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  1. Article: Dynamic pictures of membrane proteins in two-dimensional crystal, lipid bilayer and detergent as revealed by site-directed solid-state 13C NMR.

    Saitô, Hazime

    Chemistry and physics of lipids

    2004  Volume 132, Issue 1, Page(s) 101–112

    Abstract: We have compared site-directed 13C solid-state NMR spectra of [3-13C]Ala- and/or [1-13C]Val-labeled membrane proteins, including bacteriorhodopsin (bR), pharaonis phoborhodopin (ppR), its cognate transducer (pHtrII) and Escherichia coli diacylglycerol ... ...

    Abstract We have compared site-directed 13C solid-state NMR spectra of [3-13C]Ala- and/or [1-13C]Val-labeled membrane proteins, including bacteriorhodopsin (bR), pharaonis phoborhodopin (ppR), its cognate transducer (pHtrII) and Escherichia coli diacylglycerol kinase (DGK), in two-dimensional (2D) crystal, lipid bilayers, and detergent. Restricted fluctuation motions of these membrane proteins due to oligomerization of bR by specific protein-protein interactions in the 2D crystalline lattice or protein complex between ppR and pHtrII provide the most favorable environment to yield well-resolved, fully visible 13C NMR signals for [3-13C]Ala-labeled proteins. In contrast, several signals from such membrane proteins were broadened or lost owing to interference of inherent fluctuation frequencies (10(4)-10(5)Hz) with frequency of either proton decoupling or magic angle spinning, if their 13C NMR spectra were recorded as a monomer in lipid bilayers at ambient temperature. The presence of such protein dynamics is essential for the respective proteins to achieve their own biological functions. Finally, spectral broadening found for bR and DGK in detergents were discussed.
    MeSH term(s) Carbon Isotopes ; Crystallography/methods ; Detergents/chemistry ; Lipid Bilayers/chemistry ; Magnetic Resonance Spectroscopy ; Membrane Fluidity ; Membrane Proteins/chemistry ; Motion ; Multiprotein Complexes/chemistry ; Powders ; Protein Conformation
    Chemical Substances Carbon Isotopes ; Detergents ; Lipid Bilayers ; Membrane Proteins ; Multiprotein Complexes ; Powders
    Language English
    Publishing date 2004-11
    Publishing country Ireland
    Document type Comparative Study ; Journal Article
    ZDB-ID 213869-4
    ISSN 1873-2941 ; 0009-3084
    ISSN (online) 1873-2941
    ISSN 0009-3084
    DOI 10.1016/j.chemphyslip.2004.09.009
    Database MEDical Literature Analysis and Retrieval System OnLINE

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    In stock of ZB MED Cologne/Königswinter

    Zs.A 804: Show issues Location:
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  2. Article ; Online: Dynamic Structure and Orientation of Melittin Bound to Acidic Lipid Bilayers, As Revealed by Solid-State NMR and Molecular Dynamics Simulation.

    Norisada, Kazushi / Javkhlantugs, Namsrai / Mishima, Daisuke / Kawamura, Izuru / Saitô, Hazime / Ueda, Kazuyoshi / Naito, Akira

    The journal of physical chemistry. B

    2017  Volume 121, Issue 8, Page(s) 1802–1811

    Abstract: Melittin is a venom peptide that disrupts lipid bilayers at temperatures below the liquid-crystalline to gel phase transition temperature ( ... ...

    Abstract Melittin is a venom peptide that disrupts lipid bilayers at temperatures below the liquid-crystalline to gel phase transition temperature (T
    Language English
    Publishing date 2017-03-02
    Publishing country United States
    Document type Journal Article
    ISSN 1520-5207
    ISSN (online) 1520-5207
    DOI 10.1021/acs.jpcb.6b11207
    Database MEDical Literature Analysis and Retrieval System OnLINE

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  3. Article ; Online: Combined laparoscopic resection of intestinal stenosis of Garré and open preperitoneal mesh repair for irreducible femoral hernia.

