Data regarding the sensibility to proteolysis of a natural apolipoprotein A-I mutant.
The article shows dataset of the proteolysis of a natural variant of apolipoprotein A-I (apoA-I) with a substitution of a leucine by and arginine in position 60 (L60R), in comparison with the protein with the native sequence (Wt). This information demonstrates the potential of in vitro partial prote...
| Main Authors: | , , , , , , |
|---|---|
| Format: | Article |
| Language: | English |
| Published: |
Elsevier
2020-08-01
|
| Series: | Data in Brief |
| Subjects: | |
| Online Access: | http://www.sciencedirect.com/science/article/pii/S2352340920308544 |
| _version_ | 1811331852430999552 |
|---|---|
| author | Gisela M. Gaddi Romina A. Gisonno Silvana A. Rosú M. Fernanda Cortez Gabriela S. Finarelli Nahuel A. Ramella M. Alejandra Tricerri |
| author_facet | Gisela M. Gaddi Romina A. Gisonno Silvana A. Rosú M. Fernanda Cortez Gabriela S. Finarelli Nahuel A. Ramella M. Alejandra Tricerri |
| author_sort | Gisela M. Gaddi |
| collection | DOAJ |
| description | The article shows dataset of the proteolysis of a natural variant of apolipoprotein A-I (apoA-I) with a substitution of a leucine by and arginine in position 60 (L60R), in comparison with the protein with the native sequence (Wt). This information demonstrates the potential of in vitro partial proteolysis experiments as it may be applicable to different approaches in the biophysical field. We have analyzed by different electrophoresis techniques apoA-I variants, quantified the degree of proteolysis after staining and compared the proteolysis efficiency with the computed cleavage patterns. The data shown here clearly strengthen the usefulness of this approach to test protein flexibility, as it may be attained with enzymes which are not expected to modify in vivo this protein but have a well-known digestion pattern. In addition it is appropriate for evaluating protein catabolism, as it is exemplified here by the evidence with metalloproteinase 12 (MMP-12), which is a physiological protease that may elicit the pro-inflammatory processing of this variant within the lesions. We support the work “Structural analysis of a natural apolipoprotein A-I variant (L60R) associated with amyloidosis” (Gaddi, et al., 2020), gaining insights on protein folding from a characterization by proteolysis analysis [1]. |
| first_indexed | 2024-04-13T16:28:04Z |
| format | Article |
| id | doaj.art-be0b9e4f26ec49139e994b3f3ff21d8f |
| institution | Directory Open Access Journal |
| issn | 2352-3409 |
| language | English |
| last_indexed | 2024-04-13T16:28:04Z |
| publishDate | 2020-08-01 |
| publisher | Elsevier |
| record_format | Article |
| series | Data in Brief |
| spelling | doaj.art-be0b9e4f26ec49139e994b3f3ff21d8f2022-12-22T02:39:42ZengElsevierData in Brief2352-34092020-08-0131105960Data regarding the sensibility to proteolysis of a natural apolipoprotein A-I mutant.Gisela M. Gaddi0Romina A. Gisonno1Silvana A. Rosú2M. Fernanda Cortez3Gabriela S. Finarelli4Nahuel A. Ramella5M. Alejandra Tricerri6Instituto de Investigaciones Bioquímicas de La Plata (INIBIOLP), CONICET, La Plata, Buenos Aires, Argentina; Facultad de Ciencias Médicas, Universidad Nacional de La Plata, Calle 60 y 120. La Plata, Buenos Aires, ArgentinaInstituto de Investigaciones Bioquímicas de La Plata (INIBIOLP), CONICET, La Plata, Buenos Aires, Argentina; Facultad de Ciencias Médicas, Universidad Nacional de La Plata, Calle 60 y 120. La Plata, Buenos Aires, ArgentinaInstituto de Investigaciones Bioquímicas de La Plata (INIBIOLP), CONICET, La Plata, Buenos Aires, Argentina; Facultad de Ciencias Médicas, Universidad Nacional de La Plata, Calle 60 y 120. La Plata, Buenos Aires, ArgentinaInstituto de Investigaciones Bioquímicas de La Plata (INIBIOLP), CONICET, La Plata, Buenos Aires, ArgentinaInstituto de Investigaciones Bioquímicas de La Plata (INIBIOLP), CONICET, La Plata, Buenos Aires, ArgentinaInstituto de Investigaciones Bioquímicas