High field 17O solid-state NMR study of alanine tripeptides

Yamauchi, Kazuo; Okonogi, Michi; Kurosu, Hiromichi; Tansho, Masataka; Shimizu, Tadashi; Gullion, Terry; Asakura, Tetsuo

doi:10.1016/j.jmr.2007.11.006

Cited by 22 publications

(18 citation statements)

References 19 publications

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“…17 O MAS spectra at 21.8 T (126 MHz) and 20 kHz MAS have been reported for two kinds of Ala-[ 17 O]Ala-Ala one with parallel (P) and the other with anti-parallel (AP) β-sheet structures [226]. The (δ iso , e 2 qQ/h and η Q ) values are (O1: 302±5 ppm, 8.7±0.5 MHz, 0.40±0.1; O2: 270±5 ppm, 8.7±0.5 MHz, 0.35±0.1) and (O1: 293±5 ppm, 8.7±0.5 MHz, 0.30±0.1; O2: 293±5 ppm, 8.7±0.5 MHz, 0.30±0.1) for P and AP β-sheet structures, respectively.…”

Section: Anisotropic Chemical Shiftsmentioning

confidence: 99%

Chemical shift tensor – The heart of NMR: Insights into biological aspects of proteins

Saitô¹,

Ando

Ramamoorthy

2010

Progress in Nuclear Magnetic Resonance Spectroscopy

181

245

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Section: Anisotropic Chemical Shiftsmentioning

confidence: 99%

Chemical shift tensor – The heart of NMR: Insights into biological aspects of proteins

Saitô¹,

Ando

Ramamoorthy

2010

Progress in Nuclear Magnetic Resonance Spectroscopy

181

245

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“…The 17 O QC constants (C Q ) for N-acyl imidazoles are between 9.1 and 10.2 MHz, consistently larger than those observed for normal amides including peptides, C Q < 9 MHz. [19][20][21][22][23][24][25][26] We also note that the asymmetry parameter ( Q ) increases slightly from Q = 0.0 in MCA-Im to Q = 0.1 in DAB-Im and to Q = 0.2 in TMB-Im (vide infra). While the C Q ( 17 O) values have never been reported for highly twisted amides in the literature, we expect that they should be similar to those observed for N-acyl imidazoles, i.e., 9 < C Q < 11 MHz.…”

Section: Crystal Structuresmentioning

confidence: 69%

“…These trends are in agreement with all previous 17 O NMR observations for carbonyl compounds. [19][20][21][22][23][24][25][26][27][28][29][30]…”

Section: Crystal Structuresmentioning

confidence: 99%

Are the amide bonds inN-acyl imidazoles twisted? A combined solid-state¹⁷O NMR, crystallographic, and computational study

et al. 2015

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We report synthesis of 17O-labeling and solid-state 17O NMR measurements of three N-acyl imidazoles of the type R-C(17O)-Im: R = p-methoxycinnamoyl (MCA-Im), R = 4-(dimethylamino)benzoyl (DAB-Im), and R = 2,4,6-trimethylbenzoyl (TMB-Im). Solid-state 17O NMR experiments allowed us to determine for the first time the 17O quadrupole coupling and chemical shift tensors in this class of organic compounds. We also determined the crystal structures of these compounds using single-crystal X-ray diffraction. The crystal structures show that, while the C(O)–N amide bond in DAB-Im exhibits a small twist, those in MCA-Im and TMB-Im are essentially planar. We found that, in these N-acyl imidazoles, the 17O quadrupole coupling and chemical shift tensors depend critically on the torsion angle between the conjugated acyl group and the C(O)–N amide plane. The computational results from a plane-wave DFT approach, which takes into consideration the entire crystal lattice, are in excellent agreement with the experimental solid-state 17O NMR results. Quantum chemical computations also show that the dependence of 17O NMR parameters on the Ar–C(O) bond rotation is very similar to that previously observed for the C(O)–N bond rotation in twisted amides. We conclude that one should be cautious in linking the observed NMR chemical shifts only to the twist of the C(O)–N amide bond.

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“…Polyalanine peptides have been reported to adopt a variety of conformations like right handed α-helix, β-sheet/ β-strand, PPII helix and random coil [20]- [24]. Alanine is a simple amino acid with methyl group as side chain and has highest propensity to form right handed helix [25].…”

Section: Resultsmentioning

confidence: 99%

Gly→Ala Point Mutation and Conformation of Poly-Ala Stretch of PABPN1: A Molecular Dynamics Study

Shafique¹,

Garg²,

Nandel³

2015

JBPC

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Single nucleotide replacing mutations in genes cause a number of diseases, but sometimes these mutations mimic other genetic mutations such as trinucleotide repeats expansions. A mutation in codon GGG→GCG results in Gly→Ala at the N-terminal of PABPN1 protein that mimics the trinucleotide repeat expansion disease called Oculopharyngeal muscular dystrophy (OPMD). Molecular dynamics simulations in water with peptide models having sequence Ac-A10-GA2GG-NHme (peptide A) and Ac-A10A3GG-NHme (peptide B) reveal an increase in the length of helical segment in peptide B. The α-helical length is found to be stable in peptide B with starting geometry of a right handed helix, while in the case peptide A, the helical length is short. The interactions of water molecules at terminals, side chain-backbone interactions and hydrogen bonds provide stability to resultant conformation. The adopted helix by the poly-Ala stretch may lead to masking some other active parts of the PABPN1 that may trigger the aggregation, decrease in degradation and/or impaired function of protein. Hence, further studies with N-terminal may be helpful to understand unclear disease mechanism.

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High field 17O solid-state NMR study of alanine tripeptides

Cited by 22 publications

References 19 publications

Chemical shift tensor – The heart of NMR: Insights into biological aspects of proteins

Chemical shift tensor – The heart of NMR: Insights into biological aspects of proteins

Are the amide bonds inN-acyl imidazoles twisted? A combined solid-state¹⁷O NMR, crystallographic, and computational study

Gly→Ala Point Mutation and Conformation of Poly-Ala Stretch of PABPN1: A Molecular Dynamics Study

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High field 17O solid-state NMR study of alanine tripeptides

Cited by 22 publications

References 19 publications

Chemical shift tensor – The heart of NMR: Insights into biological aspects of proteins

Chemical shift tensor – The heart of NMR: Insights into biological aspects of proteins

Are the amide bonds inN-acyl imidazoles twisted? A combined solid-state17O NMR, crystallographic, and computational study

Gly→Ala Point Mutation and Conformation of Poly-Ala Stretch of PABPN1: A Molecular Dynamics Study

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Are the amide bonds inN-acyl imidazoles twisted? A combined solid-state¹⁷O NMR, crystallographic, and computational study