Single‐chain triple helical structure

Ramachandran, G.; Doyle, Barbara; Bloot, E. R.

doi:10.1002/bip.1968.360061213

Cited by 44 publications

(32 citation statements)

References 7 publications

Supporting

Mentioning

Contrasting

Order By: Relevance

“…In bone, collagen type I is the most abundant protein and commonly used for reconstructing palaeodiet (Ambrose 1990). Collagen type I is a triple helix (Ramachandran et al 1968;Bornstein and Traub 1979;Piez 1976) and contains two alpha 1 and one alpha 2 helices (Piez 1984). The alpha 1 and alpha 2 chains differ only slightly and consist mainly of triplets with the order Gly-X-Y (where X stands for proline and Y for hydroxyproline); all other amino acids are less well represented (Piez 1976).…”

Section: Introductionmentioning

confidence: 99%

Establishing collagen quality criteria for sulphur isotope analysis of archaeological bone collagen

Nehlich

Richards

2009

Archaeol Anthropol Sci

229

192

View full text Add to dashboard Cite

Sulphur isotope measurements of bone collagen from archaeological sites are beginning to be applied more often, yet there are no clear criteria to assess the quality of the collagen and therefore the validity of the sulphur isotope values. We provide elemental data from different methods (DNA sequences, amino acid sequences and mass spectrometric measurements) which are used to establish a reliable system of quality criteria for sulphur isotope analyses of bone collagen. The difference in the amount of sulphur from fish and mammalian collagen type I led to the suggestion to use different criteria to assess the in vivo character of the collagen between these two categories. For establishing quality ranges, the bone collagen of 140 modern animals were analysed. The amount of sulphur in fish and mammalian bone collagen is 0.63±0.08% and 0.28 ±0.07%, respectively. Based on these results we define for mammalian bone collagen an atomic C:S ratio of 600±300 and an atomic N:S ratio of 200±100, and for fish bone an atomic C:S ratio of 175±50 and an atomic N:S ratio of 60± 20. These quality criteria were then applied to 305 specimens from different archaeological contexts.

show abstract

Section: Introductionmentioning

confidence: 99%

Establishing collagen quality criteria for sulphur isotope analysis of archaeological bone collagen

Nehlich

Richards

2009

Archaeol Anthropol Sci

229

192

View full text Add to dashboard Cite

show abstract

“…Elkan Blout's laboratory became one center of this activity. [7][8][9][10][11] His background in chemistry facilitated synthesis of oligopeptides and polytripeptides, while his pioneering research in spectroscopy provided the impetus to apply optical rotary dispersion, circular dichroism spectroscopy, and infrared spectroscopy to establish relationships between amino acid sequence and triple-helix stability, and conformation. Stabilizing solvents such as hexafluoroisopropanol and trifluoroethanol were used to induce helix formation, and comparisons were made of solid state and solution.…”

Section: Introductionmentioning

confidence: 99%

Triple‐helical peptides: An approach to collagen conformation, stability, and self‐association

et al. 2008

View full text Add to dashboard Cite

Peptides have been an integral part of the collagen triple‐helix structure story, and have continued to serve as useful models for biophysical studies and for establishing biologically important sequence‐structure‐function relationships. High resolution structures of triple‐helical peptides have confirmed the basic Ramachandran triple‐helix model and provided new insights into the hydration, hydrogen bonding, and sequence dependent helical parameters in collagen. The dependence of collagen triple‐helix stability on the residues in its (Gly‐X‐Y)n repeating sequence has been investigated by measuring melting temperatures of host‐guest peptides and an on‐line collagen stability calculator is now available. Although the presence of Gly as every third residue is essential for an undistorted structure, interruptions in the repeating (Gly‐X‐Y)n amino acid sequence pattern are found in the triple‐helical domains of all nonfibrillar collagens, and are likely to play a role in collagen binding and degradation. Peptide models indicate that small interruptions can be incorporated into a rod‐like triple‐helix with a highly localized effect, which perturbs hydrogen bonds and places the standard triple‐helices on both ends out of register. In contrast to natural interruptions, missense mutations which replace one Gly in a triple‐helix domain by a larger residue have pathological consequences, and studies on peptides containing such Gly substitutions clarify their effect on conformation, stability, and folding. Recent studies suggest peptides may also be useful in defining the basic principles of collagen self‐association to the supramolecular structures found in tissues. © 2008 Wiley Periodicals, Inc. Biopolymers 89: 345–353, 2008.This article was originally published online as an accepted preprint. The “Published Online” date corresponds to the preprint version. You can request a copy of the preprint by emailing the Biopolymers editorial office at biopolymers@wiley.com

show abstract

“…1). The small positive peak at ϳ225 nm and the deep negative peak at ϳ197 nm are typical of that of a collagen triple helix (3,19). The foldon domain has contributions to the peak at 225 nm ( Fig.…”

