Flexibility of tropocollagen from sedimentation and viscosity

Utiyama, Hiroyasu; Sakato, Kuniaki; Ikehara, Kenji; Setsuiye, Takashi; Kurata, Michio

doi:10.1002/bip.1973.360120106

Cited by 46 publications

(23 citation statements)

References 42 publications

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“…The tissue-derived collagen preparations always contain a fraction of chemically cross-linked monomers (Nimni, 1983). The intermolecular and intramolecular cross-links could have an effect on the persistence length of collagen (Utiyama et al, 1973;Saito et al, 1982;Nestler et al, 1983;Hofmann et al, 1984). Finally, the persistence length of biopolymers can be significantly influenced by the physicochemical properties of a solvent (Hagerman, 1988;Baumann et al, 1997;Wang et al, 1997).…”

Section: Resultsmentioning

confidence: 98%

“…Finally, the persistence length of biopolymers can be significantly influenced by the physicochemical properties of a solvent (Hagerman, 1988;Baumann et al, 1997;Wang et al, 1997). Because collagen molecules do not aggregate into fibrils at low pH levels (Boedtker and Doty, 1956), in previous studies, tissueextracted collagen monomers were tested in acidic solutions (Utiyama et al, 1973;Saito et al, 1982;Nestler et al, 1983) or protein samples were dissolved in acidic solutions before measurement (Hofmann et al, 1984). While at extreme pH levels the net charge of collagen molecule is markedly changed, the measurements are significantly hampered.…”

Section: Resultsmentioning

confidence: 99%

“…A number of hydrodynamic methods and electron microscopy have been used to quantify the flexibility of collagen (Utiyama et al, 1973;Saito et al, 1982;Nestler et al, 1983;Hofmann et al, 1984;Sun et al, 2002). The persistence length of collagen was evaluated as 130-180 nm from several hydrodynamic measurements.…”

Section: Resultsmentioning

confidence: 99%

“…While there has been great progress in characterizing mechanical properties of molecules, many researchers found collagen has some flexibility (Fletcher, 1976;Thomas and Fletcher, 1979;George and Veis, 1991;Shattuck et al, 1994). Due to intrinsic limitations of various methods and assumptions in the models, however, the conflicting results were obtained using different methods to quantify the flexibility of collagen molecules (Utiyama et al, 1973;Saito et al, 1982;Nestler et al, 1983;Hofmann et al, 1984;Sun et al, 2002). The nature of the collagen flexibility remains controversial.…”

Section: Introductionmentioning

confidence: 95%

See 3 more Smart Citations

Stretching type II collagen with optical tweezers

Sun

Luo

Fertala

et al. 2004

Journal of Biomechanics

126

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Section: Resultsmentioning

confidence: 98%

Section: Resultsmentioning

confidence: 99%

Section: Resultsmentioning

confidence: 99%

Section: Introductionmentioning

confidence: 95%

See 2 more Smart Citations

Stretching type II collagen with optical tweezers

Sun

Luo

Fertala

et al. 2004

Journal of Biomechanics

126

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“…On the other hand, a literature analysis shows that great variability in persistence length value can be found considering different kinds of experimental tests. The pioneering work in this analysis is represented by Utiyama and co-workers, 37 who considered sedimentation constants and the intrinsic viscosity of purified collagen molecules and calculated a value for the persistence length close to 130 nm. Saito and co-workers, 38 considering the hydrodynamic properties of collagen, derived the intrinsic viscosity and the sedimentation constant of collagen and, from these values, the persistence length, equal to 160-180 nm.…”

Section: Validation Of the Extended Martini Model: Young's Modulus Anmentioning

confidence: 99%

Coarse-Grained Model of Collagen Molecules Using an Extended MARTINI Force Field

Gautieri

Russo

Vesentini

et al. 2010

J. Chem. Theory Comput.

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Abstract:Collagen is the most abundant protein in the human body, providing mechanical stability, elasticity, and strength to connective tissues such as tendons, ligaments, and bone. Here, we report an extension of the MARTINI coarse-grained force field, originally developed for lipids, proteins, and carbohydrates, used to describe the structural and mechanical properties of collagen molecules. We identify MARTINI force field parameters to describe hydroxyproline amino acid residues and for the triple helical conformational structure found in collagen. We validate the extended MARTINI model through direct molecular dynamics simulations of Young's modulus of a short 8-nm-long collagen-like molecule, resulting in a value of approximately 4 GPa, in good agreement with earlier full atomistic simulations in explicit solvent as well as experimental results. We also apply the extended MARTINI model to simulate a 300-nm-long human type I collagen molecule with the actual amino acid sequence and calculate its persistence length from molecular dynamics trajectories. We obtain a value of 51.5 ( 6.7 nm for the persistence length, which is within the range of earlier experimental results. Our work extends the applicability of molecular models of collagenous tissues by providing a modeling tool to study collagen molecules and fibrils at much larger scales than accessible to existing full atomistic models, while incorporating key chemical and mechanical features and thereby presenting a powerful approach to computational materiomics.

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Elongational flow studies on the molecular properties of collagen and its thermal denaturation

Sasaki

Atkins

Fulton

1991

J of Applied Polymer Sci

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SYNOPSISAn elongational flow method established in polymer physics was applied to study dynamic structure and properties of biopolymers in solution. Type I collagen solutions in the dilute to semidilute region are studied in elongational flow fields, generated in a Taylor four-roll mill, for temperatures from 20°C through the melting temperature to 60°C. A nonlocalized birefringent signal, characteristic of stiff molecules, is observed a t all temperatures. The conformational changes as a function of temperature can be divided into two separate temperature dependent stages. In stage I, at lower temperatures, the collagen molecule behaves as a rigid rod and the birefringent signal A n rises as a function of increasing strain rate i. Throughout this stage the type of molecular interaction in semidilute solution does not change but the rate of interaction is increased by thermal excitation. In stage 11, a characteristic criticality in the A n vs. i plot is observed. For strain rates up to a characteristic value, to, the birefringence remains zero and for i > to whole field bright birefringence is observed. The plateau values of birefringence, An,, at high strain rates in the An vs. i curve decreased with rising temperature in stage 11. This criticality in behavior and the decreasing tendency in An, with temperature are explained by the collagen molecule changing to a hinged-rod conformation. Thus the untwining of collagen as a function of temperature initiates at several places simultaneously, probably at specific amino acid sequences, within the collagen rodlike molecule.

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Flexibility of tropocollagen from sedimentation and viscosity

Cited by 46 publications

References 42 publications

Stretching type II collagen with optical tweezers

Stretching type II collagen with optical tweezers

Coarse-Grained Model of Collagen Molecules Using an Extended MARTINI Force Field

Elongational flow studies on the molecular properties of collagen and its thermal denaturation

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