Self-assembled semi-crystallinity at parallel β -sheet nanocrystal interfaces in clustered MaSp1 (spider silk) proteins
| Autor: | Parvez Alam, Erly Sintya |
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| Rok vydání: | 2016 |
| Předmět: |
Models
Molecular Materials science Molecular Sequence Data Silk Beta sheet Bioengineering Nanotechnology 02 engineering and technology 010402 general chemistry 01 natural sciences Protein Structure Secondary Biomaterials Molecular dynamics Crystallinity Elastic Modulus Animals Spider silk Amino Acid Sequence Soft matter Spiders 021001 nanoscience & nanotechnology 0104 chemical sciences Amorphous solid SILK Nanocrystal Mechanics of Materials Chemical physics Nanoparticles Thermodynamics Crystallization 0210 nano-technology |
| Zdroj: | Materials Science and Engineering: C. 58:366-371 |
| ISSN: | 0928-4931 |
| DOI: | 10.1016/j.msec.2015.08.038 |
| Popis: | In this communication, we use molecular dynamics methods to model the self-assembly of semi-crystalline domains at β-sheet nanocrystal interfaces in clusters of spider silk (MaSp1) proteins. Our research elucidates that the energetics at interfaces between crystalline and amorphous domains control effectively, the extent to which semi-crystalline domains can form at interfaces. Stability at nanocrystal interfaces is not linearly related to the internal (bulk) stability of the β-sheet nanocrystal. Rather, interfacial stability is found to be highly sensitive to the number of alanine repeat units that make up each sheet. Intriguingly, the most stable interface for the development of semi-crystallinity is built up of polyalanine β-sheets of a length similar to that which is spun naturally in spider dragline silk. |
| Databáze: | OpenAIRE |
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