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Stabilization of collagen structure: Dependence of collagen denaturation enthalpy on the imino acid content

✍ Scribed by T. V. Burjanadze

Publisher: Wiley (John Wiley & Sons)
Year: 1982
Tongue: English
Weight: 497 KB
Volume: 21
Category: Article
ISSN: 0006-3525
DOI: 10.1002/bip.360210809

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✦ Synopsis

Abstract

An analysis of the available data on the enthalpy (Δ__H__~r~) of denaturation (melting) of collagens with different imino acid content in solution and in the aggregated state has shown that Δ__H__~r~ in solution increases with increasing denaturation temperature, whereas in the aggregated state there is an inverse dependence. Δ__H__~r~ in solution correlates with the hydroxyproline content but not with that of proline. No correlation between the change of Δ__H__~r~ and the imino acid content is observed for the aggregated state.

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✍ T. V. Burjanadze; E. L. Kisiriya 📂 Article 📅 1982 🏛 Wiley (John Wiley & Sons) 🌐 English ⚖ 349 KB 👁 1 views

## Abstract The probable number of hydrogen bonds has been calculated as a function of the imino acid content for water‐bridged collagen structures. With increasing imino acid content in collagen, the number of hydrogen bonds stabilizing triple‐helical structures become saturation. This might expla