Random heteropolymers preserve protein function in foreign environments
Panganiban, B., Qiao, B., Jiang, T., Del; Re, C., Obadia, M. M., Nguyen, T. D., Smith, A. A. A., Hall, A., Sit, I., Crosby, M. G., Dennis, P. B., Drockenmuller, E., Olvera de la Cruz, M., Xu, T.
American Association for the Advancement of Science (AAAS)
Published 2018
American Association for the Advancement of Science (AAAS)
Published 2018
| Publication Date: |
2018-03-16
|
|---|---|
| Publisher: |
American Association for the Advancement of Science (AAAS)
|
| Print ISSN: |
0036-8075
|
| Electronic ISSN: |
1095-9203
|
| Topics: |
Biology
Chemistry and Pharmacology
Geosciences
Computer Science
Medicine
Natural Sciences in General
Physics
|
| Keywords: |
Materials Science
|
| Published by: |
| _version_ | 1836398849321598977 |
|---|---|
| autor | Panganiban, B., Qiao, B., Jiang, T., Del; Re, C., Obadia, M. M., Nguyen, T. D., Smith, A. A. A., Hall, A., Sit, I., Crosby, M. G., Dennis, P. B., Drockenmuller, E., Olvera de la Cruz, M., Xu, T. |
| beschreibung | The successful incorporation of active proteins into synthetic polymers could lead to a new class of materials with functions found only in living systems. However, proteins rarely function under the conditions suitable for polymer processing. On the basis of an analysis of trends in protein sequences and characteristic chemical patterns on protein surfaces, we designed four-monomer random heteropolymers to mimic intrinsically disordered proteins for protein solubilization and stabilization in non-native environments. The heteropolymers, with optimized composition and statistical monomer distribution, enable cell-free synthesis of membrane proteins with proper protein folding for transport and enzyme-containing plastics for toxin bioremediation. Controlling the statistical monomer distribution in a heteropolymer, rather than the specific monomer sequence, affords a new strategy to interface with biological systems for protein-based biomaterials. |
| citation_standardnr | 6209064 |
| datenlieferant | ipn_articles |
| feed_id | 25 |
| feed_publisher | American Association for the Advancement of Science (AAAS) |
| feed_publisher_url | http://www.aaas.org/ |
| insertion_date | 2018-03-16 |
| journaleissn | 1095-9203 |
| journalissn | 0036-8075 |
| publikationsjahr_anzeige | 2018 |
| publikationsjahr_facette | 2018 |
| publikationsjahr_intervall | 7984:2015-2019 |
| publikationsjahr_sort | 2018 |
| publisher | American Association for the Advancement of Science (AAAS) |
| quelle | Science |
| relation | http://science.sciencemag.org/cgi/content/short/359/6381/1239?rss=1 |
| schlagwort | Materials Science |
| search_space | articles |
| shingle_author_1 | Panganiban, B., Qiao, B., Jiang, T., Del; Re, C., Obadia, M. M., Nguyen, T. D., Smith, A. A. A., Hall, A., Sit, I., Crosby, M. G., Dennis, P. B., Drockenmuller, E., Olvera de la Cruz, M., Xu, T. |
| shingle_author_2 | Panganiban, B., Qiao, B., Jiang, T., Del; Re, C., Obadia, M. M., Nguyen, T. D., Smith, A. A. A., Hall, A., Sit, I., Crosby, M. G., Dennis, P. B., Drockenmuller, E., Olvera de la Cruz, M., Xu, T. |
| shingle_author_3 | Panganiban, B., Qiao, B., Jiang, T., Del; Re, C., Obadia, M. M., Nguyen, T. D., Smith, A. A. A., Hall, A., Sit, I., Crosby, M. G., Dennis, P. B., Drockenmuller, E., Olvera de la Cruz, M., Xu, T. |
| shingle_author_4 | Panganiban, B., Qiao, B., Jiang, T., Del; Re, C., Obadia, M. M., Nguyen, T. D., Smith, A. A. A., Hall, A., Sit, I., Crosby, M. G., Dennis, P. B., Drockenmuller, E., Olvera de la Cruz, M., Xu, T. |
| shingle_catch_all_1 | Random heteropolymers preserve protein function in foreign environments Materials Science The successful incorporation of active proteins into synthetic polymers could lead to a new class of materials with functions found only in living systems. However, proteins rarely function under the conditions suitable for polymer processing. On the basis of an analysis of trends in protein sequences and characteristic chemical patterns on protein surfaces, we designed four-monomer random heteropolymers to mimic intrinsically disordered proteins for protein solubilization and stabilization in non-native environments. The heteropolymers, with optimized composition and statistical monomer distribution, enable cell-free synthesis of membrane proteins with proper protein folding for transport and enzyme-containing plastics for toxin bioremediation. Controlling the statistical monomer distribution in a heteropolymer, rather than the specific monomer sequence, affords a new strategy to interface with biological systems for protein-based biomaterials. Panganiban, B., Qiao, B., Jiang, T., Del; Re, C., Obadia, M. M., Nguyen, T. D., Smith, A. A. A., Hall, A., Sit, I., Crosby, M. G., Dennis, P. B., Drockenmuller, E., Olvera de la Cruz, M., Xu, T. American Association for the Advancement of Science (AAAS) 0036-8075 00368075 1095-9203 10959203 |
