ReviewMacromolecular rapid communications2019
Experimental Methods for Characterizing the Secondary Structure and Thermal Properties of Silk Proteins.
Review in Macromolecular rapid communications, 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 25 papers.
What it found
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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
The trial behind it
Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.
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Who cites it
25 citing papers in PubMed, 82 citations in OpenAlex.
- Hierarchical picot-fiber hydrogel coating with ultralow friction and high wear resistance.Nature communications · 2026Article
- A cell-laden methacrylated chitosan-based photocrosslinkable hydrogel for bone tissue engineering and its in vitro structural and biological characterization.Scientific reports · 2026Article
- Manipulating the Assembly and Architecture of Fibrillar Silk.Advanced materials (Deerfield Beach, Fla.) · 2025Article
- Biomimetic Silk Nanoparticle Manufacture: Calcium Ion-Mediated Assembly.ACS biomaterials science & engineering · 2025Article
- Silk-engineered bioactive nanoparticles for targeted alleviation of acute inflammatory disease via macrophage reprogramming.Journal of nanobiotechnology · 2025Article
- Exploring the functional properties ofMaterials today. Communications · 2025Article
- Silk fibroin-based inks forBioactive materials · 2024Article
- Silk wastes and autoclaved degumming as an alternative for a sustainable silk process.Scientific reports · 2023Article
- Factors Influencing Properties of Spider Silk Coatings and Their Interactions within a Biological Environment.Journal of functional biomaterials · 2023Review
- Methods for Silk Property Analyses across Structural Hierarchies and Scales.Molecules (Basel, Switzerland) · 2023Review
- Recent Developments of Silk-Based Scaffolds for Tissue Engineering and Regenerative Medicine Applications: A Special Focus on the Advancement of 3D Printing.Biomimetics (Basel, Switzerland) · 2023Review
- Chemical Modification of Silk Fibroin through Serine Amino Acid Residues.Materials (Basel, Switzerland) · 2022Article
- Microbial production of megadalton titin yields fibers with advantageous mechanical properties.Nature communications · 2021Article
- Mesoscale structure development reveals when a silkworm silk is spun.Nature communications · 2021Article
- Correlation between protein secondary structure and mechanical performance for the ultra-tough dragline silk of Darwin's bark spider.Journal of the Royal Society, Interface · 2021Article
- Native-like Flow Properties of an Artificial Spider Silk Dope.ACS biomaterials science & engineering · 2021Article
- Comparative Study of Silk-Based Magnetic Materials: Effect of Magnetic Particle Types on the Protein Structure and Biomaterial Properties.International journal of molecular sciences · 2020Article
- Precision Delivery of Multiscale Payloads to Tissue-Specific Targets in Plants.Advanced science (Weinheim, Baden-Wurttemberg, Germany) · 2020Article
- Unravelling the fibrillation mechanism of ovalbumin in the presence of mercury at its isoelectric pH.RSC advances · 2020Article
- The Mechanical Properties, Secondary Structure, and Osteogenic Activity of Photopolymerized Fibroin.Polymers · 2020Article
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
3 authors at 2 institutions in 1 country.
Funding
Abstract
Silk proteins are biopolymers produced by spinning organisms that have been studied extensively for applications in materials engineering, regenerative medicine, and devices due to their high tensile strength and extensibility. This remarkable combination of mechanical properties arises from their unique semi-crystalline secondary structure and block copolymer features. The secondary structure of silks is highly sensitive to processing, and can be manipulated to achieve a wide array of material profiles. Studying the secondary structure of silks is therefore critical to understanding the relationship between structure and function, the strength and stability of silk-based materials, and the natural fiber synthesis process employed by spinning organisms. However, silks present unique challenges to structural characterization due to high-molecular-weight protein chains, repetitive sequences, and heterogeneity in intra- and interchain domain sizes. Here, experimental techniques used to study the secondary structure of silks, the information attainable from these techniques, and the limitations associated with them are reviewed. Ultimately, the appropriate utilization of a suite of techniques discussed here will enable detailed characterization of silk-based materials, from studying fundamental processing-structure-function relationships to developing commercially useful quality control assessments.
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Registered trials
Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.