The removal of disulfide bonds in amylin oligomers leads to the conformational change of the ‘native’ amylin oligomers

Literature Information

Publication Date 2016-04-13
DOI 10.1039/C6CP01196A
Impact Factor 3.676
Authors

Lucia Tudorachi


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Abstract

The α-helical structure of the N-terminus of the ‘native’ amylin Lys1–Cys7 consists of a disulfide bond between Cys2 and Cys7. The ‘native’ amylin oligomers demonstrate polymorphic states. Removal of the disulfide bonds in the ‘native’ amylin oligomers decreases the polymorphism and induces the formation of longer stable cross-β strands in the N-termini.

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Physical Chemistry Chemical Physics

Physical Chemistry Chemical Physics
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Physical Chemistry Chemical Physics (PCCP) is an international journal co-owned by 19 physical chemistry and physics societies from around the world. This journal publishes original, cutting-edge research in physical chemistry, chemical physics and biophysical chemistry. To be suitable for publication in PCCP, articles must include significant innovation and/or insight into physical chemistry; this is the most important criterion that reviewers and Editors will judge against when evaluating submissions. The journal has a broad scope and welcomes contributions spanning experiment, theory, computation and data science. Topical coverage includes spectroscopy, dynamics, kinetics, statistical mechanics, thermodynamics, electrochemistry, catalysis, surface science, quantum mechanics, quantum computing and machine learning. Interdisciplinary research areas such as polymers and soft matter, materials, nanoscience, energy, surfaces/interfaces, and biophysical chemistry are welcomed if they demonstrate significant innovation and/or insight into physical chemistry. Joined experimental/theoretical studies are particularly appreciated when complementary and based on up-to-date approaches.

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