A convenient protein library for spectroscopic calibrations
| Autor: | Joëlle De Meutter, Erik Goormaghtigh |
|---|---|
| Jazyk: | angličtina |
| Rok vydání: | 2020 |
| Předmět: |
Materials science
lcsh:Biotechnology Biophysics Protein Data Bank (RCSB PDB) Analytical chemistry Biochemistry 03 medical and health sciences symbols.namesake 0302 clinical medicine Structural Biology lcsh:TP248.13-248.65 Secondary structure Genetics Calibration Fourier transform infrared spectroscopy Amino acid content Protein secondary structure 030304 developmental biology ComputingMethodologies_COMPUTERGRAPHICS 0303 health sciences Généralités Computer Science Applications Protein spectroscopy FTIR spectroscopy Protein selection 030220 oncology & carcinogenesis Helix symbols Raman spectroscopy Biotechnology DSSP (hydrogen bond estimation algorithm) Research Article |
| Zdroj: | Computational and Structural Biotechnology Journal Computational and Structural Biotechnology Journal, Vol 18, Iss, Pp 1864-1876 (2020) Computational and Structural Biotechnology Journal, 18 |
| ISSN: | 2001-0370 |
| Popis: | 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. SCOPUS: ar.j info:eu-repo/semantics/published |
| Databáze: | OpenAIRE |
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