de La Plata (INIBIOLP), CONICET, La Plata, Buenos Aires, Argentina; Facultad de Ciencias Médicas, Universidad Nacional de La Plata, Calle 60 y 120. La Plata, Buenos Aires, Argentina; Corresponding authors at: Instituto de Investigaciones Bioquímicas de La Plata (INIBIOLP), CONICET, La Plata, Buenos Aires, ArgentinaInstituto de Investigaciones Bioquímicas de La Plata (INIBIOLP), CONICET, La Plata, Buenos Aires, Argentina; Facultad de Ciencias Médicas, Universidad Nacional de La Plata, Calle 60 y 120. La Plata, Buenos Aires, Argentina; Corresponding authors at: Instituto de Investigaciones Bioquímicas de La Plata (INIBIOLP), CONICET, La Plata, Buenos Aires, ArgentinaThe article shows dataset of the proteolysis of a natural variant of apolipoprotein A-I (apoA-I) with a substitution of a leucine by and arginine in position 60 (L60R), in comparison with the protein with the native sequence (Wt). This information demonstrates the potential of in vitro partial proteolysis experiments as it may be applicable to different approaches in the biophysical field. We have analyzed by different electrophoresis techniques apoA-I variants, quantified the degree of proteolysis after staining and compared the proteolysis efficiency with the computed cleavage patterns. The data shown here clearly strengthen the usefulness of this approach to test protein flexibility, as it may be attained with enzymes which are not expected to modify in vivo this protein but have a well-known digestion pattern. In addition it is appropriate for evaluating protein catabolism, as it is exemplified here by the evidence with metalloproteinase 12 (MMP-12), which is a physiological protease that may elicit the pro-inflammatory processing of this variant within the lesions. We support the work “Structural analysis of a natural apolipoprotein A-I variant (L60R) associated with amyloidosis” (Gaddi, et al., 2020), gaining insights on protein folding from a characterization by proteolysis analysis [1].http://www.sciencedirect.com/science/article/pii/S2352340920308544Apolipoprotein A-I -partial proteolysis analysis-protein structure and catabolism-protein flexibility |
| spellingShingle | Gisela M. Gaddi Romina A. Gisonno Silvana A. Rosú M. Fernanda Cortez Gabriela S. Finarelli Nahuel A. Ramella M. Alejandra Tricerri Data regarding the sensibility to proteolysis of a natural apolipoprotein A-I mutant. Data in Brief Apolipoprotein A-I -partial proteolysis analysis-protein structure and catabolism-protein flexibility |
| title | Data regarding the sensibility to proteolysis of a natural apolipoprotein A-I mutant. |
| title_full | Data regarding the sensibility to proteolysis of a natural apolipoprotein A-I mutant. |
| title_fullStr | Data regarding the sensibility to proteolysis of a natural apolipoprotein A-I mutant. |
| title_full_unstemmed | Data regarding the sensibility to proteolysis of a natural apolipoprotein A-I mutant. |
| title_short | Data regarding the sensibility to proteolysis of a natural apolipoprotein A-I mutant. |
| title_sort | data regarding the sensibility to proteolysis of a natural apolipoprotein a i mutant |
| topic | Apolipoprotein A-I -partial proteolysis analysis-protein structure and catabolism-protein flexibility |
| url | http://www.sciencedirect.com/science/article/pii/S2352340920308544 |
| work_keys_str_mv | AT giselamgaddi dataregardingthesensibilitytoproteolysisofanaturalapolipoproteinaimutant AT rominaagisonno dataregardingthesensibilitytoproteolysisofanaturalapolipoproteinaimutant AT silvanaarosu dataregardingthesensibilitytoproteolysisofanaturalapolipoproteinaimutant AT mfernandacortez dataregardingthesensibilitytoproteolysisofanaturalapolipoproteinaimutant AT gabrielasfinarelli dataregardingthesensibilitytoproteolysisofanaturalapolipoproteinaimutant AT nahuelaramella dataregardingthesensibilitytoproteolysisofanaturalapolipoproteinaimutant AT malejandratricerri dataregardingthesensibilitytoproteolysisofanaturalapolipoproteinaimutant |