• Description

  • Application Data


Polyproline-13 (Pro13) forms helices and is proposed to be part of the protein state. Pro13 is used in protein folding analysis.

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Application Data

Catalogue number crb1001298
Molecular Weight 1279.7
Sequence (one letter code)


Sequence (three letter code)


Aliase Pro13, PPII, PPI, polyproline helix
Purity >95%
Storage -20°C

Clemmer et al., (2017). Characterizing the conformationome: toward a structural understanding of the proteome. Acc. Chem. Res., 50(3): 556. doi: 10.1021/acs.accounts.6b00548. 

Manufactured in: United Kingdom
Data Sheet Material Safety Data Sheet (MSDS)

Polyproline-13 (Pro13) forms a helix, and it is a naturally occurring secondary structure. Pro13 is used as a model peptide to help understand the folding mechanisms and intermediates of the proteome. Pro13 can exist in a cis-orientation leading to the formation of the right-handed PPI helix; this is more favourable in non-polar solvents. Alternatively, Pro13 can have a trans-orientation leading to a left-handed PPII helix favoured in polar solvents. Pro13 can interchange these forms by altering the solvent composition, as determined by circular dichronism spectroscopy. The ability to observe the reversible transition between PPI and PPII, and its intermediates, has been hampered by a lack of methodologies, and thus the mechanistic pathway remains unclear. There is PPII helix content in proteins, and the role that PPII conformations play in the non-structured state of polypeptides is still being investigated. Free energy landscapes of polyprolines in various solvents have helped to understand their relative stability and improve the information about the transition pathway between the helices.


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