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Specialty Chemistry Forums => Biochemistry and Chemical Biology Forum => Topic started by: Proteonomeo22 on November 11, 2021, 05:39:00 AM

Title: Secondary structure of peptide-chain
Post by: Proteonomeo22 on November 11, 2021, 05:39:00 AM
I have the following peptide-sequence #IATGMVGALLLLLVVALGIGLFM# Which secondary structure would it get and why? What would stablize it? My reasoning is that it would become a beta-sheet because we have Val and Ile that  destabilizes alfa-helix structures but are ok in beta-sheets. On the other hand we have a majority of alfa-helix probable aminoacids, and this is where I can't come to a conclusion. What would stabilize the beta-sheet of this particular peptide-sequence (if it now is a beta-sheet) and how do I know why it would become this structure. Also how do I know if the netcharge is 0?

PEPTIDE-SEQUENCE

IATGMVGALLLLLVVALGIGLFM

Thank you!
Title: Re: Secondary structure of peptide-chain
Post by: Proteonomeo22 on November 11, 2021, 12:09:05 PM
The sequence
Title: Re: Secondary structure of peptide-chain
Post by: Babcock_Hall on November 11, 2021, 06:13:35 PM
A peptide of this length may not have any secondary structure in solution.  If it were part of a larger peptide, that is another matter.