DOI: 10.1073/pnas.032307099. Type I collagen is thermally unstable at body temperature

Type I collagen is thermally unstable at body temperature

10.1073/pnas.032307099

Crossref journal-article

Proceedings of the National Academy of Sciences

Proceedings of the National Academy of Sciences (341)

Abstract

Measured by ultra-slow scanning calorimetry and isothermal circular dichroism, human lung collagen monomers denature at 37°C within a couple of days. Their unfolding rate decreases exponentially at lower temperature, but complete unfolding is observed even below 36°C. Refolding of full-length, native collagen triple helices does occur, but only below 30°C. Thus, contrary to the widely held belief, the energetically preferred conformation of the main protein of bone and skin in physiological solution is a random coil rather than a triple helix. These observations suggest that once secreted from cells collagen helices would begin to unfold. We argue that initial microunfolding of their least stable domains would trigger self-assembly of fibers where the helices are protected from complete unfolding. Our data support an earlier hypothesis that in fibers collagen helices may melt and refold locally when needed, giving fibers their strength and elasticity. Apparently, Nature adjusts collagen hydroxyproline content to ensure that the melting temperature of triple helical monomers is several degrees below rather than above body temperature.

Bibliography

Leikina, E., Mertts, M. V., Kuznetsova, N., & Leikin, S. (2002). Type I collagen is thermally unstable at body temperature. Proceedings of the National Academy of Sciences, 99(3), 1314â1318.

Authors 4

E. Leikina (first)
M. V. Mertts (additional)
N. Kuznetsova (additional)
S. Leikin (additional)

References 27 Referenced 479

P L Privalov Adv Prot Chem 35, 1–104 (1982). / Adv Prot Chem by Privalov P L (1982)
K A Piez Extracellular Matrix Biochemistry, eds K A Piez, A H Reddi (Elsevier, New York), pp. 1–40 (1984). / Extracellular Matrix Biochemistry by Piez K A (1984)
10.1038/33573
10.1002/1097-0282(20010415)58:5<459::AID-BIP1021>3.0.CO;2-V
10.1074/jbc.273.48.31822
10.1096/fasebj.5.7.2010058
10.1073/pnas.070050097
10.1006/jmbi.1994.0035
10.1021/bi980089
10.1074/jbc.274.51.36083
10.1021/bi00872a035
10.1016/S0934-8832(11)80077-6
S R Lamande, J F Bateman Cell Dev Biol 10, 455–464 (1999). / Cell Dev Biol by Lamande S R (1999)
10.1016/S0945-053X(00)00071-8
10.1016/S0006-3495(99)77476-X
10.1016/S0945-053X(01)00137-8
10.1016/S0945-053X(01)00138-X
S P Robins Biology of Collagen, eds A Viidik, J Vuust (Academic, London), pp. 135–151 (1980). / Biology of Collagen by Robins S P (1980)
10.1042/bj1020143
10.1042/bj1600243
10.1042/bj2400431
10.1111/j.1432-1033.1984.tb08115.x
10.1093/emboj/19.10.2204
10.1083/jcb.150.6.1499
10.1016/S0968-0004(06)80023-X
10.1016/0003-9861(83)90621-5
10.1016/S0021-9258(19)81546-6

Dates

Type	When
Created	23 years, 1 month ago (July 26, 2002, 10:36 a.m.)
Deposited	3 years, 4 months ago (April 12, 2022, 9:06 a.m.)
Indexed	1 week ago (Aug. 21, 2025, 1:57 p.m.)
Issued	23 years, 7 months ago (Jan. 22, 2002)
Published	23 years, 7 months ago (Jan. 22, 2002)
Published Online	23 years, 7 months ago (Jan. 22, 2002)
Published Print	23 years, 6 months ago (Feb. 5, 2002)

Funders 0

None

BibTeX

@article{Leikina_2002, title={Type I collagen is thermally unstable at body temperature}, volume={99}, ISSN={1091-6490}, url={http://dx.doi.org/10.1073/pnas.032307099}, DOI={10.1073/pnas.032307099}, number={3}, journal={Proceedings of the National Academy of Sciences}, publisher={Proceedings of the National Academy of Sciences}, author={Leikina, E. and Mertts, M. V. and Kuznetsova, N. and Leikin, S.}, year={2002}, month=jan, pages={1314–1318} }

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