Long-Lived States to Monitor Protein Unfolding by Proton NMR.
Chemphyschem. 2011 Aug 31;
Authors: Bornet A, Ahuja P, Sarkar R, Fernandes L, Hadji S, Lee SY, Haririnia A, Fushman D, Bodenhausen G, Vasos PR
Abstract
The relaxation of long-lived states (LLS) corresponds to the slow return to statistical thermal equilibrium between symmetric and antisymmetric proton spin states. This process is remarkably sensitive to the presence of external spins and can be used to obtain information about partial unfolding of proteins. We detected the appearance of a destabilized conformer of ubiquitin when urea is added to the protein in its native state. This conformer shows increased mobility in the C-terminus, which significantly extends the lifetimes of proton LLS magnetisation in Ser-65. These changes could not be detected by conventional measurements of T(1) and T(2) relaxation times of protons, and would hardly be sensed by carbon-13 or nitrogen-15 relaxation measurements. Conformers with similar dynamic and structural features, as revealed by LLS relaxation times, could be observed, in the absence of urea, in two ubiquitin mutants, L67S and L69S.
PMID: 21882334 [PubMed - as supplied by publisher]
In-cell NMR in E. coli to Monitor Maturation Steps of hSOD1.
In-cell NMR in E. coli to Monitor Maturation Steps of hSOD1.
In-cell NMR in E. coli to Monitor Maturation Steps of hSOD1.
PLoS One. 2011;6(8):e23561
Authors: Banci L, Barbieri L, Bertini I, Cantini F, Luchinat E
Abstract
In-cell NMR allows characterizing the folding state of a protein as well as posttranslational events at molecular level, in the cellular context. Here, the initial maturation steps of human copper, zinc superoxide dismutase 1 are characterized in the E. coli cytoplasm by in-cell NMR: from the apo protein, which is...
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Ultra High-Resolution NMR: Sustained Induction Decays of Long-Lived Coherences
Ultra High-Resolution NMR: Sustained Induction Decays of Long-Lived Coherences
Aure?lien Bornet, Sami Jannin, J. A. (Ton) Konter, Patrick Hautle, Ben van den Brandt and Geoffrey Bodenhausen
http://pubs.acs.org/appl/literatum/publisher/achs/journals/content/jacsat/0/jacsat.ahead-of-print/ja2052792/aop/images/medium/ja-2011-052792_0005.gif
Journal of the American Chemical Society
DOI: 10.1021/ja2052792
http://feeds.feedburner.com/~ff/acs/jacsat?d=yIl2AUoC8zA
http://feeds.feedburner.com/~r/acs/jacsat/~4/F3VMiSJp4h4
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[NMR paper] A high-resolution NMR study of long-lived water molecules in both oxidation states of
A high-resolution NMR study of long-lived water molecules in both oxidation states of a minimal cytochrome c.
Related Articles A high-resolution NMR study of long-lived water molecules in both oxidation states of a minimal cytochrome c.
Biochemistry. 2003 Apr 1;42(12):3457-63
Authors: Bertini I, Ghosh K, Rosato A, Vasos PR
The interaction of water with oxidized and reduced cytochrome c from the Gram-positive bacterium Bacillus pasteurii (a 71-amino acid long monoheme cytochrome) is investigated through CLEANEX experiments and (15)N-edited...
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11-24-2010 09:01 PM
[NMR paper] Mechanical unfolding of a titin Ig domain: structure of unfolding intermediate reveal
Mechanical unfolding of a titin Ig domain: structure of unfolding intermediate revealed by combining AFM, molecular dynamics simulations, NMR and protein engineering.
Related Articles Mechanical unfolding of a titin Ig domain: structure of unfolding intermediate revealed by combining AFM, molecular dynamics simulations, NMR and protein engineering.
J Mol Biol. 2002 Sep 27;322(4):841-9
Authors: Fowler SB, Best RB, Toca Herrera JL, Rutherford TJ, Steward A, Paci E, Karplus M, Clarke J
The mechanical unfolding of an immunoglobulin domain from the...
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Long-Lived Coherences for Line-Narrowing in High-Field NMR
Long-Lived Coherences for Line-Narrowing in High-Field NMR
Publication year: 2010
Source: Progress in Nuclear Magnetic Resonance Spectroscopy, In Press, Accepted Manuscript, Available online 21 October 2010</br>
Riddhiman, Sarkar , Puneet, Ahuja , Paul R., Vasos , Aurélien, Bornet , Olivier, Wagnières , ...</br>
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10-22-2010 07:34 AM
NMR methods to monitor the enzymatic depolymerization of heparin.
NMR methods to monitor the enzymatic depolymerization of heparin.
http://www.ncbi.nlm.nih.gov/corehtml/query/egifs/http:--production.springer.de-OnlineResources-Logos-springerlink.gif Related Articles NMR methods to monitor the enzymatic depolymerization of heparin.
Anal Bioanal Chem. 2010 Sep 4;
Authors: Limtiaco JF, Beni S, Jones CJ, Langeslay DJ, Larive CK
Heparin and the related glycosaminoglycan, heparan sulfate, are polydisperse linear polysaccharides that mediate numerous biological processes due to their interaction with proteins....
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09-05-2010 05:53 AM
[NMR paper] Thermodynamics of unfolding of ribonuclease A under high pressure. A study by proton
Thermodynamics of unfolding of ribonuclease A under high pressure. A study by proton NMR.
http://www.ncbi.nlm.nih.gov/corehtml/query/egifs/http:--linkinghub.elsevier.com-ihub-images-PubMedLink.gif Related Articles Thermodynamics of unfolding of ribonuclease A under high pressure. A study by proton NMR.
J Mol Biol. 1995 Jul 28;250(5):689-94
Authors: Yamaguchi T, Yamada H, Akasaka K
Thermodynamic stability of ribonuclease A (6.2 mM pH 1.0, 0.15 M KCl, in 2H2O) has been studied in the pressure range of 1 to 2000 atm and in the temperature range...
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Long-Lived Coherences for Homogeneous Line Narrowing in Spec
Long-Lived Coherences for Homogeneous Line Narrowing in Spec
Physical Review Letters publication on application of long-lived coherences to line-narrowing in NMR by Dr. Geoffrey Bodenhausen and his group.
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Long-Lived States to Monitor Protein Unfolding by Proton NMR.
Linear Mode
