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LIBRIS Formathandbok  (Information om MARC21)
FältnamnIndikatorerMetadata
00004772naa a2200457 4500
001oai:DiVA.org:kth-283157
003SwePub
008201006s2020 | |||||||||||000 ||eng|
0247 a https://urn.kb.se/resolve?urn=urn:nbn:se:kth:diva-2831572 URI
0247 a https://doi.org/10.1039/d0sm00916d2 DOI
040 a (SwePub)kth
041 a engb eng
042 9 SwePub
072 7a ref2 swepub-contenttype
072 7a art2 swepub-publicationtype
1001 a Jansen, Karin A.u AMOLF, Biol Soft Matter Grp, Utrecht, Netherlands.;UMC Utrecht, Dept Pathol, NL-3508 GA Utrecht, Netherlands.4 aut
2451 0a Molecular packing structure of fibrin fibers resolved by X-ray scattering and molecular modeling
264 c 2020
264 1b Royal Society of Chemistry (RSC),c 2020
338 a print2 rdacarrier
500 a QC 20201006
520 a Fibrin is the major extracellular component of blood clots and a proteinaceous hydrogel used as a versatile biomaterial. Fibrin forms branched networks built of laterally associated double-stranded protofibrils. This multiscale hierarchical structure is crucial for the extraordinary mechanical resilience of blood clots, yet the structural basis of clot mechanical properties remains largely unclear due, in part, to the unresolved molecular packing of fibrin fibers. Here the packing structure of fibrin fibers is quantitatively assessed by combining Small Angle X-ray Scattering (SAXS) measurements of fibrin reconstituted under a wide range of conditions with computational molecular modeling of fibrin protofibrils. The number, positions, and intensities of the Bragg peaks observed in the SAXS experiments were reproduced computationally based on the all-atom molecular structure of reconstructed fibrin protofibrils. Specifically, the model correctly predicts the intensities of the reflections of the 22.5 nm axial repeat, corresponding to the half-staggered longitudinal arrangement of fibrin molecules. In addition, the SAXS measurements showed that protofibrils within fibrin fibers have a partially ordered lateral arrangement with a characteristic transverse repeat distance of 13 nm, irrespective of the fiber thickness. These findings provide fundamental insights into the molecular structure of fibrin clots that underlies their biological and physical properties.
650 7a NATURVETENSKAPx Kemi0 (SwePub)1042 hsv//swe
650 7a NATURAL SCIENCESx Chemical Sciences0 (SwePub)1042 hsv//eng
7001 a Zhmurov, Artemu KTH,Parallelldatorcentrum, PDC,Sechenov Univ, Moscow 119991, Russia.4 aut0 (Swepub:kth)u17tvbr9
7001 a Vos, Bart E.u AMOLF, Biol Soft Matter Grp, Utrecht, Netherlands.;Univ Munster, Ctr Mol Biol Inflammat, Inst Cell Biol, Munster, Germany.4 aut
7001 a Portale, Giuseppeu Univ Groningen, Zernike Inst Adv Mat, Macromol Chem & New Polymer Mat, Nijenborgh 4, NL-9747 AG Groningen, Netherlands.4 aut
7001 a Hermida-Merino, Danielu ESRF, DUBBLE CRG, Netherlands Org Sci Res NWO, 71 Ave Martyrs, F-38000 Grenoble, France.4 aut
7001 a Litvinov, Rustem, Iu Univ Penn, Perelman Sch Med, Dept Cell & Dev Biol, Philadelphia, PA 19104 USA.;Kazan Fed Univ, Inst Fundamental Med & Biol, 18 Kremlyovskaya St, Kazan 420008, Russia.4 aut
7001 a Tutwiler, Valerieu Univ Penn, Perelman Sch Med, Dept Cell & Dev Biol, Philadelphia, PA 19104 USA.4 aut
7001 a Kurniawan, Nicholas A.u AMOLF, Biol Soft Matter Grp, Utrecht, Netherlands.;Eindhoven Univ Technol, Dept Biomed Engn, Eindhoven, Netherlands.;Eindhoven Univ Technol, Inst Complex Mol Syst, Eindhoven, Netherlands.4 aut
7001 a Bras, Wimu ESRF, DUBBLE CRG, Netherlands Org Sci Res NWO, 71 Ave Martyrs, F-38000 Grenoble, France.;Oak Ridge Natl Lab, Chem Sci Div, One Bethel Valley Rd, Oak Ridge, TN 37831 USA.4 aut
7001 a Weisel, John W.u Univ Penn, Perelman Sch Med, Dept Cell & Dev Biol, Philadelphia, PA 19104 USA.4 aut
7001 a Barsegov, Valeriu Univ Massachusetts, Dept Chem, 1 Univ Ave, Lowell, MA 01854 USA.4 aut
7001 a Koenderink, Gijsje H.u AMOLF, Biol Soft Matter Grp, Utrecht, Netherlands.;Delft Univ Technol, Kavli Inst Nanosci Delft, Dept Bionanosci, Maasweg 9, NL-2629 HZ Delft, Netherlands.4 aut
7102 a AMOLF, Biol Soft Matter Grp, Utrecht, Netherlands.;UMC Utrecht, Dept Pathol, NL-3508 GA Utrecht, Netherlands.b Parallelldatorcentrum, PDC4 org
7730 t Soft Matterd : Royal Society of Chemistry (RSC)g 16:35, s. 8272-8283q 16:35<8272-8283x 1744-683Xx 1744-6848
8564 u https://doi.org/10.1039/d0sm00916dy Fulltext
8564 u https://pubs.rsc.org/en/content/articlepdf/2020/sm/d0sm00916d
8564 8u https://urn.kb.se/resolve?urn=urn:nbn:se:kth:diva-283157
8564 8u https://doi.org/10.1039/d0sm00916d

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