    Soeta, Nobutoshi / Saito, Takuro / Higuchi, Mitsunori / Nemoto, Tetsutaro / Matsuida, Hazime / Oshibe, Ikuro

    Asian journal of endoscopic surgery

    2017  Volume 11, Issue 1, Page(s) 68–70

    Abstract: Intestinal stenosis of Garré is a rare condition caused by a benign fibrous bowel stricture due to complicated strangulated hernia. We present a case of intestinal stenosis of Garré associated with right femoral hernia in an 85-year-old woman. The ... ...

    Abstract Intestinal stenosis of Garré is a rare condition caused by a benign fibrous bowel stricture due to complicated strangulated hernia. We present a case of intestinal stenosis of Garré associated with right femoral hernia in an 85-year-old woman. The patient visited our hospital with a 2-day history of vomiting. Her abdomen was slightly distended. A mass was palpated in the right groin region. CT showed prolapse of the small intestine in the right groin region. An incarcerated right femoral hernia was diagnosed and manually reduced. Thirteen days later, the patient complained of abdominal pain. CT revealed dilatation and caliber change in part of the small bowel, indicating a small bowel obstruction due to intestinal stenosis of Garré. Laparoscopic release of the bowel obstruction and femoral hernia repair via an anterior approach were performed simultaneously. No recurrence of femoral hernia or bowel obstruction was noted at the 15-month follow-up.
    MeSH term(s) Abdominal Pain/diagnosis ; Abdominal Pain/etiology ; Aged, 80 and over ; Combined Modality Therapy ; Female ; Follow-Up Studies ; Hernia, Femoral/diagnostic imaging ; Hernia, Femoral/surgery ; Herniorrhaphy/adverse effects ; Herniorrhaphy/methods ; Humans ; Intestinal Obstruction/etiology ; Intestinal Obstruction/physiopathology ; Intestinal Obstruction/surgery ; Laparoscopy/methods ; Laparotomy/methods ; Peritoneum/physiopathology ; Peritoneum/surgery ; Risk Assessment ; Severity of Illness Index ; Surgical Mesh ; Time Factors ; Tomography, X-Ray Computed/methods ; Treatment Outcome
    Language English
    Publishing date 2017-06-30
    Publishing country Japan
    Document type Case Reports ; Journal Article
    ZDB-ID 2492135-X
    ISSN 1758-5910 ; 1758-5902
    ISSN (online) 1758-5910
    ISSN 1758-5902
    DOI 10.1111/ases.12402
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  4. Article ; Online: Chemical shift tensor - the heart of NMR: Insights into biological aspects of proteins.

    Saitô, Hazime / Ando, Isao / Ramamoorthy, Ayyalusamy

    Progress in nuclear magnetic resonance spectroscopy

    2010  Volume 57, Issue 2, Page(s) 181–228

    MeSH term(s) Animals ; Bacteria/chemistry ; Bacterial Proteins/chemistry ; Models, Molecular ; Nuclear Magnetic Resonance, Biomolecular/methods ; Protein Conformation ; Proteins/chemistry ; Quantum Theory
    Chemical Substances Bacterial Proteins ; Proteins
    Language English
    Publishing date 2010-05-07
    Publishing country England
    Document type Journal Article ; Research Support, N.I.H., Extramural ; Review
    ZDB-ID 209325-x
    ISSN 1873-3301 ; 0079-6565
    ISSN (online) 1873-3301
    ISSN 0079-6565
    DOI 10.1016/j.pnmrs.2010.04.005
    Database MEDical Literature Analysis and Retrieval System OnLINE

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    In stock of ZB MED Cologne/Königswinter

    Zs.A 2654: Show issues Location:
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  5. Article: NMR studies on fully hydrated membrane proteins, with emphasis on bacteriorhodopsin as a typical and prototype membrane protein.

    Saitô, Hazime / Naito, Akira

    Biochimica et biophysica acta

    2007  Volume 1768, Issue 12, Page(s) 3145–3161

    Abstract: The 3D structures or dynamic feature of fully hydrated membrane proteins are very important at ambient temperature, in relation to understanding their biological activities, although their data, especially from the flexible portions such as surface ... ...

