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of 6
pro vyhledávání: '"Mustapha Carab Ahmed"'
Autor:
Mustapha Carab Ahmed, Line K. Skaanning, Alexander Jussupow, Estella A. Newcombe, Birthe B. Kragelund, Carlo Camilloni, Annette E. Langkilde, Kresten Lindorff-Larsen
Publikováno v:
Frontiers in Molecular Biosciences, Vol 8 (2021)
The inherent flexibility of intrinsically disordered proteins (IDPs) makes it difficult to interpret experimental data using structural models. On the other hand, molecular dynamics simulations of IDPs often suffer from force-field inaccuracies, and
Externí odkaz:
https://doaj.org/article/86f6af80565f4194b9e0b758008f8a7f
Publikováno v:
PeerJ, Vol 6, p e4967 (2018)
Salt bridges form between pairs of ionisable residues in close proximity and are important interactions in proteins. While salt bridges are known to be important both for protein stability, recognition and regulation, we still do not have fully accur
Externí odkaz:
https://doaj.org/article/8b7d846568a74260a16796bb9a0171ba
Publikováno v:
Methods in molecular biology (Clifton, N.J.). 2141
The level of compaction of an intrinsically disordered protein may affect both its physical and biological properties, and can be probed via different types of biophysical experiments. Small-angle X-ray scattering (SAXS) probe the radius of gyration
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=pmid________::de854e8b2e59bdcdc7972762398c7c2e
https://pubmed.ncbi.nlm.nih.gov/32696370
https://pubmed.ncbi.nlm.nih.gov/32696370
Publikováno v:
Methods in Molecular Biology ISBN: 9781071605233
Digital.CSIC. Repositorio Institucional del CSIC
instname
Digital.CSIC. Repositorio Institucional del CSIC
instname
The level of compaction of an intrinsically disordered protein may affect both its physical and biological properties, and can be probed via different types of biophysical experiments. Small-angle X-ray scattering (SAXS) probe the radius of gyration
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::1742d4d74932ef416e0ade4300982427
http://hdl.handle.net/10261/233265
http://hdl.handle.net/10261/233265
The level of compaction of an intrinsically disordered protein may affect both its physical and biological properties, and can be probed via different types of biophysical experiments. Small-angle X-ray scattering (SAXS) probe the radius of gyration
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::636cf32bdf923e59498be5659f20e6ca
https://doi.org/10.1101/679373
https://doi.org/10.1101/679373
Publikováno v:
PeerJ, Vol 6, p e4967 (2018)
Ahmed, M C H, Papaleo, E & Lindorff-Larsen, K 2018, ' How well do force fields capture the strength of salt bridges in proteins? ', PeerJ, vol. 6, 4967 . https://doi.org/10.7717/peerj.4967
Ahmed, M C H, Papaleo, E & Lindorff-Larsen, K 2018, ' How well do force fields capture the strength of salt bridges in proteins? ', PeerJ, vol. 6, 4967 . https://doi.org/10.7717/peerj.4967
Salt bridges form between pairs of ionisable residues in close proximity and are important interactions in proteins. While salt bridges are known to be important both for protein stability, recognition and regulation, we still do not have fully accur
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::19262fb3ff479a2198c5d8421b953113
https://peerj.com/articles/4967.pdf
https://peerj.com/articles/4967.pdf