ReviewBiophysical reviews2017
Going deep into protein secondary structure with synchrotron radiation circular dichroism spectroscopy.
Review in Biophysical reviews, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 11 papers.
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Who cites it
11 citing papers in PubMed.
- UV Circular Dichroism of Molecular Films on Plasmonic Nanostructures: A Comparative Case Study with On-Resonant Aluminum and Off-Resonant Silver Nanoparticles.ACS photonics · 2025Article
- Bovine Serum Albumin Bends Over Backward to Interact with Aged Plastics: A Model for Understanding Protein Attachment to Plastic Debris.Environmental science & technology · 2024Article
- Kunitz-Type Peptides from Sea Anemones Protect Neuronal Cells against Parkinson's Disease Inductors via Inhibition of ROS Production and ATP-Induced P2X7 Receptor Activation.International journal of molecular sciences · 2022Article
- Effect of setting data collection parameters on the reliability of a circular dichroism spectrum.European biophysics journal : EBJ · 2021Article
- Protein nanoparticles in drug delivery: animal protein, plant proteins and protein cages, albumin nanoparticles.Journal of nanobiotechnology · 2021Review
- Conformational Change and Activity Enhancement of Rabbit Muscle Lactate Dehydrogenase Induced by Polyethyleneimine.ACS omega · 2021Article
- Gold Nanoparticles Functionalized with Angiogenin for Wound Care Application.Nanomaterials (Basel, Switzerland) · 2021Article
- Production and immunogenicity of Fubc subunit protein redesigned from DENV envelope protein.Applied microbiology and biotechnology · 2020Article
- The Secondary Structure of a Major Wine Protein is Modified upon Interaction with Polyphenols.Molecules (Basel, Switzerland) · 2020Article
- Structural diversity in the Mycobacteria DUF3349 superfamily.Protein science : a publication of the Protein Society · 2020Article
- Sample Volume Reduction Using the Schwarzschild Objective for a Circular Dichroism Spectrophotometer and an Application to the Structural Analysis of Lysine-36 Trimethylated Histone H3 Protein.Molecules (Basel, Switzerland) · 2018Article
Corrections and comments
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Authors and funding
3 authors.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Circular dichroism (CD) spectroscopy is a fast, powerful, well-established, and widely used analytical technique in the biophysical and structural biology community to study protein secondary structure and to track changes in protein conformation in different environments. The use of the intense light of a synchrotron beam as the light source for collecting CD measurements has emerged as an enhanced method, known as synchrotron radiation circular dichroism (SRCD) spectroscopy, that has several advantages over the conventional CD method, including a significant spectral range extension for data collection, deeper access to the lower limit (cut-off) of conventional CD spectroscopy, an improved signal-to-noise ratio to increase accuracy in the measurements, and the possibility to collect measurements in highly absorbing solutions. In this review, we discuss different applications of the SRCD technique by researchers from Latin America. In this context, we specifically look at the use of this method for examining the secondary structure and conformational behavior of proteins belonging to the four main classes of the hierarchical protein domain classification CATH (Class, Architecture, Topology, Homology) database, focusing on the advantages and improvements associated with SRCD spectroscopy in terms of characterizing proteins composed of different structural elements.
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Registered trials
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