    Abstract The 3D structures or dynamic feature of fully hydrated membrane proteins are very important at ambient temperature, in relation to understanding their biological activities, although their data, especially from the flexible portions such as surface regions, are unavailable from X-ray diffraction or cryoelectron microscope at low temperature. In contrast, high-resolution solid-state NMR spectroscopy has proved to be a very convenient alternative means to be able to reveal their dynamic structures. To clarify this problem, we describe here how we are able to reveal such structures and dynamic features, based on intrinsic probes from high-resolution solid-state NMR studies on bacteriorhodopsin (bR) as a typical membrane protein in 2D crystal, regenerated preparation in lipid bilayer and detergents. It turned out that their dynamic features are substantially altered upon their environments where bR is present. We further review NMR applications to study structure and dynamics of a variety of membrane proteins, including sensory rhodopsin, rhodopsin, photoreaction centers, diacylglycerol kinases, etc.
    MeSH term(s) Bacteriorhodopsins/chemistry ; Carbon Isotopes ; Magnetic Resonance Spectroscopy/methods ; Membrane Proteins/chemistry ; Models, Biological
    Chemical Substances Carbon Isotopes ; Membrane Proteins ; Bacteriorhodopsins (53026-44-1)
    Language English
    Publishing date 2007-12
    Publishing country Netherlands
    Document type Journal Article ; Review
    ZDB-ID 60-7
    ISSN 1879-2596 ; 1879-260X ; 1872-8006 ; 1879-2642 ; 1879-2618 ; 1879-2650 ; 0006-3002 ; 0005-2728 ; 0005-2736 ; 0304-4165 ; 0167-4838 ; 1388-1981 ; 0167-4889 ; 0167-4781 ; 0304-419X ; 1570-9639 ; 0925-4439 ; 1874-9399
    ISSN (online) 1879-2596 ; 1879-260X ; 1872-8006 ; 1879-2642 ; 1879-2618 ; 1879-2650
    ISSN 0006-3002 ; 0005-2728 ; 0005-2736 ; 0304-4165 ; 0167-4838 ; 1388-1981 ; 0167-4889 ; 0167-4781 ; 0304-419X ; 1570-9639 ; 0925-4439 ; 1874-9399
    DOI 10.1016/j.bbamem.2007.08.026
    Database MEDical Literature Analysis and Retrieval System OnLINE

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    Uc I Zs.247: Show issues Location:
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  6. Article: Dynamic Structure and Orientation of Melittin Bound to Acidic Lipid Bilayers, As Revealed by Solid-State NMR and Molecular Dynamics Simulation

    Norisada, Kazushi / Javkhlantugs Namsrai / Mishima Daisuke / Kawamura Izuru / Saitô Hazime / Ueda Kazuyoshi / Naito Akira

    Journal of physical chemistry. 2017 Mar. 02, v. 121, no. 8

    2017  

    Abstract: Melittin is a venom peptide that disrupts lipid bilayers at temperatures below the liquid-crystalline to gel phase transition temperature (Tc). Notably, the ability of melittin to disrupt acidic dimyristoylphosphatidylglycerol (DMPG) bilayers was weaker ... ...

    Abstract Melittin is a venom peptide that disrupts lipid bilayers at temperatures below the liquid-crystalline to gel phase transition temperature (Tc). Notably, the ability of melittin to disrupt acidic dimyristoylphosphatidylglycerol (DMPG) bilayers was weaker than its ability to disrupt neutral dimyristoylphosphatidylcholine bilayers. The structure and orientation of melittin bound to DMPG bilayers were revealed by analyzing the ¹³C chemical shift anisotropy of [1-¹³C]-labeled melittin obtained from solid-state ¹³C NMR spectra. ¹³C chemical shift anisotropy showed oscillatory shifts with the index number of residues. Analysis of the chemical shift oscillation properties indicated that melittin bound to a DMPG membrane adopts a bent α-helical structure with tilt angles for the N- and C-terminal helices of −32 and +30°, respectively. The transmembrane melittin in DMPG bilayers indicates that the peptide protrudes toward the C-terminal direction from the core region of the lipid bilayer to show a pseudotransmembrane bent α-helix. Molecular dynamics simulation was performed to characterize the structure and interaction of melittin with lipid molecules in DMPG bilayers. The simulation results indicate that basic amino acid residues in melittin interact strongly with lipid head groups to generate a pseudo-transmembrane alignment. The N-terminus is located within the lipid core region and disturbs the lower surface of the lipid bilayer.
    Keywords amino acids ; arsenic ; gels ; lipid bilayers ; lipids ; melittin ; molecular dynamics ; nuclear magnetic resonance spectroscopy ; phase transition ; stable isotopes ; temperature ; venoms
    Language English
    Dates of publication 2017-0302
    Size p. 1802-1811.
    Publishing place American Chemical Society
    Document type Article
    ISSN 1520-5207
    DOI 10.1021%2Facs.jpcb.6b11207
    Database NAL-Catalogue (AGRICOLA)