Section: Resultsmentioning

confidence: 92%

“…When modeled in short synthetic peptides, the 15 amino acid residues (residue 886 -900) immediately N terminus to G901S fail to refold without the addition of a renucleation domain GPO(GAO) 3 (25,26). The triple helix formation in the N-terminal region of G901S and G913S can start from the repeating GPP sequence (diagram 1), which shares the same two major features with GPO(GAO) 3 : a high triple helix propensity and high imino acid content (25). NMR studies reveal an ordered structure around the Gly-901 substitution site when attached to the renucleation sequence GPO(GAO) 3 , although with a degree of helix untwisting and alteration of the H-bond network.…”

Section: Discussionmentioning

confidence: 99%

“…The collagen triple helix consists of three polypeptide chains each in extended polyproline II conformation and with the characteristic (Gly-X-Y) n repeating amino acid sequence (1)(2)(3). The Gly at every third position is necessitated by the close packing of the helix; while the X and Y residues (where X and Y can be any amino acids) contribute directlytothestabilityofthetriplehelixandconferthesequencedependent properties of collagen (4).…”

mentioning

confidence: 99%

See 1 more Smart Citation

Recombinant Collagen Studies Link the Severe Conformational Changes Induced by Osteogenesis Imperfecta Mutations to the Disruption of a Set of Interchain Salt Bridges

Nowak

Kirchner

et al. 2008

Journal of Biological Chemistry

View full text Add to dashboard Cite

The clinical severity of Osteogenesis Imperfecta (OI), also known as the brittle bone disease, relates to the extent of conformational changes in the collagen triple helix induced by Gly substitution mutations. The lingering question is why Gly substitutions at different locations of collagen cause different disruptions of the triple helix. Here, we describe markedly different conformational changes of the triple helix induced by two Gly substitution mutations placed only 12 residues apart. The effects of the Gly substitutions were characterized using a recombinant collagen fragment modeling the 63-residue segment of the ␣1 chain of type I collagen containing no Hyp (residues 877-939) obtained from Escherichia coli. Two Gly 3 Ser substitutions at Gly-901 and Gly-913 associated with, respectively, mild and severe OI variants were introduced by site-directed mutagenesis. Biophysical characterization and limited protease digestion experiments revealed that while the substitution at Gly-901 causes relatively minor destabilization of the triple helix, the substitution at Gly-913 induces large scale unfolding of an unstable region C-terminal to the mutation site. This extensive unfolding is caused by the intrinsic low stability of the C-terminal region of the helix and the mutation induced disruption of a set of salt bridges, which functions to lock this unstable region into the triple helical conformation. The extensive conformational changes associated with the loss of the salt bridges highlight the long range impact of the local interactions of triple helix and suggest a new mechanism by which OI mutations cause severe conformational damages in collagen.Considerable effort has been made to elucidate the mechanisms by which Gly substitution mutations of the collagen triple helix cause Osteogenesis Imperfecta (OI), 2 also known as brittle bone disease. The collagen triple helix consists of three polypeptide chains each in extended polyproline II conformation and with the characteristic (Gly-X-Y) n repeating amino acid sequence (1-3). The Gly at every third position is necessitated by the close packing of the helix; while the X and Y residues (where X and Y can be any amino acids) contribute directlytothestabilityofthetriplehelixandconferthesequencedependent properties of collagen (4). Missense mutations that replace the obligatory Gly by another amino acid residue in type I collagen, the major component of bones, are the most common cause of OI (5, 6). The triple helix domain of type I collagen is a heterotrimer composed of two ␣1 chains and one ␣2 chain each with more than 1000 amino acids in an uninterrupted (Gly-X-Y) n sequence (7). Nearly 800 Gly replacing mutations from both ␣1 and ␣2 chains have been linked to OI, yet, depending on the location and the identity of the Gly substitution, the clinical severity of OI varies from mild increase of bone fragility to the most severe type characterized by death at the prenatal stage (the Type II OI) (6). It remains unclear what molecular properties are related to the se...

show abstract

Single‐chain triple helical structure

Cited by 44 publications

References 7 publications

Establishing collagen quality criteria for sulphur isotope analysis of archaeological bone collagen

Establishing collagen quality criteria for sulphur isotope analysis of archaeological bone collagen

Triple‐helical peptides: An approach to collagen conformation, stability, and self‐association

Recombinant Collagen Studies Link the Severe Conformational Changes Induced by Osteogenesis Imperfecta Mutations to the Disruption of a Set of Interchain Salt Bridges

Contact Info

Product

Resources

About