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Literature DB >> 22911008

Study of protein dynamics in solution by measurement of (13)C (α)- (13)CO NOE and (13)CO longitudinal relaxation.

Abstract

(13)C(α)-(13)CO homonuclear NOE and (13)CO T(1) relaxation were measured for a 20 kDa protein using tripleresonance pulse sequences. The experiments were sufficiently sensitive to obtain statistically significant differences in relaxation parameters over the molecule. The (13)C(α)-(13)CO cross-relaxation rate, obtained from these data, is directly proportional to an order parameter describing local motion and it is largely independent of the local correlation time. It is therefore a relatively straightforward observable for the identification of local dynamics.

Year: 1996 PMID： 22911008 DOI： 10.1007/BF00203826

Source DB: PubMed Journal: J Biomol NMR ISSN： 0925-2738 Impact factor: 2.835

11 in total

1. Structure of bacteriophage T4 lysozyme refined at 1.7 A resolution.

Authors: L H Weaver; B W Matthews
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Authors: G Barbato; M Ikura; L E Kay; R W Pastor; A Bax
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3. Dynamics of methyl groups in proteins as studied by proton-detected 13C NMR spectroscopy. Application to the leucine residues of staphylococcal nuclease.

Authors: L K Nicholson; L E Kay; D M Baldisseri; J Arango; P E Young; A Bax; D A Torchia
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4. 15N, 13C, and 1H NMR assignments and secondary structure for T4-lysozyme.

Authors: M W Fischer; A Majumdar; F W Dahlquist; E R Zuiderweg
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5. Backbone dynamics of a two-domain protein: 15N relaxation studies of the amino-terminal fragment of urokinase-type plasminogen activator.

Authors: A P Hansen; A M Petros; R P Meadows; S W Fesik
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Authors: R Brüschweiler; X Liao; P E Wright
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8. Determination of (13)C (α) relaxation times in uniformly (13)C/ (15)N-enriched proteins.

Authors: J Engelke; H Rüterjans
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9. Backbone dynamics of proteins as studied by 15N inverse detected heteronuclear NMR spectroscopy: application to staphylococcal nuclease.

Authors: L E Kay; D A Torchia; A Bax
Journal: Biochemistry Date: 1989-11-14 Impact factor: 3.162

10. A novel approach for sequential assignment of 1H, 13C, and 15N spectra of proteins: heteronuclear triple-resonance three-dimensional NMR spectroscopy. Application to calmodulin.

Authors: M Ikura; L E Kay; A Bax
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Authors: A L Lee; A J Wand
Journal: J Biomol NMR Date: 1999-02 Impact factor: 2.835

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Authors: Fabien Ferrage; Philippe Pelupessy; David Cowburn; Geoffrey Bodenhausen
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Review 4. NMR studies of dynamic biomolecular conformational ensembles.

Authors: Dennis A Torchia
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6. Characterizing semilocal motions in proteins by NMR relaxation studies.

Authors: M W Fischer; L Zeng; A Majumdar; E R Zuiderweg
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7. Measurement of (13)C (α)- (13)CO cross-relaxation rates in (15)N-/ (13)C-labelled proteins.

Authors: F Cordier; B Brutscher; D Marion
Journal: J Biomol NMR Date: 1996-03 Impact factor: 2.835

8. Backbone dynamics of proteins derived from carbonyl carbon relaxation times at 500, 600 and 800 MHz: Application to ribonuclease T1.

Authors: J Engelke; H Rüterjans
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9. Model selection for the interpretation of protein side chain methyl dynamics.

Authors: Wing-Yiu Choy; Lewis E Kay
Journal: J Biomol NMR Date: 2003-04 Impact factor: 2.835

10. Side chain dynamics monitored by 13C-13C cross-relaxation.

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