Related ArticlesConformation and backbone dynamics of bacteriorhodopsin revealed by (13)C-NMR.
Biochim Biophys Acta. 2000 Aug 30;1460(1):39-48
Authors: Saitô H, Tuzi S, Yamaguchi S, Tanio M, Naito A
It is demonstrated here how the secondary structure and dynamics of transmembrane helices, as well as surface residues, such as interhelical loops and N- or C-terminus of bacteriorhodopsin (bR) in purple membrane, can be determined at ambient temperature based on very simple (13)C-NMR measurements, together with a brief experimental background. In contrast to the static picture of bR, currently available from X-ray diffraction or cryo-electron microscopy, the structure consists of dynamically heterogeneous domains which undergo various types of local fluctuations with a frequency range of 10(2)--10 (8) Hz. The significance of this picture is discussed in relation to the biological function of this protein.
[NMR paper] Dynamic aspect of bacteriorhodopsin as a typical membrane protein as revealed by site
Dynamic aspect of bacteriorhodopsin as a typical membrane protein as revealed by site-directed solid-state 13C NMR.
Related Articles Dynamic aspect of bacteriorhodopsin as a typical membrane protein as revealed by site-directed solid-state 13C NMR.
Solid State Nucl Magn Reson. 2004 Jan;25(1-3):5-14
Authors: Saitô H, Yamaguchi S, Okuda H, Shiraishi A, Tuzi S
We demonstrate here a general feature of dynamic aspect of membrane proteins as revealed by site-directed 13C NMR studies on bacteriorhodopsin (bR) as a typical membrane protein and a...
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[NMR paper] Riboflavin synthase of Schizosaccharomyces pombe. Protein dynamics revealed by 19F NM
Riboflavin synthase of Schizosaccharomyces pombe. Protein dynamics revealed by 19F NMR protein perturbation experiments.
Related Articles Riboflavin synthase of Schizosaccharomyces pombe. Protein dynamics revealed by 19F NMR protein perturbation experiments.
BMC Biochem. 2003 Dec 23;4:18
Authors: Fischer M, Schott AK, Kemter K, Feicht R, Richter G, Illarionov B, Eisenreich W, Gerhardt S, Cushman M, Steinbacher S, Huber R, Bacher A
BACKGROUND: Riboflavin synthase catalyzes the transformation of 6,7-dimethyl-8-ribityllumazine into riboflavin in...
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[NMR paper] Alteration of conformation and dynamics of bacteriorhodopsin induced by protonation o
Alteration of conformation and dynamics of bacteriorhodopsin induced by protonation of Asp 85 and deprotonation of Schiff base as studied by 13C NMR.
Related Articles Alteration of conformation and dynamics of bacteriorhodopsin induced by protonation of Asp 85 and deprotonation of Schiff base as studied by 13C NMR.
Biochemistry. 2000 Nov 28;39(47):14472-80
Authors: Kawase Y, Tanio M, Kira A, Yamaguchi S, Tuzi S, Naito A, Kataoka M, Lanyi JK, Needleman R, Saitô H
According to previous X-ray diffraction studies, the D85N mutant of...
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[NMR paper] DNA bending and sequence-dependent backbone conformation NMR and computer experiments
DNA bending and sequence-dependent backbone conformation NMR and computer experiments.
Related Articles DNA bending and sequence-dependent backbone conformation NMR and computer experiments.
Eur J Biochem. 1999 Oct 1;265(1):35-53
Authors: Ojha RP, Dhingra MM, Sarma MH, Shibata M, Farrar M, Turner CJ, Sarma RH
Although DNA bending plays a crucial role in several biological processes, very little is known experimentally about the relationship between sugar phosphate conformation and sequence directed bending. In this paper, we determine the...
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[NMR paper] Phospholipid headgroup dynamics in DOPG-d5-cytochrome c complexes as revealed by 2H a
Phospholipid headgroup dynamics in DOPG-d5-cytochrome c complexes as revealed by 2H and 31P NMR: the effects of a peripheral protein on collective lipid fluctuations.
http://www.ncbi.nlm.nih.gov/corehtml/query/egifs/http:--linkinghub.elsevier.com-ihub-images-PubMedLink.gif Related Articles Phospholipid headgroup dynamics in DOPG-d5-cytochrome c complexes as revealed by 2H and 31P NMR: the effects of a peripheral protein on collective lipid fluctuations.
Solid State Nucl Magn Reson. 1997 Mar;8(1):55-64
Authors: Pinheiro TJ, Duer MJ, Watts A
The...
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[NMR paper] Phospholipid headgroup dynamics in DOPG-d5-cytochrome c complexes as revealed by 2H a
Phospholipid headgroup dynamics in DOPG-d5-cytochrome c complexes as revealed by 2H and 31P NMR: the effects of a peripheral protein on collective lipid fluctuations.
http://www.ncbi.nlm.nih.gov/corehtml/query/egifs/http:--linkinghub.elsevier.com-ihub-images-PubMedLink.gif Related Articles Phospholipid headgroup dynamics in DOPG-d5-cytochrome c complexes as revealed by 2H and 31P NMR: the effects of a peripheral protein on collective lipid fluctuations.
Solid State Nucl Magn Reson. 1997 Mar;8(1):55-64
Authors: Pinheiro TJ, Duer MJ, Watts A
The...
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High-Resolution MAS NMR Analysis of PI3-SH3 Amyloid Fibrils: Backbone Conformation an
High-Resolution MAS NMR Analysis of PI3-SH3 Amyloid Fibrils: Backbone Conformation and Implications for Protofilament Assembly and Structure
http://pubs.acs.org//appl/literatum/publisher/achs/journals/content/bichaw/0/bichaw.ahead-of-print/bi100864t/aop/images/medium/bi-2010-00864t_0004.gifBiochemistry, Volume 0, Issue 0, Articles ASAP (As Soon As Publishable).
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High-Resolution MAS NMR Analysis of PI3-SH3 Amyloid Fibrils: Backbone Conformation an
High-Resolution MAS NMR Analysis of PI3-SH3 Amyloid Fibrils: Backbone Conformation and Implications for Protofilament Assembly and Structure .
Related Articles High-Resolution MAS NMR Analysis of PI3-SH3 Amyloid Fibrils: Backbone Conformation and Implications for Protofilament Assembly and Structure .
Biochemistry. 2010 Aug 13;
Authors: Bayro MJ, Maly T, Birkett NR, Macphee CE, Dobson CM, Griffin RG
The SH3 domain of the PI3 kinase (PI3-SH3 or PI3K-SH3) readily aggregates into fibrils in vitro and has served as an important model system in the...