ArticleBiomacromolecules2022
In Situ Identification of Secondary Structures in Unpurified
Article in Biomacromolecules, 2022. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 8 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
8 citing papers in PubMed, 18 citations in OpenAlex.
- The Origin of the Frequency-Dependence of OH Stretch Vibrational Lifetimes in Liquid Water.The journal of physical chemistry letters · 2026Article
- Role of the Surface in Conformational Changes in Lysozymes: Effect of a Gold Surface and a Lipid Membrane.International journal of molecular sciences · 2025Article
- Effect of Silk Fibroin on the Mechanical and Transport Properties of Agarose Hydrogels.Gels (Basel, Switzerland) · 2024Article
- Structural adaptability and surface activity of peptides derived from tardigrade proteins.Protein science : a publication of the Protein Society · 2024Article
- Molecular organization of fibroin heavy chain and mechanism of fibre formation in Bombyx mori.Communications biology · 2024Article
- Labile assembly of a tardigrade protein induces biostasis.Protein science : a publication of the Protein Society · 2024Article
- Flow-Induced Protein Chain Deformation, Segmental Orientation, and Phase Separation in Native Silk Feedstock.Biomacromolecules · 2023Article
- Broadband Multidimensional Spectroscopy Identifies the Amide II Vibrations in Silkworm Films.Molecules (Basel, Switzerland) · 2022Article
Corrections and comments
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Authors and funding
8 authors at 3 institutions in 3 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
The mechanical properties of biomaterials are dictated by the interactions and conformations of their building blocks, typically proteins. Although the macroscopic behavior of biomaterials is widely studied, our understanding of the underlying molecular properties is generally limited. Among the noninvasive and label-free methods to investigate molecular structures, infrared spectroscopy is one of the most commonly used tools because the absorption bands of amide groups strongly depend on protein secondary structure. However, spectral congestion usually complicates the analysis of the amide spectrum. Here, we apply polarized two-dimensional (2D) infrared spectroscopy (IR) to directly identify the protein secondary structures in native silk films cast from
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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.