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Literature DB >> 16683749

Characterization of the fast dynamics of protein amino acid side chains using NMR relaxation in solution.

Tatyana I Igumenova¹, Kendra King Frederick, A Joshua Wand.

Abstract

Mesh：

Substances：
Amino Acids
Proteins

Year: 2006 PMID： 16683749 PMCID： PMC2547146 DOI： 10.1021/cr040422h

Source DB: PubMed Journal: Chem Rev ISSN： 0009-2665 Impact factor: 60.622

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102 in total

1. Temperature dependence of the internal dynamics of a calmodulin-peptide complex.

Authors: Andrew L Lee; Kim A Sharp; James K Kranz; Xiang-Jin Song; A Joshua Wand
Journal: Biochemistry Date: 2002-11-19 Impact factor: 3.162

2. Ligand-dependent dynamics and intramolecular signaling in a PDZ domain.

Authors: Ernesto J Fuentes; Channing J Der; Andrew L Lee
Journal: J Mol Biol Date: 2004-01-23 Impact factor: 5.469

3. Correlation between 2H NMR side-chain order parameters and sequence conservation in globular proteins.

Authors: Anthony Mittermaier; Alan R Davidson; Lewis E Kay
Journal: J Am Chem Soc Date: 2003-07-30 Impact factor: 15.419

4. What contributions to protein side-chain dynamics are probed by NMR experiments? A molecular dynamics simulation analysis.

Authors: Robert B Best; Jane Clarke; Martin Karplus
Journal: J Mol Biol Date: 2005-03-16 Impact factor: 5.469

Review 5. [The SAIL method: a new NMR approach for larger protection].

Authors: Takuya Torizawa; Tsutomu Terauchi; Akira Ono; Masatsune Kainosho
Journal: Tanpakushitsu Kakusan Koso Date: 2005-08

6. Protein folding and association: insights from the interfacial and thermodynamic properties of hydrocarbons.

Authors: A Nicholls; K A Sharp; B Honig
Journal: Proteins Date: 1991

7. The energy landscapes and motions of proteins.

Authors: H Frauenfelder; S G Sligar; P G Wolynes
Journal: Science Date: 1991-12-13 Impact factor: 47.728

8. Carbon relaxation in randomly fractionally 13C-enriched proteins.

Authors: A J Wand; R J Bieber; J L Urbauer; R P McEvoy; Z Gan
Journal: J Magn Reson B Date: 1995-08

9. Deuterium spin probes of side-chain dynamics in proteins. 2. Spectral density mapping and identification of nanosecond time-scale side-chain motions.

Authors: Nikolai R Skrynnikov; Oscar Millet; Lewis E Kay
Journal: J Am Chem Soc Date: 2002-06-05 Impact factor: 15.419

10. Energetics of target peptide recognition by calmodulin: a calorimetric study.

Authors: P L Wintrode; P L Privalov
Journal: J Mol Biol Date: 1997-03-14 Impact factor: 5.469

129 in total

1. Is a malleable protein necessarily highly dynamic? The hydrophobic core of the nuclear coactivator binding domain is well ordered.

Authors: Magnus Kjaergaard; Flemming M Poulsen; Kaare Teilum
Journal: Biophys J Date: 2012-04-03 Impact factor: 4.033

2. NMR dynamics investigation of ligand-induced changes of main and side-chain arginine N-H's in human phosphomevalonate kinase.

Authors: Andrew L Olson; Sheng Cai; Timothy J Herdendorf; Henry M Miziorko; Daniel S Sem
Journal: J Am Chem Soc Date: 2010-02-24 Impact factor: 15.419

Characterization of the fast dynamics of protein amino acid side chains using NMR relaxation in solution.

1. Temperature dependence of the internal dynamics of a calmodulin-peptide complex.

2. Ligand-dependent dynamics and intramolecular signaling in a PDZ domain.

3. Correlation between 2H NMR side-chain order parameters and sequence conservation in globular proteins.

4. What contributions to protein side-chain dynamics are probed by NMR experiments? A molecular dynamics simulation analysis.

Review 5. [The SAIL method: a new NMR approach for larger protection].

6. Protein folding and association: insights from the interfacial and thermodynamic properties of hydrocarbons.

7. The energy landscapes and motions of proteins.

8. Carbon relaxation in randomly fractionally 13C-enriched proteins.

9. Deuterium spin probes of side-chain dynamics in proteins. 2. Spectral density mapping and identification of nanosecond time-scale side-chain motions.

10. Energetics of target peptide recognition by calmodulin: a calorimetric study.

1. Is a malleable protein necessarily highly dynamic? The hydrophobic core of the nuclear coactivator binding domain is well ordered.

2. NMR dynamics investigation of ligand-induced changes of main and side-chain arginine N-H's in human phosphomevalonate kinase.

Review 3. Structural dynamics of bio-macromolecules by NMR: the slowly relaxing local structure approach.

4. The unusual internal motion of the villin headpiece subdomain.

Review 5. Solution NMR Spectroscopy for the Study of Enzyme Allostery.

6. Accurate determination of rates from non-uniformly sampled relaxation data.

7. Entropic origin of cobalt-carbon bond cleavage catalysis in adenosylcobalamin-dependent ethanolamine ammonia-lyase.

8. The p66 immature precursor of HIV-1 reverse transcriptase.

Review 9. NMR-based investigations into target DNA search processes of proteins.

10. Dynamically Coupled Residues within the SH2 Domain of FYN Are Key to Unlocking Its Activity.