Revealing the Compact Structure of Lactic Acid Bacterial Heteroexopolysaccharides by SAXS and DLS

Research output: Contribution to journalJournal articleResearchpeer-review

Standard

Revealing the Compact Structure of Lactic Acid Bacterial Heteroexopolysaccharides by SAXS and DLS. / Khan, Sanaullah; Birch, Johnny; Harris, Pernille; Van Calsteren, Marie Rose; Ipsen, Richard; Peters, Günther H J; Svensson, Birte; Almdal, Kristoffer.

In: Biomacromolecules, Vol. 18, No. 3, 2017, p. 747-756.

Research output: Contribution to journalJournal articleResearchpeer-review

Harvard

Khan, S, Birch, J, Harris, P, Van Calsteren, MR, Ipsen, R, Peters, GHJ, Svensson, B & Almdal, K 2017, 'Revealing the Compact Structure of Lactic Acid Bacterial Heteroexopolysaccharides by SAXS and DLS', Biomacromolecules, vol. 18, no. 3, pp. 747-756. https://doi.org/10.1021/acs.biomac.6b01597

APA

Khan, S., Birch, J., Harris, P., Van Calsteren, M. R., Ipsen, R., Peters, G. H. J., ... Almdal, K. (2017). Revealing the Compact Structure of Lactic Acid Bacterial Heteroexopolysaccharides by SAXS and DLS. Biomacromolecules, 18(3), 747-756. https://doi.org/10.1021/acs.biomac.6b01597

Vancouver

Khan S, Birch J, Harris P, Van Calsteren MR, Ipsen R, Peters GHJ et al. Revealing the Compact Structure of Lactic Acid Bacterial Heteroexopolysaccharides by SAXS and DLS. Biomacromolecules. 2017;18(3):747-756. https://doi.org/10.1021/acs.biomac.6b01597

Author

Khan, Sanaullah ; Birch, Johnny ; Harris, Pernille ; Van Calsteren, Marie Rose ; Ipsen, Richard ; Peters, Günther H J ; Svensson, Birte ; Almdal, Kristoffer. / Revealing the Compact Structure of Lactic Acid Bacterial Heteroexopolysaccharides by SAXS and DLS. In: Biomacromolecules. 2017 ; Vol. 18, No. 3. pp. 747-756.

Bibtex

@article{11ab262356d24e84986bd359c9ba33be,
title = "Revealing the Compact Structure of Lactic Acid Bacterial Heteroexopolysaccharides by SAXS and DLS",
abstract = "Molecular structures of exopolysaccharides are required to understand their functions and the relationships between the structure and physical and rheological properties. Small-angle X-ray scattering and dynamic light scattering were used in conjunction with molecular modeling to characterize solution structures of three lactic acid bacterial heteroexopolysaccharides (HePS-1, HePS-2, and HePS-3). Values of radius of gyration RG, cross-sectional radius of gyration RXS, approximate length L, and hydrodynamic diameter were not directly proportional to the molar mass and indicated the HePSs adopted a compact coil-like rather than an extended conformation. Constrained molecular modeling of 15000 randomized HePS-1 conformers resulted in five best-fit structures with R factor of 3.9-4.6{\%} revealing random coil-like structure. φ and ψ angle analysis of glycosidic linkages in HePS-1 structures suggests Galf residues significantly influence the conformation. Ab initio scattering modeling of HePS-2 and HePS-3 gave excellent curve fittings with χ2 of 0.43 and 0.34 for best-fit models, respectively, compatible with coil-like conformation. The findings disclose solution behavior of HePS relevant for their interactions with biomacromolecules, for example, milk proteins.",
author = "Sanaullah Khan and Johnny Birch and Pernille Harris and {Van Calsteren}, {Marie Rose} and Richard Ipsen and Peters, {G{\"u}nther H J} and Birte Svensson and Kristoffer Almdal",
year = "2017",
doi = "10.1021/acs.biomac.6b01597",
language = "English",
volume = "18",
pages = "747--756",
journal = "Biomacromolecules",
issn = "1525-7797",
publisher = "American Chemical Society",
number = "3",

}

RIS

TY - JOUR

T1 - Revealing the Compact Structure of Lactic Acid Bacterial Heteroexopolysaccharides by SAXS and DLS

AU - Khan, Sanaullah

AU - Birch, Johnny

AU - Harris, Pernille

AU - Van Calsteren, Marie Rose

AU - Ipsen, Richard

AU - Peters, Günther H J

AU - Svensson, Birte

AU - Almdal, Kristoffer

PY - 2017

Y1 - 2017

N2 - Molecular structures of exopolysaccharides are required to understand their functions and the relationships between the structure and physical and rheological properties. Small-angle X-ray scattering and dynamic light scattering were used in conjunction with molecular modeling to characterize solution structures of three lactic acid bacterial heteroexopolysaccharides (HePS-1, HePS-2, and HePS-3). Values of radius of gyration RG, cross-sectional radius of gyration RXS, approximate length L, and hydrodynamic diameter were not directly proportional to the molar mass and indicated the HePSs adopted a compact coil-like rather than an extended conformation. Constrained molecular modeling of 15000 randomized HePS-1 conformers resulted in five best-fit structures with R factor of 3.9-4.6% revealing random coil-like structure. φ and ψ angle analysis of glycosidic linkages in HePS-1 structures suggests Galf residues significantly influence the conformation. Ab initio scattering modeling of HePS-2 and HePS-3 gave excellent curve fittings with χ2 of 0.43 and 0.34 for best-fit models, respectively, compatible with coil-like conformation. The findings disclose solution behavior of HePS relevant for their interactions with biomacromolecules, for example, milk proteins.

AB - Molecular structures of exopolysaccharides are required to understand their functions and the relationships between the structure and physical and rheological properties. Small-angle X-ray scattering and dynamic light scattering were used in conjunction with molecular modeling to characterize solution structures of three lactic acid bacterial heteroexopolysaccharides (HePS-1, HePS-2, and HePS-3). Values of radius of gyration RG, cross-sectional radius of gyration RXS, approximate length L, and hydrodynamic diameter were not directly proportional to the molar mass and indicated the HePSs adopted a compact coil-like rather than an extended conformation. Constrained molecular modeling of 15000 randomized HePS-1 conformers resulted in five best-fit structures with R factor of 3.9-4.6% revealing random coil-like structure. φ and ψ angle analysis of glycosidic linkages in HePS-1 structures suggests Galf residues significantly influence the conformation. Ab initio scattering modeling of HePS-2 and HePS-3 gave excellent curve fittings with χ2 of 0.43 and 0.34 for best-fit models, respectively, compatible with coil-like conformation. The findings disclose solution behavior of HePS relevant for their interactions with biomacromolecules, for example, milk proteins.

U2 - 10.1021/acs.biomac.6b01597

DO - 10.1021/acs.biomac.6b01597

M3 - Journal article

C2 - 28042938

AN - SCOPUS:85015158330

VL - 18

SP - 747

EP - 756

JO - Biomacromolecules

JF - Biomacromolecules

SN - 1525-7797

IS - 3

ER -

ID: 176654369