Deutsch
 
Hilfe Datenschutzhinweis Impressum
  DetailsucheBrowse

Datensatz

DATENSATZ AKTIONENEXPORT

Freigegeben

Zeitschriftenartikel

Ordering of protein and water molecules at their interfaces with chitin nano-crystals

MPG-Autoren
/persons/resource/persons121957

Valverde Serrano,  Clara
Yael Politi, Biomaterialien, Max Planck Institute of Colloids and Interfaces, Max Planck Society;

/persons/resource/persons187910

Leemreize,  Hanna
Yael Politi, Biomaterialien, Max Planck Institute of Colloids and Interfaces, Max Planck Society;

/persons/resource/persons130281

Bar-On,  Benny
Yael Politi, Biomaterialien, Max Planck Institute of Colloids and Interfaces, Max Planck Society;

/persons/resource/persons121298

Fratzl,  Peter
Peter Fratzl, Biomaterialien, Max Planck Institute of Colloids and Interfaces, Max Planck Society;

/persons/resource/persons121733

Politi,  Yael
Yael Politi, Biomaterialien, Max Planck Institute of Colloids and Interfaces, Max Planck Society;

Externe Ressourcen
Es sind keine externen Ressourcen hinterlegt
Volltexte (beschränkter Zugriff)
Für Ihren IP-Bereich sind aktuell keine Volltexte freigegeben.
Volltexte (frei zugänglich)

2239063.pdf
(Verlagsversion), 2MB

Ergänzendes Material (frei zugänglich)
Es sind keine frei zugänglichen Ergänzenden Materialien verfügbar
Zitation

Valverde Serrano, C., Leemreize, H., Bar-On, B., Barth, F. G., Fratzl, P., Zolotoyabko, E., et al. (2016). Ordering of protein and water molecules at their interfaces with chitin nano-crystals. Journal of Structural Biology, 193(2), 124-131. doi:10.1016/j.jsb.2015.12.004.


Zitierlink: https://hdl.handle.net/11858/00-001M-0000-0029-36C5-5
Zusammenfassung
Synchrotron X-ray diffraction was applied to study the structure of biogenic α-chitin crystals composing the tendon of the spider Cupiennius salei. Measurements were carried out on pristine chitin crystals stabilized by proteins and water, as well as after their deproteinization and dehydration. We found substantial shifts (up to Δq/q = 9% in the wave vector q-space) in the (020) diffraction peak position between intact and purified chitin samples. However, chitin lattice parameters extracted from the set of reflections (hkl), which did not contain the (020)-reflection, showed no systematic variation between the pristine and the processed samples. The observed shifts in the (020) peak position are discussed in terms of the ordering-induced modulation of the protein and water electron density near the surface of the ultra-thin chitin fibrils, due to strong protein/chitin and water/chitin interactions. The extracted modulation periods can be used as a quantitative parameter characterizing the interaction length.