Predicting collagen stability from sequence
The collagen triple helix motif is found widely in structural proteins of the extracellular matrix and in an increasing set of non-collagenous proteins, many of which are involved in host-defense function. The close packing of three supercoiled chains in the collagen triple helix generates a requirement for Gly as every third amino acid residue.
Experimental thermal stability data obtained from host-guest peptides is integrated here to produce an algorithm for predicting global melting temperatures of collagen triple helical peptides and short fragments, and for detecting modulations in relative stability along a collagen chain.
Please choose one of the two options below.
Predict melting temperature (Tm) of short peptides
For short collagen peptides (<90 residues per chain). Good agreement was observed between predicted and observed stabilities (see References). Run your sequence through the predictor before spending time and money making peptides.
Generate relative stability profile for longer collagen sequences
For local stability variations along full-length collagens and their relation to functional domains or mutation sites, including heterotrimers. No size limit. Please check your sequences and read the Help page before submitting.
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