Methionine in a protein hydrophobic core drives tight interactions required for assembly of spider silk
- Location
-
Deutsche Nationalbibliothek Frankfurt am Main
- Extent
-
Online-Ressource
- Language
-
Englisch
- Bibliographic citation
-
In: Nature Communications, 10.2019, Nr. 1, Art. 4378, doi:10.1038/s41467-019-12365-5
- Classification
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Biowissenschaften, Biologie
- Event
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Veröffentlichung
- (where)
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Frankfurt am Main
- (who)
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Universitätsbibliothek Johann Christian Senckenberg
- (when)
-
2019
- Creator
- URN
-
urn:nbn:de:hebis:30:3-512788
- Rights
-
Der Zugriff auf das Objekt ist unbeschränkt möglich.
- Last update
-
15.08.2025, 7:35 AM CEST
Data provider
This object is provided by:
Deutsche Nationalbibliothek. If you have any questions about the object, please contact the data provider.
Deutsche Nationalbibliothek. If you have any questions about the object, please contact the data provider.
Associated
- Heiby, Julia C.
- Goretzki, Benedikt
- Johnson, Christopher M.
- Hellmich, Ute
- Neuweiler, Hannes
- Universitätsbibliothek Johann Christian Senckenberg
Time of origin
- 2019
Other Objects (12)
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Recombinant spider silk: promises and bottlenecks
Multiscale modeling of spider dragline silk
Protein secondary structure in spider silk nanofibrils
Stress-induced long-range ordering in spider silk
Untangling spider silk evolution with spidroin terminal domains
Novel Processing Technologies for Recombinant Spider Silk Proteins
Methionine in a protein hydrophobic core drives tight interactions required for assembly of spider silk
Expression of spider silk and spider silk like proteins in potato and tobacco
Water-based spider silk films
Spider Silk‐Inspired Artificial Fibers
Biofabrication using recombinant spider silk proteins
Spider silk foam coating of fabric
Recombinant spider silk: promises and bottlenecks
Multiscale modeling of spider dragline silk
Protein secondary structure in spider silk nanofibrils
Stress-induced long-range ordering in spider silk
Untangling spider silk evolution with spidroin terminal domains
Novel Processing Technologies for Recombinant Spider Silk Proteins
Methionine in a protein hydrophobic core drives tight interactions required for assembly of spider silk
Expression of spider silk and spider silk like proteins in potato and tobacco
Water-based spider silk films
Spider Silk‐Inspired Artificial Fibers
Biofabrication using recombinant spider silk proteins
Spider silk foam coating of fabric
Recombinant spider silk: promises and bottlenecks
Multiscale modeling of spider dragline silk
Protein secondary structure in spider silk nanofibrils
Stress-induced long-range ordering in spider silk
Untangling spider silk evolution with spidroin terminal domains