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Sigrid Bernstorff

Researcher at Elettra Sincrotrone Trieste

Publications -  354
Citations -  7068

Sigrid Bernstorff is an academic researcher from Elettra Sincrotrone Trieste. The author has contributed to research in topics: Grazing-incidence small-angle scattering & Amorphous solid. The author has an hindex of 35, co-authored 344 publications receiving 6478 citations. Previous affiliations of Sigrid Bernstorff include Austrian Academy of Sciences & Marche Polytechnic University.

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Fibrillar structure and mechanical properties of collagen

TL;DR: It was observed that the strain within collagen fibrils is always considerably smaller than in the whole tendon, which points toward the existence of additional gliding processes occurring at the interfibrillar level.
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Viscoelastic properties of collagen: synchrotron radiation investigations and structural model

TL;DR: In this paper, a simple structural model was proposed to describe the tendon at a hierarchical level, where fibrils and interfibrillar matrix act as coupled viscoelastic systems, and all qualitative features of the strain-rate dependence of both normal and crosslink-deficient collagen can be reproduced within this model.
Journal Article

Viscoelastic properties of collagen: synchrotron radiation investigations and structural model

TL;DR: A simple structural model is proposed, which describes the tendon at a hierarchical level, where fibrils and interfibrillar matrix act as coupled viscoelastic systems, and all qualitative features of the strain-rate dependence of both normal and cross-link-deficient collagen can be reproduced within this model.
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First performance assessment of the small-angle X-ray scattering beamline at ELETTRA.

TL;DR: The double-focusing high-flux wiggler beamline dedicated to small-angle X-ray scattering (SAXS) and wide-angle OXS at ELETTRA has gone into user operation recently.
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The Importance of Protein-Protein Interactions on the pH-Induced Conformational Changes of Bovine Serum Albumin: A Small-Angle X-Ray Scattering Study

TL;DR: It is confirmed that the protein concentration plays an important role on the pH-unfolded BSA state, due to a delicate compromise between interaction forces and crowding effects.