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Title of Journal: J Biomol NMR

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Abbravation: Journal of Biomolecular NMR

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Springer Netherlands

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DOI

10.1016/0002-9378(48)90501-8

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1573-5001

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Complexity of aromatic ringflip motions in protei

Authors: D Krishna Rao Abani K Bhuyan
Publish Date: 2007/09/11
Volume: 39, Issue: 3, Pages: 187-196
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Abstract

Dynamics of largeamplitude conformational motions in proteins are complex and less understood although these processes are intimately associated with structure folding stability and function of proteins Here we use a large set of spectra obtained by crossrelaxation suppressed exchange NMR spectroscopy EXSY to study the 180° flipping motion of the Y97 ring of horse ferricytochrome c as a function of nearphysiological temperature in the 288–308 K range With rising temperature the ringflip rate constant makes a continuous transition from Arrhenius to antiArrhenius behavior through a narrow Arrheniuslike zone This behavior is seen not only for the native state of the protein but also for nativelike states generated by adding subdenaturing amounts of guanidine deuterochloride GdnDCl Moderately destabilizing concentrations of the denaturant 15 M GdnDCl completely removes the Arrheniuslike feature from the temperature window employed The Arrhenius to antiArrhenius transition can be explained by the heat capacity model where temperature strengthens ground state interactions perhaps hydrophobic in nature The effect of the denaturant may appear to arise from direct proteindenaturant interactions that are structurestabilizing under subdenaturing conditions The temperature distribution of rate constants under different stability conditions also suggests that the prefactor in Arrheniuslike relations is temperature dependent Although the use of the transition state theory TST offers several challenges associated with data interpretation the present results and a consideration of others published earlier provide evidence for complexity of ringflip dynamics in proteinsThis work was supported by grants from the Department of Biotechnology BRB/15/227/2001 the Department of Science Technology 4/1/2003SF and the University Grants Commission UPE Funding Government of India AKB is the recipient of a Swarnajayanti Fellowship from the DST

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  2. Statistical removal of background signals from high-throughput 1 H NMR line-broadening ligand-affinity screens
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  4. HNHC: a triple resonance experiment for correlating the H2, N1(N3) and C2 resonances in adenine nucleobases of 13 C-, 15 N-labeled RNA oligonucleotides
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  7. Selective 1 H- 13 C NMR spectroscopy of methyl groups in residually protonated samples of large proteins
  8. Fast methionine-based solution structure determination of calcium-calmodulin complexes
  9. A procedure to validate and correct the 13 C chemical shift calibration of RNA datasets
  10. Complete dissociation of the HIV-1 gp41 ectodomain and membrane proximal regions upon phospholipid binding
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  12. A rigid disulfide-linked nitroxide side chain simplifies the quantitative analysis of PRE data
  13. S3EPY: a Sparky extension for determination of small scalar couplings from spin-state-selective excitation NMR experiments
  14. Improved NMR experiments with 13 C-isotropic mixing for assignment of aromatic and aliphatic side chains in labeled proteins
  15. Out-and-back 13 C– 13 C scalar transfers in protein resonance assignment by proton-detected solid-state NMR under ultra-fast MAS
  16. Perspectives for sensitivity enhancement in proton-detected solid-state NMR of highly deuterated proteins by preserving water magnetization
  17. A probe to monitor performance of 15 N longitudinal relaxation experiments for proteins in solution
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