A convenient protein library for spectroscopic calibrations
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 th...
| Main Authors: | , |
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| Format: | Article |
| Language: | English |
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Elsevier
2020-01-01
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| Series: | Computational and Structural Biotechnology Journal |
| Subjects: | |
| Online Access: | http://www.sciencedirect.com/science/article/pii/S2001037020303330 |
| _version_ | 1818325404343074816 |
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| author | Joëlle De Meutter Erik Goormaghtigh |
| author_facet | Joëlle De Meutter Erik Goormaghtigh |
| author_sort | Joëlle De Meutter |
| collection | DOAJ |
| description | 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. |
| first_indexed | 2024-12-13T11:43:56Z |
| format | Article |
| id | doaj.art-ed11f6c2040247e09b2721c0b6e58c93 |
| institution | Directory Open Access Journal |
| issn | 2001-0370 |
| language | English |
| last_indexed | 2024-12-13T11:43:56Z |
| publishDate | 2020-01-01 |
| publisher | Elsevier |
| record_format | Article |
| series | Computational and Structural Biotechnology Journal |
| spelling | doaj.art-ed11f6c2040247e09b2721c0b6e58c932022-12-21T23:47:34ZengElsevierComputational and Structural Biotechnology Journal2001-03702020-01-011818641876A convenient protein library for spectroscopic calibrationsJoëlle De Meutter0Erik Goormaghtigh1Center for Structural Biology and Bioinformatics, Laboratory for the Structure and Function of Biological Membranes, Campus Plaine CP206/02, Brussels, BelgiumUniversité Libre de Bruxelles CP206/2, B1050 Brussels, Belgium; Corresponding author.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.http://www.sciencedirect.com/science/article/pii/S2001037020303330Protein selectionFTIR spectroscopySecondary structureProtein spectroscopy |
| spellingShingle | Joëlle De Meutter Erik Goormaghtigh A convenient protein library for spectroscopic calibrations Computational and Structural Biotechnology Journal Protein selection FTIR spectroscopy Secondary structure Protein spectroscopy |
| title | A convenient protein library for spectroscopic calibrations |
| title_full | A convenient protein library for spectroscopic calibrations |
| title_fullStr | A convenient protein library for spectroscopic calibrations |
| title_full_unstemmed | A convenient protein library for spectroscopic calibrations |
| title_short | A convenient protein library for spectroscopic calibrations |
| title_sort | convenient protein library for spectroscopic calibrations |
| topic | Protein selection FTIR spectroscopy Secondary structure Protein spectroscopy |
| url | http://www.sciencedirect.com/science/article/pii/S2001037020303330 |
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