Cooperative equilibrium transitions coupled with a slow annealing step explain the sharpness and hysteresis of collagen folding. (Q52075488)

21 April 2018

title

Cooperative equilibrium transitions coupled with a slow annealing step explain the sharpness and hysteresis of collagen folding. (English)

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21 April 2018

author name string

Engel J

series ordinal

1

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21 April 2018

Bächinger HP

series ordinal

2

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21 April 2018

publication date

1 July 2000

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21 April 2018

published in

Matrix Biology

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21 April 2018

volume

19

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21 April 2018

issue

3

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21 April 2018

page(s)

235-244

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21 April 2018

The role of cis-trans isomerization of peptide bonds in the coil leads to and comes from triple helix conversion of collagen

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Consideration of the possibility that the slow step in protein denaturation reactions is due to cis-trans isomerism of proline residues

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Three conformationally distinct domains in the amino-terminal segment of type III procollagen and its rapid triple helix leads to and comes from coil transition

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Formation of the triple helix of type I procollagen in cellulo. A kinetic model based on cis-trans isomerization of peptide bonds

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Inductive Effects on the Energetics of Prolyl Peptide Bond Isomerization: Implications for Collagen Folding and Stability

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Glycosylated threonine but not 4-hydroxyproline dominates the triple helix stabilizing positions in the sequence of a hydrothermal vent worm cuticle collagen

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Detection of cis and trans X-Pro peptide bonds in proteins by 13C NMR: application to collagen

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7 January 2021

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Identifiers

DOI

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21 April 2018

1 reference

21 April 2018