Zobrazeno 1 - 10
of 280
pro vyhledávání: '"protein-carbohydrate interaction"'
Akademický článek
Tento výsledek nelze pro nepřihlášené uživatele zobrazit.
K zobrazení výsledku je třeba se přihlásit.
K zobrazení výsledku je třeba se přihlásit.
Autor:
Marie Sofie Møller
Publikováno v:
Molecules, Vol 27, Iss 6, p 1915 (2022)
Glycoside hydrolase family 5 subfamily 8 (GH5_8) mannanases belong to Firmicutes, Actinomycetia, and Proteobacteria. The presence or absence of carbohydrate-binding modules (CBMs) present a striking difference. While various GH5_8 mannanases need a C
Externí odkaz:
https://doaj.org/article/f788d564796242a0bee38b3303a63572
Publikováno v:
Frontiers in Plant Science, Vol 9 (2018)
Biosynthesis of starch is catalyzed by a cascade of enzymes. The activity of a large number of these enzymes depends on interaction with polymeric substrates via carbohydrate binding sites, which are situated outside of the catalytic site and its imm
Externí odkaz:
https://doaj.org/article/06161f66ff7242e59fbf97cd6b1cc54b
Autor:
Pedro M. Nieto
Publikováno v:
Frontiers in Molecular Biosciences, Vol 5 (2018)
Carbohydrates are biologically ubiquitous and are essential to the existence of all known living organisms. Although they are better known for their role as energy sources (glucose/glycogen or starch) or structural elements (chitin or cellulose), car
Externí odkaz:
https://doaj.org/article/794706fe802e47fd8ee4c585fcf43443
Publikováno v:
Molecules, Vol 20, Iss 5, Pp 7700-7718 (2015)
Carbohydrate recognition by proteins, such as lectins and other (bio)molecules, can be essential for many biological functions. Recently, interest has arisen due to potential protein and drug design and future bioengineering applications. A quantitat
Externí odkaz:
https://doaj.org/article/642b31ce8a404882907fe3637c78da16
Autor:
Mikkel Madsen, Andreas Prestel, Eva Madland, Peter Westh, Anne Tøndervik, Håvard Sletta, Günther H. J. Peters, Finn L. Aachmann, Birthe B. Kragelund, Birte Svensson
Publikováno v:
Madsen, M, Prestel, A, Madland, E, Westh, P, Tøndervik, A, Sletta, H, Peters, G H J, Aachmann, F L, Kragelund, B B & Svensson, B 2023, ' Molecular insights into alginate β-lactoglobulin A multivalencies – the foundation for their amorphous aggregates and coacervation ', Protein Science, vol. 32, no. 2, e4556 . https://doi.org/10.1002/pro.4556
Madsen, M, Prestel, A, Madland, E, Westh, P, Tondervik, A, Sletta, H, Peters, G H J, Aachmann, F L L, Kragelund, B B B & Svensson, B 2023, ' Molecular insights into alginate beta-lactoglobulin A multivalencies : The foundation for their amorphous aggregates and coacervation ', Protein Science, vol. 32, no. 2, 4556 . https://doi.org/10.1002/pro.4556
Madsen, M, Prestel, A, Madland, E, Westh, P, Tondervik, A, Sletta, H, Peters, G H J, Aachmann, F L L, Kragelund, B B B & Svensson, B 2023, ' Molecular insights into alginate beta-lactoglobulin A multivalencies : The foundation for their amorphous aggregates and coacervation ', Protein Science, vol. 32, no. 2, 4556 . https://doi.org/10.1002/pro.4556
For improved control of biomaterial property design, a better understanding of complex coacervation involving anionic polysaccharides and proteins is needed. Here, we address the initial steps in condensate formation of β-lactoglobulin A (β-LgA) wi
Autor:
Rewati Dixit, Khushal Khambhati, Kolli Venkata Supraja, Vijai Singh, Franziska Lederer, Pau-Loke Show, Mukesh Kumar Awasthi, Abhinav Sharma, Rohan Jain
Publikováno v:
Bioresource Technology 370(2023), 128522
Machine learning (ML) applications have become ubiquitous in all fields of research including protein science and engineering. Apart from protein structure and mutation prediction, scientists are focusing on knowledge gaps with respect to the molecul
Akademický článek
Tento výsledek nelze pro nepřihlášené uživatele zobrazit.
K zobrazení výsledku je třeba se přihlásit.
K zobrazení výsledku je třeba se přihlásit.
Publikováno v:
Glycoconjugate Journal
Lectins are proteins with diverse molecular structures that share the ability to recognize and bind specifically and reversibly to carbohydrate structures without changing the carbohydrate moiety. The history of lectins started with the discovery of
Publikováno v:
Applied Biochemistry and Biotechnology
We compare three different methods to quantify the monosaccharide fucose in solutions using the displacement of a large glycoprotein, lactoferrin. Two microfluidic analysis methods, namely fluorescence detection of (labeled) lactoferrin as it is disp