For interpreting the pressure induced shifts of resonance lines of folded as well as unfolded proteins the availability of data from well-defined model systems is indispensable. Here, we report the pressure dependence of 1H and 15N chemical shifts of the side chain atoms in the protected tetrapeptides Ac-Gly-Gly-Xxx-Ala-NH2 (Xxx is one of the 20 canonical amino acids) measured at 800Ā*MHz proton frequency. As observed earlier for other nuclei the chemical shifts of the side chain nuclei have a nonlinear dependence on pressure in the range from 0.1 to 200Ā*MPa. The pressure response is described by a second degree polynomial with the pressure coefficients B1 and B2 that are dependent on the atom type and type of amino acid studied. A number of resonances could be assigned stereospecifically including the 1H and 15N resonances of the guanidine group of arginine. In addition, stereoselectively isotope labeled SAIL amino acids were used to support the stereochemical assignments. The random-coil pressure coefficients are also dependent on the neighbor in the sequence as an analysis of the data shows. For HĪ± and HN correction factors for different amino acids were derived. In addition, a simple correction of compression effects in thermodynamic analysis of structural transitions in proteins was derived on the basis of random-coil pressure coefficients.
[NMR paper] A (13)C-detected (15)N double-quantum NMR experiment to probe arginine side-chain guanidinium (15)N(?) chemical shifts.
A (13)C-detected (15)N double-quantum NMR experiment to probe arginine side-chain guanidinium (15)N(?) chemical shifts.
A (13)C-detected (15)N double-quantum NMR experiment to probe arginine side-chain guanidinium (15)N(?) chemical shifts.
J Biomol NMR. 2017 Nov 10;:
Authors: Mackenzie HW, Hansen DF
Abstract
Arginine side-chains are often key for enzyme catalysis, protein-ligand and protein-protein interactions. The importance of arginine stems from the ability of the terminal guanidinium group to form many key interactions,...
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11-13-2017 12:45 AM
A 13 C-detected 15 N double-quantum NMR experiment to probe arginine side-chain guanidinium 15 N Ī· chemical shifts
A 13 C-detected 15 N double-quantum NMR experiment to probe arginine side-chain guanidinium 15 N Ī· chemical shifts
Abstract
Arginine side-chains are often key for enzyme catalysis, proteinā??ligand and proteinā??protein interactions. The importance of arginine stems from the ability of the terminal guanidinium group to form many key interactions, such as hydrogen bonds and salt bridges, as well as its perpetual positive charge. We present here an arginine 13CĪ¶-detected NMR experiment in which a double-quantum coherence involving the two 15NĪ· nuclei...
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11-10-2017 05:01 PM
Pressure dependence of side chain 13 C chemical shifts in model peptides Ac-Gly-Gly-Xxx-Ala-NH 2
Pressure dependence of side chain 13 C chemical shifts in model peptides Ac-Gly-Gly-Xxx-Ala-NH 2
Abstract
For evaluating the pressure responses of folded as well as intrinsically unfolded proteins detectable by NMR spectroscopy the availability of data from well-defined model systems is indispensable. In this work we report the pressure dependence of 13C chemical shifts of the side chain atoms in the protected tetrapeptides Ac-Gly-Gly-Xxx-Ala-NH2 (Xxx, one of the 20 canonical amino acids). Contrary to expectation the chemical shifts of a number of...
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09-14-2017 11:59 AM
Pressure dependence of backbone chemical shifts in the model peptides Ac-Gly-Gly-Xxx-Ala-NH 2
Pressure dependence of backbone chemical shifts in the model peptides Ac-Gly-Gly-Xxx-Ala-NH 2
Abstract
For a better understanding of nuclear magnetic resonance (NMR) detected pressure responses of folded as well as unstructured proteins the availability of data from well-defined model systems are indispensable. In this work we report the pressure dependence of chemical shifts of the backbone atoms 1HĪ±, 13CĪ± and 13Cā?² in the protected tetrapeptides Ac-Gly-Gly-Xxx-Ala-NH2 (Xxx one of the 20 canonical amino acids). Contrary to...
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06-22-2016 09:14 PM
Pressure response of amide one-bond J-couplings in model peptides and proteins
Pressure response of amide one-bond J-couplings in model peptides and proteins
Abstract
The pressure dependence of the one-bond indirect spinā??spin coupling constants 1 J Nā??H was studied in the protected tetrapeptides Ac-Gly-Gly-Xxx-Ala-NH2 (with Xxx being one of the 20 proteinogenic amino acids). The response of the 1 J Nā??H coupling constants is amino acid type specific, with an average...
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08-13-2014 07:49 AM
A Simple Method to Measure Protein Side-Chain MobilityUsing NMR Chemical Shifts
A Simple Method to Measure Protein Side-Chain MobilityUsing NMR Chemical Shifts
Mark V. Berjanskii and David S. Wishart
http://pubs.acs.org/appl/literatum/publisher/achs/journals/content/jacsat/0/jacsat.ahead-of-print/ja407509z/aop/images/medium/ja-2013-07509z_0003.gif
Journal of the American Chemical Society
DOI: 10.1021/ja407509z
http://feeds.feedburner.com/~ff/acs/jacsat?d=yIl2AUoC8zA
http://feeds.feedburner.com/~r/acs/jacsat/~4/qRQjRZhXxAM
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09-23-2013 09:41 PM
[NMR paper] A simple method to measure protein side-chain mobility using NMR chemical shifts.
A simple method to measure protein side-chain mobility using NMR chemical shifts.
http://www.bionmr.com//www.ncbi.nlm.nih.gov/corehtml/query/egifs/http:--pubs.acs.org-images-pubmed-acspubs.jpg Related Articles A simple method to measure protein side-chain mobility using NMR chemical shifts.
J Am Chem Soc. 2013 Sep 13;
Authors: Berjanskii MV, Wishart DS
Abstract
Protein side-chain motions are involved in many important biological processes including enzymatic catalysis, allosteric regulation, and the mediation of protein-protein,...
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09-17-2013 11:36 PM
[NMR paper] Backbone and side-chain heteronuclear resonance assignments and hyperfine NMR shifts
Backbone and side-chain heteronuclear resonance assignments and hyperfine NMR shifts in horse cytochrome c.
Related Articles Backbone and side-chain heteronuclear resonance assignments and hyperfine NMR shifts in horse cytochrome c.
Protein Sci. 2003 Sep;12(9):2104-8
Authors: Liu W, Rumbley J, Englander SW, Wand AJ
The mutant of horse heart cytochrome c was expressed in E. coli during growth on isotopically enriched minimal media. Complete resonance assignments of both the diamagnetic reduced (spin zero) and paramagnetic oxidized (spin (1/2))...
Pressure dependence of side chain 1 H and 15 N-chemical shifts in the model peptides Ac-Gly-Gly-Xxx-Ala-NH 2
Linear Mode
