Stability and mobility of the collagen structure

Privalov, Peter L.; Tiktopulo, E. I.; Tischenko, V. M.

doi:10.1016/0022-2836(79)90240-7

Cited by 102 publications

(48 citation statements)

References 30 publications

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“…In our structure the helical water molecules are situated at such a distance from the axis (see table 1). The data on IR dichroism, NMR and thermodynamic measurements are also compatible with the water-carbonyl structure of collagen (reviews [8,17,[21][22][23]). …”

Section: Discussionmentioning

confidence: 55%

A novel structural model for collagen: Water—carbonyl helix

Lim

1981

FEBS Letters

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Section: Discussionmentioning

confidence: 55%

A novel structural model for collagen: Water—carbonyl helix

Lim

1981

FEBS Letters

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“…(i) Local unfolding is opening of at least one GXY triplet i, which breaks interchain hydrogen bonds and exposes buried Gly-NH to water. It affects adjacent triplets j whose contribution is weighted by expϪ(i Ϫ j) 2 /n 2 ], where n characterizes the extent of the perturbation. (ii) The sequence dependence of the activation energies is the same in collagen and host-guest peptides.…”

Section: Model Analysismentioning

confidence: 99%

“…Because Gly-NH groups in the GXY triplets are buried in the core of the helix, their H-D exchange rate is limited. Local triplet helix unfolding is required to expose them to surrounding water and OD Ϫ (2,38,40). Different rates of local unfolding within different regions of the helix may contribute to the observed wide range of slow exchange rates (from minutes to days).…”

Section: Analysis Of Local Stability By H-d Exchange-mentioning

confidence: 99%

“…Based on the (Gly-Xaa-Yaa) 338 triplet repeat within each chain (1), the triple helix is commonly viewed as a single domain (Xaa and Yaa stand for variable residues). However, this picture may not accurately represent variations in the stability of different regions within the triple helix that fold and unfold cooperatively (2)(3)(4). The triple helix is only metastable or marginally stable at physiological temperature (3,(5)(6)(7)(8).…”

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confidence: 99%

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Structural Heterogeneity of Type I Collagen Triple Helix and Its Role in Osteogenesis Imperfecta

Makareeva

Mertz

Kuznetsova

et al. 2008

Journal of Biological Chemistry

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We investigated regions of different helical stability within human type I collagen and discussed their role in intermolecular interactions and osteogenesis imperfecta (OI). By differential scanning calorimetry and circular dichroism, we measured and mapped changes in the collagen melting temperature (⌬T m ) for 41 different Gly substitutions from 47 OI patients. In contrast to peptides, we found no correlations of ⌬T m with the identity of the substituting residue. Instead, we observed regular variations in ⌬T m with the substitution location in different triple helix regions. To relate the ⌬T m map to peptide-based stability predictions, we extracted the activation energy of local helix unfolding (⌬G ‡ ) from the reported peptide data. We constructed the ⌬G ‡ map and tested it by measuring the H-D exchange rate for glycine NH residues involved in interchain hydrogen bonds. Based on the ⌬T m and ⌬G ‡ maps, we delineated regional variations in the collagen triple helix stability. Two large, flexible regions deduced from the ⌬T m map aligned with the regions important for collagen fibril assembly and ligand binding. One of these regions also aligned with a lethal region for Gly substitutions in the ␣1(I) chain.The mature type I collagen molecule is a 300-nm-long triple helix formed by two ␣1(I) and one ␣2(I) chains, which is flanked by short terminal peptides. Based on the (Gly-Xaa-Yaa) 338 triplet repeat within each chain (1), the triple helix is commonly viewed as a single domain (Xaa and Yaa stand for variable residues). However, this picture may not accurately represent variations in the stability of different regions within the triple helix that fold and unfold cooperatively (2-4). The triple helix is only metastable or marginally stable at physiological temperature (3, 5-8). Its local structure appears to be highly dynamic and intimately related to local stability. The more labile regions may exist in a loose conformation, constantly undergoing unfolding/refolding transitions while more stable "clamp" regions prevent unfolding of the whole molecule (3, 9 -12). Such structural and dynamic heterogeneity is believed to play an important role in self-assembly (9, 13) and function (3) of collagen fibers.Significant progress in understanding regional variations in the triple helix stability in different collagens has been reported in recent years. For example, some flexible sites were localized by observing triple helix bending in electron microscopy (14) and/or increased susceptibility to proteolytic cleavage (9, 15). Genetically generated reshuffling of different triple helix regions was shown to have a significant effect on the overall stability of the molecule (11, 16). Relative local stability maps were proposed based on scoring different sequences (17) or on the denaturation temperature (T m ) measured for triple-helical host-guest peptides (18).The existence of looser, less stable, and tighter, more stable structural regions within the triple helix is now commonly accepted. However, knowledge of their loca...

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“…When compared with their mesophilic counterparts these enzymes display a higher specific activity and a strongly reduced thermostability. This is probably due to an increased conformational flexibility which is now regarded as the main adaptive feature to low temperatures (3)(4)(5). It is thought that the higher flexibility of psychrophilic enzymes allows them to better accommodate their substrates and to undergo the fast conformational changes required for catalysis at low energy cost (4).…”

mentioning

confidence: 99%

Structural, Kinetic, and Calorimetric Characterization of the Cold-active Phosphoglycerate Kinase from the AntarcticPseudomonas sp. TACII18

Bentahir

Feller

Aittaleb

et al. 2000

Journal of Biological Chemistry

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The gene encoding the phosphoglycerate kinase (PGK) from the Antarctic Pseudomonas sp. TACII18 has been cloned and found to be inserted between the genes encoding for glyceraldhyde-3-phosphate dehydrogenase and fructose aldolase. The His-tagged and the native recombinant PGK from the psychrophilic Pseudomonas were expressed in Escherichia coli. The wild-type and the native recombinant enzymes displayed identical properties, such as a decreased thermostability and a 2-fold higher catalytic efficiency at 25°C when compared with the mesophilic PGK from yeast. These properties, which reflect typical features of cold-adapted enzymes, were strongly altered in the His-tagged recombinant PGK. The structural model of the psychrophilic PGK indicated that a key determinant of its low stability is the reduced number of salt bridges, surface charges, and aromatic interactions when compared with mesophilic and thermophilic PGK. Differential scanning calorimetry of the psychrophilic PGK revealed unusual variations in its conformational stability for the free and substrate-bound forms. In the free form, a heatlabile and a thermostable domain unfold independently. It is proposed that the heat-labile domain acts as a destabilizing domain, providing the required flexibility around the active site for catalysis at low temperatures.

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Stability and mobility of the collagen structure

Cited by 102 publications

References 30 publications

A novel structural model for collagen: Water—carbonyl helix

A novel structural model for collagen: Water—carbonyl helix

Structural Heterogeneity of Type I Collagen Triple Helix and Its Role in Osteogenesis Imperfecta

Structural, Kinetic, and Calorimetric Characterization of the Cold-active Phosphoglycerate Kinase from the AntarcticPseudomonas sp. TACII18

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