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  1. Article: The Quest for Simplicity: Remarks on the Free-Approach Models

    Jaremko, Łukasz / Jaremko Mariusz / Nowakowski Michał / Ejchart Andrzej

    Journal of physical chemistry. 2015 Sept. 10, v. 119, no. 36

    2015  

    Abstract: Nuclear magnetic relaxation provides a powerful method giving insight into molecular motions at atomic resolution on a broad time scale. Dynamics of biological macromolecules has been widely exploited by measuring ¹⁵N and ¹³C relaxation data. ... ...

    Abstract Nuclear magnetic relaxation provides a powerful method giving insight into molecular motions at atomic resolution on a broad time scale. Dynamics of biological macromolecules has been widely exploited by measuring ¹⁵N and ¹³C relaxation data. Interpretation of these data relies almost exclusively on the use of the model-free approach (MFA) and its extended version (EMFA) which requires no particular physical model of motion and a small number of parameters. It is shown that EMFA is often unable to cope with three different time scales and fails to describe slow internal motions properly. In contrast to EMFA, genuine MFA with two time scales can reproduce internal motions slower than the overall tumbling. It is also shown that MFA and simplified EMFA are equivalent with respect to the values of the N–H bond length and chemical shift anisotropy. Therefore, the vast majority of ¹⁵N relaxation data for proteins can be satisfactorily interpreted solely with MFA.
    Keywords chemical bonding ; models ; nitrogen ; proteins ; stable isotopes
    Language English
    Dates of publication 2015-0910
    Size p. 11978-11987.
    Publishing place American Chemical Society
    Document type Article
    ISSN 1520-5207
    DOI 10.1021%2Facs.jpcb.5b07181
    Database NAL-Catalogue (AGRICOLA)

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  2. Article: Structure of the Mitochondrial Translocator Protein in Complex with a Diagnostic Ligand

    Jaremko, Łukasz / Karin Giller / Mariusz Jaremko / Markus Zweckstetter / Stefan Becker

    Science. 2014 Mar. 21, v. 343, no. 6177

    2014  

    Abstract: Translocation in Injury The translocator protein TSPO is essential for the import of cholesterol and porphyrins into mitochondria. TSPO expression increases in areas of brain injury and during neuroinflammation and, thus, has diagnostic and therapeutic ... ...

    Abstract Translocation in Injury The translocator protein TSPO is essential for the import of cholesterol and porphyrins into mitochondria. TSPO expression increases in areas of brain injury and during neuroinflammation and, thus, has diagnostic and therapeutic implications. Jaremko et al. (p. 1363) used nuclear magnetic resonance spectroscopy to determine the high-resolution structure of the 18- kilodalton mammalian TSPO with the ligand PK11195, which stabilized the structure and resolved the conformation as a tight bundle of five helices.
    Keywords brain ; cholesterol ; ligands ; mammals ; mitochondria ; nuclear magnetic resonance spectroscopy ; porphyrins
    Language English
    Dates of publication 2014-0321
    Size p. 1363-1366.
    Publishing place American Association for the Advancement of Science
    Document type Article
    ZDB-ID 128410-1
    ISSN 1095-9203 ; 0036-8075
    ISSN (online) 1095-9203
    ISSN 0036-8075
    DOI 10.1126/science.1248725
    Database NAL-Catalogue (AGRICOLA)

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  3. Article: Impact of Calcium Binding and Thionylation of S100A1 Protein on Its Nuclear Magnetic Resonance-Derived Structure and Backbone Dynamics

    Nowakowski, Michał / Ruszczyńska-Bartnik Katarzyna / Budzińska Monika / Jaremko Łukasz / Jaremko Mariusz / Zdanowski Konrad / Bierzyński Andrzej / Ejchart Andrzej

    Biochemistry. 2013 Feb. 19, v. 52, no. 7

    2013  

    Abstract: S100 proteins play a crucial role in multiple important biological processes in vertebrate organisms acting predominantly as calcium signal transmitters. S100A1 is a typical representative of this family of proteins. After four Ca²⁺ ions bind, it ... ...

    Abstract S100 proteins play a crucial role in multiple important biological processes in vertebrate organisms acting predominantly as calcium signal transmitters. S100A1 is a typical representative of this family of proteins. After four Ca²⁺ ions bind, it undergoes a dramatic conformational change, resulting in exposure, in each of its two identical subunits, a large hydrophobic cleft that binds to target proteins. It has been shown that abnormal expression of S100A1 is strongly correlated with a number of severe human diseases: cardiomyopathy and neurodegenerative disorders. A few years ago, we found that thionylation of Cys 85, the unique cysteine in two identical S100A1 subunits, leads to a drastic increase of the affinity of the protein for calcium. We postulated that the protein activated by thionylation becomes a more efficient calcium signal transmitter. Therefore, we decided to undertake, using nuclear magnetic resonance methods, a comparative study of the structure and dynamics of native and thionylated human S100A1 in its apo and holo states. In this paper, we present the results obtained for both forms of this protein in its holo state and compare them with the previously published structure of native apo-S100. The main conclusion that we draw from these results is that the increased calcium binding affinity of S100A1 upon thionylation arises, most probably, from rearrangement of the hydrophobic core in its apo form.
    Keywords binding capacity ; calcium ; calcium signaling ; cardiomyopathy ; cysteine ; human diseases ; humans ; hydrophobicity ; ions ; neurodegenerative diseases ; nuclear magnetic resonance spectroscopy ; proteins
    Language English
    Dates of publication 2013-0219
    Size p. 1149-1159.
    Publishing place American Chemical Society
    Document type Article
    ZDB-ID 1108-3
    ISSN 1520-4995 ; 0006-2960
    ISSN (online) 1520-4995
    ISSN 0006-2960
    DOI 10.1021%2Fbi3015407
    Database NAL-Catalogue (AGRICOLA)

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