Výsledky vyhledávání - "Anna Katarina Tigerström"

The Biologist's Forum: Thermostability of proteins

Publikováno v: BIOS. 76:22-27

Adaptations of proteins towards an increased thermostability can be observed in nature in environments such as the marine hydrothermal vents. The principles behind an increased thermostability can then be used in the biotech industry in order to desi

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https://doi.org/10.1893/0005-3155(2005)076[0022:tbftop]2.0.co

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Effects of a Novel Disulfide Bond and Engineered Electrostatic Interactions on the Thermostability of Azurin

Autor: Frederick P. Schwarz, M. Ökvist, Lennart Sjölin, B. Göran Karlsson, Anna Katarina Tigerström, Dennis L. Maeder, Carmen Alvarez-Rúa, Frank T. Robb

Publikováno v: Biochemistry. 43:12563-12574

Identification and evaluation of factors important for thermostability in proteins is a growing research field with many industrial applications. This study investigates the effects of introducing a novel disulfide bond and engineered electrostatic i

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https://doi.org/10.1021/bi048926x

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Purification of a recombinant membrane protein tagged with a calmodulin-binding domain: properties of chimeras of the Escherichia coli nicotinamide nucleotide transhydrogenase and the C-terminus of human plasma membrane Ca2+-ATPase

Autor: Jan Rydström, Nikolay B. Pestov, Mikhail I. Shakhparonov, Tatyana V. Korneenko, M. B. Kostina, Anna Katarina Tigerström, Maxim V Egorov

Publikováno v: Protein Expression and Purification. 36:31-39

A Ca2+ -dependent calmodulin-binding peptide (CBP) is an attractive tag for affinity purification of recombinant proteins, especially membrane proteins, since elution is simply accomplished by removing/chelating Ca2+. To develop a single-step calmodu

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https://doi.org/10.1016/j.pep.2004.03.002

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Phase transitions in adsorbed lipid vesicles measured using a quartz crystal microbalance with dissipation monitoring

Autor: Anna Katarina Tigerström, Bengt Herbert Kasemo, Gabriel Ohlsson, Fredrik Höök

Publikováno v: Soft Matter. 7:10749

Phase-transition induced structural changes of 1,2-ditridecanoyl-sn-glycero-3-phosphocholine (DTPC) lipid vesicles adsorbed on a titanium oxide (TiO(2)) surface have been investigated using a quartz crystal microbalance with dissipation (QCM-D) monit

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https://doi.org/10.1039/c1sm05923h

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The organization of the membrane domain and its interaction with the NADP(H)-binding site in proton-translocating transhydrogenase from E. coli

Autor: Tania Bizouarn, Anders Pedersen, Anna Katarina Tigerström, Jenny Karlsson, Magnus Althage, Jan Rydström, Carina B. Johansson

Publikováno v: Biochimica et Biophysica Acta (BBA) - Bioenergetics. (1-3):122-127

Proton-translocating nicotinamide nucleotide transhydrogenase is a conformationally driven pump which catalyzes the reversibel reduction of NADP+ by NADH. Transhydrogenases contain three domains, i.e., the hydrophilic NAD(H)-binding domain I and the

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