Predicting Collagen Triple Helix Stability through Additive Effects of Terminal Residues and Caps
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Date
2023-01-16
Publication Type
Journal Article
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yes
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Abstract
Collagen model peptides (CMPs) consisting of proline-(2S,4R)-hydroxyproline-glycine (POG) repeats have provided a breadth of knowledge of the triple helical structure of collagen, the most abundant protein in mammals. Predictive tools for triple helix stability have, however, lagged behind since the effect of CMPs with different frames ([POG](n), [OGP](n), or [GPO](n)) and capped or uncapped termini have so far been underestimated. Here, we elucidated the impact of the frame, terminal functional group and its charge on the stability of collagen triple helices. Combined experimental and theoretical studies with frame-shifted, capped and uncapped CMPs revealed that electrostatic interactions, strand preorganization, interstrand H-bonding, and steric repulsion at the termini contribute to triple helix stability. We show that these individual contributions are additive and allow for the prediction of the melting temperatures of CMP trimers.
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published
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Journal / series
Volume
62 (3)
Pages / Article No.
Publisher
Wiley-VCH
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Edition / version
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Date collected
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Subject
Collagen; Peptides; Terminal Capping Group; Thermal Stability; nāĻ* Interaction
Organisational unit
03940 - Wennemers, Helma / Wennemers, Helma
Notes
Funding
207505 - Synthetic Collagen (SNF)
891009 - Collagen Origami (EC)
891009 - Collagen Origami (EC)