Zobrazeno 1 - 10
of 71
pro vyhledávání: '"local unfolding"'
Publikováno v:
Frontiers in Molecular Biosciences, Vol 7 (2021)
Susceptibility to endosomal degradation is a decisive contribution to a protein's immunogenicity. It is assumed that the processing kinetics of structured proteins are inherently linked to their probability of local unfolding. In this study, we quant
Externí odkaz:
https://doaj.org/article/88b9ab9f473f4d2b831cc23ed3a9773a
Autor:
Amit Kumar, Jochen Balbach
Publikováno v:
Biomolecules, Vol 11, Iss 6, p 840 (2021)
Ankyrin repeat proteins are found in all three kingdoms of life. Fundamentally, these proteins are involved in protein-protein interaction in order to activate or suppress biological processes. The basic architecture of these proteins comprises repea
Externí odkaz:
https://doaj.org/article/29e828ac9a764e948c824e901a586b1f
Autor:
Mohamad Zahid Kamal, Virender Kumar, Kundarapu Satyamurthi, Kushal Kumar Das, Nalam Madhusudhana Rao
Publikováno v:
FEBS Open Bio, Vol 6, Iss 2, Pp 126-134 (2016)
Characterization of amorphous protein aggregates may offer insights into the process of aggregation. Eleven single amino acid mutants of lipase (LipA of Bacillus subtilis) were subjected to temperature‐induced aggregation, and the resultant aggrega
Externí odkaz:
https://doaj.org/article/cf62b06f80b04ca5a15c176892d47050
Akademický článek
Tento výsledek nelze pro nepřihlášené uživatele zobrazit.
K zobrazení výsledku je třeba se přihlásit.
K zobrazení výsledku je třeba se přihlásit.
Autor:
Marguet, Philippe Robert
Driven by the development of new technologies and an ever expanding knowledge base of molecular and cellular function, Biology is rapidly gaining the potential to develop into a veritable engineering discipline - the so-called `era of synthetic biolo
Externí odkaz:
http://hdl.handle.net/10161/3143
Autor:
Hofer, Florian, Kamenik, Anna S., Fernández-Quintero, Monica L., Kraml, Johannes, Liedl, Klaus R.
Publikováno v:
Frontiers in Molecular Biosciences, Vol 7 (2021)
Frontiers in Molecular Biosciences
Frontiers in Molecular Biosciences
Susceptibility to endosomal degradation is a decisive contribution to a protein's immunogenicity. It is assumed that the processing kinetics of structured proteins are inherently linked to their probability of local unfolding. In this study, we quant
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=pmid_dedup__::8901d5f8b2cdd90077a3ffbe2ee6f2b2
https://www.frontiersin.org/articles/10.3389/fmolb.2020.603644/full
https://www.frontiersin.org/articles/10.3389/fmolb.2020.603644/full
Publikováno v:
Nature
Adaptation of organisms to environmental niches is a hallmark of evolution. One prevalent example is that of thermal adaptation, in which two descendants evolve at different temperature extremes1,2. Underlying the physiological differences between su
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::ad96f718485e53ec89093a3d994fc274
http://europepmc.org/articles/PMC6033628
http://europepmc.org/articles/PMC6033628
Publikováno v:
International Journal of Molecular Sciences, Vol 22, Iss 10296, p 10296 (2021)
International Journal of Molecular Sciences
International Journal of Molecular Sciences
The association of two or more proteins to adopt a quaternary complex is one of the most widespread mechanisms by which protein function is modulated. In this scenario, three-dimensional domain swapping (3D-DS) constitutes one plausible pathway for t
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::b7853f7aad26a136508d99a71aef8c39
https://doi.org/10.3390/ijms221910296
https://doi.org/10.3390/ijms221910296
Publikováno v:
Proceedings of the National Academy of Sciences of the United States of America
Significance The discovery that more than 40% of the eukaryotic proteome is intrinsically disordered, and that these disordered segments are enriched in phosphorylation sites, suggests that conformational heterogeneity may be important to kinase sele
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::e4648f2fcac42990a93a68cb31c3747d
https://doi.org/10.1101/866558
https://doi.org/10.1101/866558
Autor:
Jochen Balbach, Amit Kumar
Publikováno v:
Biomolecules, Vol 11, Iss 840, p 840 (2021)
Biomolecules
Biomolecules
Ankyrin repeat proteins are found in all three kingdoms of life. Fundamentally, these proteins are involved in protein-protein interaction in order to activate or suppress biological processes. The basic architecture of these proteins comprises repea
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::ee03cc9c1d28965a5e5e904b5c9942cb
https://doi.org/10.3390/biom11060840
https://doi.org/10.3390/biom11060840