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  1. Article ; Online: Biophysical Chemistry in Groningen - A Personal Note.

    Hemminga, Marcus A

    The protein journal

    2023  Volume 42, Issue 3, Page(s) 162–164

    Abstract: This paper describes the start of the Biophysical Chemistry group of prof. Herman J.C. Berendsen (1934-2019) in Groningen, The Netherlands in the years from 1964 to 1974. ...

    Abstract This paper describes the start of the Biophysical Chemistry group of prof. Herman J.C. Berendsen (1934-2019) in Groningen, The Netherlands in the years from 1964 to 1974.
    Language English
    Publishing date 2023-03-16
    Publishing country Netherlands
    Document type Journal Article ; Review
    ZDB-ID 2143071-8
    ISSN 1875-8355 ; 1572-3887
    ISSN (online) 1875-8355
    ISSN 1572-3887
    DOI 10.1007/s10930-023-10097-6
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  2. Article ; Online: Biophysical Chemistry in Groningen – A Personal Note

    Hemminga, Marcus A.

    Protein Journal

    2023  Volume 42, Issue 3

    Abstract: This paper describes the start of the Biophysical Chemistry group of prof. Herman J.C. Berendsen (1934-2019) in Groningen, The Netherlands in the years from 1964 to 1974. ...

    Abstract This paper describes the start of the Biophysical Chemistry group of prof. Herman J.C. Berendsen (1934-2019) in Groningen, The Netherlands in the years from 1964 to 1974.
    Keywords Model membranes ; NMR and ESR spectroscopy ; Proteins ; Water
    Language English
    Publishing country nl
    Document type Article ; Online
    ZDB-ID 2143071-8
    ISSN 1875-8355 ; 1572-3887
    ISSN (online) 1875-8355
    ISSN 1572-3887
    Database BASE - Bielefeld Academic Search Engine (life sciences selection)

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  3. Book ; Online: ESR Spectroscopy in Membrane Biophysics

    Hemminga, Marcus A. / Berliner, Lawrence J.

    2007  

    Author's details by Marcus A. Hemminga, Lawrence J. Berliner
    Keywords Biochemistry ; Biomedical engineering ; Particles (Nuclear physics) ; Plasma (Ionized gases) ; Radiology, Medical
    Language English
    Publisher Springer Science+Business Media, LLC
    Publishing place Boston, MA
    Document type Book ; Online
    HBZ-ID TT050386795
    ISBN 978-0-387-25066-3 ; 978-0-387-49367-1 ; 0-387-25066-2 ; 0-387-49367-0
    DOI 10.1007/978-0-387-49367-1
    Database ZB MED Catalogue: Medicine, Health, Nutrition, Environment, Agriculture

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  4. Article ; Online: Membrane protein frustration: protein incorporation into hydrophobic mismatched binary lipid mixtures.

    Stopar, David / Spruijt, Ruud B / Hemminga, Marcus A

    Biophysical journal

    2009  Volume 96, Issue 4, Page(s) 1408–1414

    Abstract: Bacteriophage M13 major coat protein was reconstituted in different nonmatching binary lipid mixtures composed of 14:1PC and 22:1PC lipid bilayers. Challenged by this lose-lose situation of hydrophobic mismatch, the protein-lipid interactions are ... ...

    Abstract Bacteriophage M13 major coat protein was reconstituted in different nonmatching binary lipid mixtures composed of 14:1PC and 22:1PC lipid bilayers. Challenged by this lose-lose situation of hydrophobic mismatch, the protein-lipid interactions are monitored by CD and site-directed spin-label electron spin resonance spectroscopy of spin-labeled site-specific single cysteine mutants located in the C-terminal protein domain embedded in the hydrophobic core of the membrane (I39C) and at the lipid-water interface (T46C). The CD spectra indicate an overall alpha-helical conformation irrespective of the composition of the binary lipid mixture. Spin-labeled protein mutant I39C senses the phase transition in 22:1PC, in contrast to spin-labeled protein mutant T46C, which is not affected by the transition. The results of both CD and electron spin resonance spectroscopy clearly indicate that the protein preferentially partitions into the shorter 14:1PC both above and below the gel-to-liquid crystalline phase transition temperature of 22:1PC. This preference is related to the protein tilt angle and energy penalty the protein has to pay in the thicker 22:1PC. Given the fact that in Escherichia coli, which is the host for M13 bacteriophage, it is easier to find shorter 14 carbon acyl chains than longer 22 carbon acyl chains, the choice the M13 coat protein makes seems to be evolutionary justified.
    MeSH term(s) Bacteriophage M13 ; Capsid Proteins/chemistry ; Capsid Proteins/genetics ; Electron Spin Resonance Spectroscopy ; Hydrophobic and Hydrophilic Interactions ; Lipid Bilayers/chemistry ; Mutation ; Protein Structure, Tertiary ; Temperature
    Chemical Substances Capsid Proteins ; Lipid Bilayers ; coat protein, Bacteriophage M13
    Language English
    Publishing date 2009-01-06
    Publishing country United States
    Document type Journal Article ; Research Support, Non-U.S. Gov't
    ZDB-ID 218078-9
    ISSN 1542-0086 ; 0006-3495
    ISSN (online) 1542-0086
    ISSN 0006-3495
    DOI 10.1016/j.bpj.2008.11.029
    Database MEDical Literature Analysis and Retrieval System OnLINE

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  5. Article: Protein-lipid interactions of bacteriophage M13 gene 9 minor coat protein.

