3P219 Conformational analysis of tryptophan residues in bacteriorhodopsin by solid-state NMR(Photobiology- vision and photoreception,Poster Presentations)

Kana Tajima; Izuru Kawamura; Satoru Tuzi; Akria Naito

doi:10.2142/biophys.47.s257_4

3P219 Conformational analysis of tryptophan residues in bacteriorhodopsin by solid-state NMR(Photobiology- vision and photoreception,Poster Presentations)

Seibutsu Butsuri ◽

10.2142/biophys.47.s257_4 ◽

2007 ◽

Vol 47 (supplement) ◽

pp. S257

Author(s):

Kana Tajima ◽

Izuru Kawamura ◽

Satoru Tuzi ◽

Akria Naito

Keyword(s):

Solid State ◽

Conformational Analysis ◽

Solid State Nmr ◽

Tryptophan Residues ◽

Poster Presentations

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Solid-State NMR Spectroscopy Detects Interactions between Tryptophan Residues of theE. coliSugar Transporter GalP and the α-Anomer of thed-Glucose Substrate

Journal of the American Chemical Society ◽

10.1021/ja075584k ◽

2008 ◽

Vol 130 (4) ◽

pp. 1236-1244 ◽

Cited By ~ 24

Author(s):

Simon G. Patching ◽

Peter J. F. Henderson ◽

Richard B. Herbert ◽

David A. Middleton

Keyword(s):

Solid State ◽

Nmr Spectroscopy ◽

Solid State Nmr ◽

Solid State Nmr Spectroscopy ◽

Tryptophan Residues

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Conformational analysis of the full-length M2 protein of the influenza A virus using solid-state NMR

Protein Science ◽

10.1002/pro.2368 ◽

2013 ◽

Vol 22 (11) ◽

pp. 1623-1638 ◽

Cited By ~ 46

Author(s):

Shu Yu Liao ◽

Keith J. Fritzsching ◽

Mei Hong

Keyword(s):

Solid State ◽

Conformational Analysis ◽

Influenza A Virus ◽

Solid State Nmr ◽

Influenza A ◽

Full Length ◽

M2 Protein

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2P251 Interaction of β-endorphin with a model membrane consisting of unsaturated lipids and cholesterol bilayers as studied by solid-state NMR(Native and artificial biomembranes-structure and properties,Poster Presentations)

Seibutsu Butsuri ◽

10.2142/biophys.47.s175_4 ◽

2007 ◽

Vol 47 (supplement) ◽

pp. S175

Author(s):

Emi Taniguchi ◽

Aya Harada ◽

Katsuyuki Nishimura ◽

Akira Naito

Keyword(s):

Solid State ◽

Solid State Nmr ◽

Model Membrane ◽

Structure And Properties ◽

Unsaturated Lipids ◽

Poster Presentations

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3P054 Amyloid fibril inhibition mechanism of amyloidogenic peptides as studied by solid state NMR spectroscopy(Proteins-stability, folding, and other physicochemical properties,Poster Presentations)

Seibutsu Butsuri ◽

10.2142/biophys.47.s216_3 ◽

2007 ◽

Vol 47 (supplement) ◽

pp. S216

Author(s):

Akira Naito ◽

Kengo Daidoji ◽

Hikari Itoh ◽

Izumi Yamane ◽

Izuru Kawamura

Keyword(s):

Solid State ◽

Nmr Spectroscopy ◽

Physicochemical Properties ◽

Solid State Nmr ◽

Amyloid Fibril ◽

Inhibition Mechanism ◽

Solid State Nmr Spectroscopy ◽

Amyloidogenic Peptides ◽

Poster Presentations

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3P053 Amyloidogenic fibrils and the structure of glucagon in the presence and absence of phospholipids as studied by ^C solid-state NMR(Proteins-stability, folding, and other physicochemical properties,Poster Presentations)

Seibutsu Butsuri ◽

10.2142/biophys.47.s216_2 ◽

2007 ◽

Vol 47 (supplement) ◽

pp. S216

Author(s):

Izumi Yamane ◽

Hideki Fujita ◽

Eri Yoshimoto ◽

Akira Naito

Keyword(s):

Solid State ◽

Physicochemical Properties ◽

Solid State Nmr ◽

Presence And Absence ◽

Poster Presentations

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2P239 Conformational analysis of adrenocorticotropic hormone (ACTH)bound to un-, and saturated phospholipid bilayers using solid state NMR

Seibutsu Butsuri ◽

10.2142/biophys.45.s179_3 ◽

2005 ◽

Vol 45 (supplement) ◽

pp. S179

Author(s):

H. Myoga ◽

K. Nishimura ◽

M. Narita ◽

A. Kira ◽

A. Naito

Keyword(s):

Solid State ◽

Conformational Analysis ◽

Solid State Nmr ◽

Adrenocorticotropic Hormone ◽

Phospholipid Bilayers

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Solid state NMR chemical shift assignment and conformational analysis of a cellulose binding protein facilitated by optimized glycerol enrichment

Journal of Biomolecular NMR ◽

10.1007/s10858-014-9838-y ◽

2014 ◽

Vol 59 (3) ◽

pp. 185-197 ◽

Cited By ~ 5

Author(s):

Hadar Ivanir ◽

Amir Goldbourt

Keyword(s):

Solid State ◽

Chemical Shift ◽

Conformational Analysis ◽

Solid State Nmr ◽

Binding Protein ◽

Chemical Shift Assignment ◽

Nmr Chemical Shift ◽

Cellulose Binding ◽

Shift Assignment

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Conformational analysis of steroid hormone molecules in the lipid environment – A solid-state NMR approach

Steroids ◽

10.1016/j.steroids.2011.02.005 ◽

2011 ◽

Vol 76 (6) ◽

pp. 558-563 ◽

Cited By ~ 6

Author(s):

Ping-Chen Shih ◽

Guo-Chian Li ◽

Kai-Jay Yang ◽

Wenlung Chen ◽

Der-Lii M. Tzou

Keyword(s):

Solid State ◽

Conformational Analysis ◽

Solid State Nmr ◽

Steroid Hormone ◽

Lipid Environment

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3P228 Analysis of Photoactivated pharaonis Phoborhodopsin by Solid-State NMR(Photobiology- vision and photoreception,Poster Presentations)

Seibutsu Butsuri ◽

10.2142/biophys.47.s260_1 ◽

2007 ◽

Vol 47 (supplement) ◽

pp. S260

Author(s):

Takudo Nishio ◽

Youichi Ikeda ◽

Akimori Wada ◽

Izuru Kawamura ◽

Naoki Kamo ◽

...

Keyword(s):

Solid State ◽

Solid State Nmr ◽

Poster Presentations

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3P051 Structural analyses and amyloid-like fibrillation mechanism of hCT and its mutant as studied by high-resolution ^C solid-state NMR(Proteins-stability, folding, and other physicochemical properties,Poster Presentations)

Seibutsu Butsuri ◽

10.2142/biophys.47.s215_4 ◽

2007 ◽

Vol 47 (supplement) ◽

pp. S215

Author(s):

Hikari Itoh ◽

Kengo Daidoji ◽

Miya Kamihira ◽

Akira Naito

Keyword(s):

Solid State ◽

High Resolution ◽

Physicochemical Properties ◽

Solid State Nmr ◽

Poster Presentations

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