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

Clara Valverde Serrano, Hanna Leemreize, Benny Bar-On, Friedrich G. Barth, Peter Fratzl, Emil Zolotoyabko, Yael Politi

Research output: Contribution to journalArticlepeer-review

19 Scopus citations


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 in q-space) in the (0 2 0) 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 (0 2 0)-reflection, showed no systematic variation between the pristine and the processed samples. The observed shifts in the (0 2 0) 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.

Original languageEnglish
Pages (from-to)124-131
Number of pages8
JournalJournal of Structural Biology
Issue number2
StatePublished - 1 Feb 2016


  • Chitin
  • Chitin/protein interaction
  • Chitin/water interaction
  • X-ray diffraction

ASJC Scopus subject areas

  • Structural Biology


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