    Houbiers, M Chantal / Hemminga, Marcus A

    Molecular membrane biology

    2004  Volume 21, Issue 6, Page(s) 351–359

    Abstract: Gene 9 protein is one of the minor coat proteins of bacteriophage M13. The protein plays a role in the assembly process by associating with the host membrane by protein-lipid interactions. The availability of chemically synthesized protein has enabled ... ...

    Abstract Gene 9 protein is one of the minor coat proteins of bacteriophage M13. The protein plays a role in the assembly process by associating with the host membrane by protein-lipid interactions. The availability of chemically synthesized protein has enabled the biophysical characterization of the membrane-bound state of the protein by using model membrane systems. This paper summarizes, discusses and further interprets this work in the light of the current state of the literature, leading to new possible models of the coat protein in a membrane. The biological implications of these findings related to the membrane-bound phage assembly are indicated.
    MeSH term(s) Bacteriophage M13/chemistry ; Bacteriophage M13/metabolism ; Capsid Proteins/chemistry ; Capsid Proteins/metabolism ; Cell Membrane/metabolism ; Lipid Metabolism ; Protein Binding
    Chemical Substances Capsid Proteins ; gene 9 minor coat protein, bacteriophage M13
    Language English
    Publishing date 2004-11
    Publishing country England
    Document type Journal Article ; Review
    ZDB-ID 1186324-9
    ISSN 1464-5203 ; 0968-7688
    ISSN (online) 1464-5203
    ISSN 0968-7688
    DOI 10.1080/09687860400012918
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  6. Article: Analytical analysis of multi-pulse NMR.

    Nazarova, Irina / Hemminga, Marcus A

    Journal of magnetic resonance (San Diego, Calif. : 1997)

    2004  Volume 170, Issue 2, Page(s) 284–289

    Abstract: It is well known that in multi-pulse applications in high-resolution NMR and MRI a steady state is reached for the magnetisation vector by the effect of relaxation in combination with the pulse repetition time. In this paper, a mathematical model is ... ...

    Abstract It is well known that in multi-pulse applications in high-resolution NMR and MRI a steady state is reached for the magnetisation vector by the effect of relaxation in combination with the pulse repetition time. In this paper, a mathematical model is developed to understand how the parameters of the pulse sequence and relaxation times T(1) and T(2) affect the behaviour of the magnetisation vector. It will be shown that even under strong simplifying conditions an analytical analysis becomes very complex and only an analytical solution can be found for 90 degrees pulses and T(1)=T(2). For other cases a numerical approach is needed. Nevertheless, the basic approach of the mathematical analysis provides a general tool for analytical multi-operator applications. Our results provide a quantitative insight in the process by which the magnetisation relaxes towards the steady-state situation in a multi-pulse sequence.
    MeSH term(s) Magnetic Resonance Spectroscopy/methods ; Mathematics ; Signal Processing, Computer-Assisted
    Language English
    Publishing date 2004-10
    Publishing country United States
    Document type Journal Article
    ZDB-ID 1469665-4
    ISSN 1096-0856 ; 1557-8968 ; 1090-7807 ; 0022-2364
    ISSN (online) 1096-0856 ; 1557-8968
    ISSN 1090-7807 ; 0022-2364
    DOI 10.1016/j.jmr.2004.06.020
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  7. Article ; Online: Distance measurements on orthogonally spin-labeled membrane spanning WALP23 polypeptides.

    Lueders, Petra / Jäger, Heidrun / Hemminga, Marcus A / Jeschke, Gunnar / Yulikov, Maxim

    The journal of physical chemistry. B

    2013  Volume 117, Issue 7, Page(s) 2061–2068

    Abstract: EPR-based Gd(III)-nitroxide distance measurements were performed on a series of membrane-incorporated orthogonally labeled WALP23 polypeptides. The obtained distance distributions were stable upon the change of detection frequency from 10 GHz (X-band) to ...

