ArticleChemical science2017
Quantitative first principles calculations of protein circular dichroism in the near-ultraviolet.
Article in Chemical science, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 9 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
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Who cites it
9 citing papers in PubMed.
- Improved albumin binding properties of Isoguvacine upon esterification as characterized by biophysical and computational tools.Scientific reports · 2025Article
- The Structural Fingerprint of Therapeutic Monoclonal Antibodies Determined Using a Combination of Near-UV Circular Dichroism and Statistical Approach for Comparative Analysis.Analytical chemistry · 2025Article
- Exo-chirality of the α-helix.Nature communications · 2024Article
- Architectural digest: Thermodynamic stability and domain structure of a consensus monomeric globin.Biophysical journal · 2023Article
- A look at the face of the molten globule: Structural model of the Helicobacter pylori apoflavodoxin ensemble at acidic pH.Protein science : a publication of the Protein Society · 2022Article
- Structural and functional analysis of SNP rs76740365 G>A in exon-3 of the alpha A-crystallin gene in lens epithelial cells.Molecular vision · 2022Article
- Near-Ultraviolet Circular Dichroism and Two-Dimensional Spectroscopy of Polypeptides.Molecules (Basel, Switzerland) · 2021Article
- Molecular Changes in Dengue Envelope Protein Domain III upon Interaction with Glycosaminoglycans.Pathogens (Basel, Switzerland) · 2020Article
- Computed optical spectra of SARS-CoV-2 proteins.Chemical physics letters · 2020Article
Corrections and comments
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Authors and funding
2 authors.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Vibrational structure in the near-UV circular dichroism (CD) spectra of proteins is an important source of information on protein conformation and can be exploited to study structure and folding. A fully quantitative theory of the relationship between protein conformation and optical spectroscopy would facilitate deeper interpretation of and insight into biophysical and simulation studies of protein dynamics and folding. We have developed new models of the aromatic side chain chromophores toluene,
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Registered trials
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