Analysis of the primary structure of collagen for the origins of molecular packing

Hulmes, David J.S.; Miller, A.; Parry, David; Piez, Karl A.; Woodhead-Galloway, John

doi:10.1016/0022-2836(73)90275-1

Cited by 406 publications

(200 citation statements)

References 20 publications

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“…It is likely that specific hydrophobic and/or electrostatic interactions are required for the specificity to determine such regular structures. 51 The incorporation of a hydrophobic sequence from Type IV collagen into a peptide resulted in temperatureinduced self-association to form a fiber-like structure with supercoiling and branching which resembles the networks of Type IV collagen in basement membranes (Figure 5c) (Kar et al, unpublished observations). Recently, the introduction of positively charged residues at the N-terminus and negatively charged residues at the C-terminus of a triple-helical peptide was shown to lead to formation of banded periodic fibrils which resemble collagen fibrils.…”

Section: Self-association Of Peptides As Models For Higher Order Strumentioning

confidence: 98%

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

et al. 2008

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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

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Section: Self-association Of Peptides As Models For Higher Order Strumentioning

confidence: 98%

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

et al. 2008

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“…The migration positions of molecular mass markers and the oligomeric forms of MBP-A are shown on the left and right, respectively. only three differences between the MBPs, in which Lys 27 , His 30 , and Ala 33 in MBP-C correspond to Arg…”

Section: Contribution Of Multiple Domains In Mbp-a To Highermentioning

confidence: 99%

Molecular Determinants of Oligomer Formation and Complement Fixation in Mannose-binding Proteins

Wallis

Drickamer²

1999

Journal of Biological Chemistry

106

138

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“…lecular interactions between the three chains and for interactions with other molecules. The highly conserved charged residues of collagen have been implicated in electrostatic interactions stabilizing the triple helix [9,10], the molecular association to form fibrils [11,12] and association of collagen with other molecules [13].…”

Section: Introductionmentioning

confidence: 99%

Acid destabilization of a triple‐helical peptide model of the macrophage scavenger receptor

1995

FEBS Letters

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Electrostatic interactions were studied in a triple-helical peptide, (POG)3PKGQKGEKG(POG)4, which contains a lysine-rich 9 residue sequence from the collagen-like domain of the macrophage scavenger receptor (MSR). This peptide adopts a stable triple-helical conformation only when the pH is higher than 4.5, corresponding to ionization of the Glu side chain. Modeling shows Glu forms ion pairs with one of the Lys residues, stabilizing the structure. Previously studied collagen-like peptides show relatively small contributions of electrostatic interactions to stability. The large magnitude of the pH mediated structural changes seen for this peptide suggests that specific placement of charged residues in the triple-helix conformation can generate strong electrostatic interactions.

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Analysis of the primary structure of collagen for the origins of molecular packing

Cited by 406 publications

References 20 publications

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

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

Molecular Determinants of Oligomer Formation and Complement Fixation in Mannose-binding Proteins

Acid destabilization of a triple‐helical peptide model of the macrophage scavenger receptor

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