloid Protocols" project page on Researchgate. This project was created by Dr. Jeffrey R. Brender, who is also following this question. You may find useful references and resources for your work on that page.
Regards,
Anant Dave
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