    Abstract EPR-based Gd(III)-nitroxide distance measurements were performed on a series of membrane-incorporated orthogonally labeled WALP23 polypeptides. The obtained distance distributions were stable upon the change of detection frequency from 10 GHz (X-band) to 35 GHz (Q-band). The α-helical pitch of WALP23 polypeptide could be experimentally observed, despite the flexibility of the two spin labels. The spectroscopic properties of Gd(III) ions and nitroxide radicals allow detecting both types of paramagnetic species selectively in different EPR experiments. In particular, this spectroscopic selectivity allows for supplementing Gd(III)-nitroxide distance measurements with independent checks of polypeptide aggregation and with measurements of the local environment of the nitroxide spin labels. All mentioned additional checks do not require preparation of further samples, as it is the case in the experiments with pairs of identical nitroxide spin labels.
    MeSH term(s) Electron Spin Resonance Spectroscopy ; Gadolinium/chemistry ; Nitrogen Oxides/chemistry ; Peptides/chemistry ; Peptides/metabolism ; Spin Labels
    Chemical Substances Nitrogen Oxides ; Peptides ; Spin Labels ; WALP23 ; Gadolinium (AU0V1LM3JT) ; nitroxyl (GFQ4MMS07W)
    Language English
    Publishing date 2013-02-21
    Publishing country United States
    Document type Journal Article ; Research Support, Non-U.S. Gov't
    ISSN 1520-5207
    ISSN (online) 1520-5207
    DOI 10.1021/jp311287t
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  8. Book: ESR spectroscopy in membrane biophysics

    Hemminga, Marcus A / Berliner, Lawrence J

    (Biological magnetic resonance ; v. 27)

    2007  

    Author's details Marcus A. Hemminga and Lawrence J. Berliner
    Series title Biological magnetic resonance ; v. 27
    Keywords Electron paramagnetic resonance spectroscopy. ; Membrane proteins/Structure. ; Membranes (Biology)/Imaging.
    Language English
    Size xiv, 379 p. :, ill. ;, 24 cm. +
    Publisher Springer
    Publishing place New York
    Document type Book
    Accompanying material 1 CD-ROM (4 3/4 in.)
    ISBN 9780387250663 ; 0387250662
    Database NAL-Catalogue (AGRICOLA)

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  9. Article ; Online: Site-directed fluorescence labeling of a membrane protein with BADAN: probing protein topology and local environment.

    Koehorst, Rob B M / Spruijt, Ruud B / Hemminga, Marcus A

    Biophysical journal

    2008  Volume 94, Issue 10, Page(s) 3945–3955

    Abstract: The work presented here describes a new and simple method based on site-directed fluorescence labeling using the BADAN label that permits the examination of protein-lipid interactions in great detail. We applied this technique to a membrane-embedded, ... ...

    Abstract The work presented here describes a new and simple method based on site-directed fluorescence labeling using the BADAN label that permits the examination of protein-lipid interactions in great detail. We applied this technique to a membrane-embedded, mainly alpha-helical reference protein, the M13 major coat protein. Using a high-throughput approach, 40 site-specific cysteine mutants were prepared of the 50-residues long protein. The steady-state fluorescence spectra were analyzed using a three-component spectral model that enabled the separation of Stokes shift contributions from water and internal label dynamics, and protein topology. We found that most of the fluorescence originated from BADAN labels that were hydrogen-bonded to water molecules even within the hydrophobic core of the membrane. Our spectral decomposition method revealed the embedment and topology of the labeled protein in the membrane bilayer under various conditions of headgroup charge and lipid chain length, as well as key characteristics of the membrane such as hydration level and local polarity, provided by the local dielectric constant.
    MeSH term(s) 2-Naphthylamine/analogs & derivatives ; 2-Naphthylamine/chemistry ; Computer Simulation ; Crystallography/methods ; Lipid Bilayers/chemistry ; Membrane Proteins/chemistry ; Membrane Proteins/ultrastructure ; Models, Chemical ; Models, Molecular ; Molecular Probe Techniques ; Protein Conformation ; Spectrometry, Fluorescence/methods
    Chemical Substances 6-bromoacetyl-2-dimethylaminonaphthalene ; Lipid Bilayers ; Membrane Proteins ; 2-Naphthylamine (CKR7XL41N4)
    Language English
    Publishing date 2008-01-30
    Publishing country United States
    Document type Evaluation Study ; Journal Article
    ZDB-ID 218078-9
    ISSN 1542-0086 ; 0006-3495
    ISSN (online) 1542-0086
    ISSN 0006-3495
    DOI 10.1529/biophysj.107.125807
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  10. Article: Multiple Pathway Relaxation Enhancement in the System Composed of Three Paramagnetic Species: Nitroxide Radical-Ln(3+)-O2.

    Lueders, Petra / Jäger, Heidrun / Hemminga, Marcus A / Jeschke, Gunnar / Yulikov, Maxim

    The journal of physical chemistry letters

    2012  Volume 3, Issue 10, Page(s) 1336–1340

    Abstract: Longitudinal relaxation of nitroxide spin-labels has been measured for a membrane-incorporated α-helical polypeptide in the presence and absence of residual amounts of membrane-dissolved O2 and paramagnetic Dy(3+) ions. Such a model system, containing ... ...

    Abstract Longitudinal relaxation of nitroxide spin-labels has been measured for a membrane-incorporated α-helical polypeptide in the presence and absence of residual amounts of membrane-dissolved O2 and paramagnetic Dy(3+) ions. Such a model system, containing three different types of paramagnetic species, provides an important example of nonadditivity of two different relaxation channels for the nitroxide spins.
    Language English
    Publishing date 2012-05-17
    Publishing country United States
    Document type Journal Article
    ISSN 1948-7185
    ISSN 1948-7185
    DOI 10.1021/jz300316q
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