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  7. Article ; Online: Modern Magnetic Resonance

    Webb, G.A. / Craik, David J. / Martin, Gary / Saito, Hazime / Standal, Inger B. / van Duynhoven, John / Aursand, Marit / Bardet, Michel / So, Po-Wah / Utz, Marcel / Huang, Yining

    2018  

    Keywords Life Science
    Language English
    Publisher Springer
    Publishing country nl
    Document type Article ; Online
    Database BASE - Bielefeld Academic Search Engine (life sciences selection)

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  8. Book: Solid state NMR spectroscopy for biopolymers

    Saitô, Hazime / Ando, Isao / Naito, Akira

    principles and applications

    2006  

    Author's details Hazime Saitô; Isao Ando; Akira Naito
    Keywords Biopolymers ; Nuclear magnetic resonance spectroscopy
    Language English
    Size XIII, 464 S, graph. Darst
    Publisher Springer
    Publishing place Dordrecht
    Document type Book
    Note Literaturangaben
    ISBN 1402043023 ; 9781402043024
    Database Library catalogue of the German National Library of Science and Technology (TIB), Hannover

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  9. Article ; Online: Two different packing arrangements of antiparallel polyalanine.

    Asakura, Tetsuo / Okonogi, Michi / Horiguchi, Kumiko / Aoki, Akihiro / Saitô, Hazime / Knight, David P / Williamson, Mike P

    Angewandte Chemie (International ed. in English)

    2012  Volume 51, Issue 5, Page(s) 1212–1215

    MeSH term(s) Alanine/chemistry ; Crystallization ; Crystallography, X-Ray ; Humans ; Models, Molecular ; Peptides/chemistry
    Chemical Substances Peptides ; polyalanine (25191-17-7) ; Alanine (OF5P57N2ZX)
    Language English
    Publishing date 2012-01-27
    Publishing country Germany
    Document type Journal Article ; Research Support, Non-U.S. Gov't
    ZDB-ID 2011836-3
    ISSN 1521-3773 ; 1433-7851
    ISSN (online) 1521-3773
    ISSN 1433-7851
    DOI 10.1002/anie.201105356
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  10. Book ; Online: Solid state NMR spectroscopy for biopolymers

    Saitô, Hazime / Ando, Isao / Naito, Akira

    principles and applications

    2006  

    Abstract: Solid state NMR spectroscopy has proved to be the most suitable and unrivaled means for investigations of biopolymers. This work provides an account on how the conformation and dynamics of such biopolymers can be revealed by solid state NMR ... ...

    Author's details Hazime Saitô; Isao Ando; Akira Naito
    Abstract Solid state NMR spectroscopy has proved to be the most suitable and unrivaled means for investigations of biopolymers. This work provides an account on how the conformation and dynamics of such biopolymers can be revealed by solid state NMR spectroscopy
    Keywords Biomaterials ; Chemistry ; Chemistry, Physical organic ; Particles (Nuclear physics) ; Polymers ; Surfaces (Physics) ; Technik / Wissen Biologie ; Technik / Wissen Physik
    Language English
    Size Online-Ressource, graph. Darst.
    Publisher Springer
    Publishing place Dordrecht
    Document type Book ; Online
    Note Includes bibliographical references and index
    ISBN 9781402043024 ; 9781402043031 ; 1402043023 ; 1402043031
    DOI 10.1007/1-4020-4303-1
    Database Former special subject collection: coastal and deep sea fishing

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