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Code for collagen's stability deciphered

Nature volume 392, pages 666–667 (1998) Cite this article

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Abstract

The most abundant protein in animals is collagen. In connective tissue, this protein is present as chains wound in tight triple helices which are organized into fibrils of great tensile strength and thermal stability1,2. We propose a new explanation for this stability.

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Figure 1: Circular dichroism spectra of collagen-related peptides.
Figure 2: Thermal denaturation of collagen-related triple helices.

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Authors and Affiliations

  1. Departments of Biochemistry and Chemistry, University of Wisconsin-Madison, Madison, 53706, Wisconsin, USA

    Steven K. Holmgren, Kimberly M. Taylor, Lynn E. Bretscher & Ronald T. Raines

Authors
  1. Steven K. Holmgren
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  2. Kimberly M. Taylor
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  3. Lynn E. Bretscher
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  4. Ronald T. Raines
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Holmgren, S., Taylor, K., Bretscher, L. et al. Code for collagen's stability deciphered. Nature 392, 666–667 (1998). https://doi.org/10.1038/33573

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