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pro vyhledávání: '"Anna Seelig"'
Autor:
Joachim Seelig, Anna Seelig
Publikováno v:
International Journal of Molecular Sciences, Vol 24, Iss 6, p 5457 (2023)
We review the key steps leading to an improved analysis of thermal protein unfolding. Thermal unfolding is a dynamic cooperative process with many short-lived intermediates. Protein unfolding has been measured by various spectroscopic techniques that
Externí odkaz:
https://doaj.org/article/a71499795f374392ac5b9f870ef84ca7
Autor:
Joachim Seelig, Anna Seelig
Publikováno v:
Biophysical Reports, Vol 2, Iss 1, Pp 100037- (2022)
Testing and predicting protein stability gained importance because proteins, including antibodies, became pharmacologically relevant in viral and cancer therapies. Isothermal scanning calorimetry is the principle method to study protein stability. He
Externí odkaz:
https://doaj.org/article/a8e96655431b4368a3abca86bbaf0035
Autor:
Anna Seelig
Publikováno v:
Frontiers in Oncology, Vol 10 (2020)
P-glycoprotein or multidrug resistance protein (MDR1) is an adenosine triphosphate (ATP) binding cassette transporter (ABCB1) intensely investigated because it is an obstacle to successful pharmacotherapy of cancers. P-glycoprotein prevents cellular
Externí odkaz:
https://doaj.org/article/3fd883691ec84d55b1512511de5b61e7
Publikováno v:
ACS Central Science, Vol 3, Iss 3, Pp 250-258 (2017)
Externí odkaz:
https://doaj.org/article/06a993b3d8844f91b9a8018d565769f8
Autor:
Joachim Seelig, Anna Seelig
Chemical unfolding with guanidineHCl or urea is a common method to study the conformational stability of proteins. The analysis of unfolding isotherms is usually performed with an empirical linear extrapolation method (LEM). The method contradicts ho
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::bbe6b3c34dc883577173e75e25fcd967
https://doi.org/10.1101/2023.05.11.540313
https://doi.org/10.1101/2023.05.11.540313
Autor:
Joachim Seelig, Anna Seelig
Protein stability is important in many areas of life sciences. Thermal protein unfolding is investigated extensively with various spectroscopic techniques. The extraction of thermodynamic properties from these measurements requires the application of
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::a4ee66b90e9fc97957b7185c39fb6319
Autor:
Anna Seelig, Xiaochun Li-Blatter
P-glycoprotein (ABCB1) is the first discovered mammalian member of the large family of ATP binding cassette (ABC) transporters. It facilitates the movement of compounds (called allocrites) across membranes, using the energy of ATP binding and hydroly
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::112f3c55faa80c8ce60dd50d0006d109
https://edoc.unibas.ch/92157/
https://edoc.unibas.ch/92157/
Autor:
Joachim Seelig, Anna Seelig
Protein stability is of utmost importance in many areas of life sciences and life science technology. The gold standard for assessing protein stability is the measurement of the heat capacity Cp(T), showing large peaks at the temperature of cold and
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::41573d867a54832b600b2488b311effb
https://doi.org/10.21203/rs.3.rs-2332836/v1
https://doi.org/10.21203/rs.3.rs-2332836/v1
Autor:
Joachim Seelig, Anna Seelig
Protein unfolding is a dynamic cooperative process with many short-lived intermediates. Cooperativity means that similar molecular elements act dependently on each other. The thermodynamics of protein unfolding can be determined with differential sca
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::143e04bd6bfd7be6c0709fca25a3b2c6
Autor:
Anna Seelig, Joachim Seelig
Publikováno v:
SSRN Electronic Journal.
Protein unfolding is a dynamic cooperative equilibrium between short lived protein conformations. The Zimm-Bragg theory is an ideal algorithm to handle cooperative processes. Here, we extend the analytical capabilities of the Zimm-Bragg theory in two