ArticleComputational and structural biotechnology journal2020
A convenient protein library for spectroscopic calibrations.
Article in Computational and structural biotechnology journal, 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 4 papers.
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4 citing papers in PubMed.
- Protein Microarrays for High Throughput Hydrogen/Deuterium Exchange Monitored by FTIR Imaging.International journal of molecular sciences · 2024Article
- Determination of Secondary Structure of Proteins by Nanoinfrared Spectroscopy.Analytical chemistry · 2023Article
- Evaluation of protein secondary structure from FTIR spectra improved after partial deuteration.European biophysics journal : EBJ · 2021Article
- Amino acid side chain contribution to protein FTIR spectra: impact on secondary structure evaluation.European biophysics journal : EBJ · 2021Article
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2 authors.
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Abstract
While several Raman, CD or FTIR spectral libraries are available for well-characterized proteins of known structure, proteins themselves are usually very difficult to acquire, preventing a convenient calibration of new instruments and new recording methods. The problem is particularly critical in the field of FTIR spectroscopy where numerous new methods are becoming available on the market. The present papers reports the construction of a protein library (cSP92) including commercially available products, that are well characterized experimentally for their purity and solubility in conditions compatible with the recording of FTIR spectra and whose high-resolution structure is available. Overall, 92 proteins were selected. These proteins cover well the CATH space at the level of classes and architectures. In terms of secondary structure content, an analysis of their high-resolution structure by DSSP shows that the mean content in the different secondary structures present in cSP92 is very similar to the mean content found in the PDB. The 92-protein set is analyzed in details for the distribution of helix length, number of strands in β- sheets, length of β-strands and amino acid content, all features that may be important for the interpretation of FTIR spectra.
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