| shingle_catch_all_2 | Random heteropolymers preserve protein function in foreign environments Materials Science The successful incorporation of active proteins into synthetic polymers could lead to a new class of materials with functions found only in living systems. However, proteins rarely function under the conditions suitable for polymer processing. On the basis of an analysis of trends in protein sequences and characteristic chemical patterns on protein surfaces, we designed four-monomer random heteropolymers to mimic intrinsically disordered proteins for protein solubilization and stabilization in non-native environments. The heteropolymers, with optimized composition and statistical monomer distribution, enable cell-free synthesis of membrane proteins with proper protein folding for transport and enzyme-containing plastics for toxin bioremediation. Controlling the statistical monomer distribution in a heteropolymer, rather than the specific monomer sequence, affords a new strategy to interface with biological systems for protein-based biomaterials. Panganiban, B., Qiao, B., Jiang, T., Del; Re, C., Obadia, M. M., Nguyen, T. D., Smith, A. A. A., Hall, A., Sit, I., Crosby, M. G., Dennis, P. B., Drockenmuller, E., Olvera de la Cruz, M., Xu, T. American Association for the Advancement of Science (AAAS) 0036-8075 00368075 1095-9203 10959203 |
| shingle_catch_all_3 | Random heteropolymers preserve protein function in foreign environments Materials Science The successful incorporation of active proteins into synthetic polymers could lead to a new class of materials with functions found only in living systems. However, proteins rarely function under the conditions suitable for polymer processing. On the basis of an analysis of trends in protein sequences and characteristic chemical patterns on protein surfaces, we designed four-monomer random heteropolymers to mimic intrinsically disordered proteins for protein solubilization and stabilization in non-native environments. The heteropolymers, with optimized composition and statistical monomer distribution, enable cell-free synthesis of membrane proteins with proper protein folding for transport and enzyme-containing plastics for toxin bioremediation. Controlling the statistical monomer distribution in a heteropolymer, rather than the specific monomer sequence, affords a new strategy to interface with biological systems for protein-based biomaterials. Panganiban, B., Qiao, B., Jiang, T., Del; Re, C., Obadia, M. M., Nguyen, T. D., Smith, A. A. A., Hall, A., Sit, I., Crosby, M. G., Dennis, P. B., Drockenmuller, E., Olvera de la Cruz, M., Xu, T. American Association for the Advancement of Science (AAAS) 0036-8075 00368075 1095-9203 10959203 |
| shingle_catch_all_4 | Random heteropolymers preserve protein function in foreign environments Materials Science The successful incorporation of active proteins into synthetic polymers could lead to a new class of materials with functions found only in living systems. However, proteins rarely function under the conditions suitable for polymer processing. On the basis of an analysis of trends in protein sequences and characteristic chemical patterns on protein surfaces, we designed four-monomer random heteropolymers to mimic intrinsically disordered proteins for protein solubilization and stabilization in non-native environments. The heteropolymers, with optimized composition and statistical monomer distribution, enable cell-free synthesis of membrane proteins with proper protein folding for transport and enzyme-containing plastics for toxin bioremediation. Controlling the statistical monomer distribution in a heteropolymer, rather than the specific monomer sequence, affords a new strategy to interface with biological systems for protein-based biomaterials. Panganiban, B., Qiao, B., Jiang, T., Del; Re, C., Obadia, M. M., Nguyen, T. D., Smith, A. A. A., Hall, A., Sit, I., Crosby, M. G., Dennis, P. B., Drockenmuller, E., Olvera de la Cruz, M., Xu, T. American Association for the Advancement of Science (AAAS) 0036-8075 00368075 1095-9203 10959203 |
| shingle_title_1 | Random heteropolymers preserve protein function in foreign environments |
| shingle_title_2 | Random heteropolymers preserve protein function in foreign environments |
| shingle_title_3 | Random heteropolymers preserve protein function in foreign environments |
| shingle_title_4 | Random heteropolymers preserve protein function in foreign environments |
| timestamp | 2025-06-30T23:33:37.024Z |
| titel | Random heteropolymers preserve protein function in foreign environments |
| titel_suche | Random heteropolymers preserve protein function in foreign environments |
| topic | W V TE-TZ SQ-SU WW-YZ TA-TD U |
| uid | ipn_articles_6209064 |