Hydrogen-bonding effect on carbon-13 NMR chemical shifts of L-alanine residue carbonyl carbons of peptides in the solid state

Asakawa, Naoki; Kuroki, Shigeki; Kurosu, Hiromichi; Ando, Isao; Shoji, Akira; Ozaki, Takuo

doi:10.1021/ja00035a016

Cited by 138 publications

(120 citation statements)

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“…We formulated a simple model for the C' CSA, which depends only on the isotropic chemical shift, d iso . [16] [16] is notably improved in comparison with previous proposals, [17,18] and is supported by a recent analysis of experimental CCR rates, although local anisotropic motion was not explicitly considered in this study. [12] We also found that the orientation of the shift tensor is site-specific with the average a angle (the angle between x 11 and the C'ÀN bond; Figure 1) varying from 228-468.…”

supporting

confidence: 80%

Local Structure and Anisotropic Backbone Dynamics from Cross‐Correlated NMR Relaxation in Proteins

2005

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The molecular function of biomacromolecules is determined by both their 3D structure and conformational dynamics. NMR cross-correlated relaxation (CCR) contains information about local structure and local anisotropic dynamics. CCR arises from the interference of two relaxation mechanisms such as chemical shift anisotropy (CSA) and dipoledipole (DD) interactions, which are described by tensors in 3D space, and contains information about the relative orientation of these tensors and their correlated motion. [1][2][3][4] In this respect, CCR rates involving CSA tensors are most useful, as they sample local structure and dynamics along three orthogonal axes. Over the past few years, numerous NMR experiments have been designed to measure crosscorrelated relaxation rates to determine local molecular geometry, [3,5] to study local dynamics, [6][7][8][9] and to characterize chemical-shift tensors in solution.[10-12] Different models of anisotropic local motion of the peptide plane have been discussed. [7,9,[13][14][15] Whereas CCR processes in principle contain an enormous amount of information, the interpretation of these relaxation rates must be treated with great care. For example, a CSA/DD relaxation process depends on many factors, including the local molecular structure, the magnitude of the CSA and orientation of the shift tensor in the fixed molecular frame, and local anisotropic dynamics.[2] To simplify this problem, the magnitude of the CSA and orientation of the shift tensor, both of which are difficult to access experimentally and theoretically, are often treated as fixed invariable parameters. Alternatively, the effect of dynamics is included through a generalized (isotropic) order parameter, which represents a considerable simplification to the complex hierarchy of internal anisotropic dynamic modes that characterize the local motion of the peptide plane. Recently, the vector fluctuations of N À H and C'ÀC a bonds were monitored by studying the temperature dependence of cross-correlated relaxation rates rather than their absolute values, thereby diminishing the influence of uncertainties in CSA parameters.

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supporting

confidence: 80%

Local Structure and Anisotropic Backbone Dynamics from Cross‐Correlated NMR Relaxation in Proteins

2005

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“…For example, in both acetamide and thioacetamide, the group 16 atom is involved in two asymmetric hydrogen bonds with neighbouring molecules (25b, 31), unlike the case for acetanilide where a single intermolecular hydrogen bond exists (30). Previous experimental and theoretical work has suggested the component of the carbonyl carbon CS tensor most sensitive to hydrogen bonding to be the component lying nearest the carbonyl bond axis, the intennediately shielded component, 822 (19,33 hydrogen bond strength. Consequently, differences in the hydrogen bonding networks may partially account for the observed deshielding of 6,, in acetainide relative to the acetanilides.…”

Section: (Ii) Results For Thi~acetanilide-'~~'~~(~~)mentioning

confidence: 99%

A solid-state ¹³C NMR and theoretical investigation of carbonyl and thiocarbonyl carbon chemical shift tensors

Kirby¹,

Lumsden²,

Wasylishen³

1995

Can. J. Chem.

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The carbon chemical shift tensors of the carbonyl and thiocarbonyl groups of acetamide, thioacetamide, thioacetanilide, 4'-methoxyacetanilide, and 4'-methoxythioacetanilide have been experimentally determined using dipolar -chemical shift solid-state 13c NMR spectroscopy. The magnitudes of the three principal components of the carbon chemical shift tensors are found to exhibit marked variations between the carbonyl and thiocarbonyl functionalities. However, in contrast to the conclusions of an earlier comparative investigation involving benzophenone and thiobenzophenone, the orientations of the principal axis systems of these chemical shift tensors are found to be similar. These experimental results represent the first complete characterizations of the carbon chemical shift tensor in organic thiocarbonyls. The results of our ab initio GIAO and LORG calculations of carbon chemical shielding tensors in formaldehyde, thiofomaldehyde, formamide, and thioformamide as well as in acetamide and thioacetamide are in qualitative agreement with experiment. The findings of the present investigation provide conclusive evidence that the well-known isotropic deshielding of the carbon nucleus in the C=S group relative to C=O is primarily attributable to the decreased energy associated with the o tt T* excitation within the thiocarbonyl fragment. This result is in contrast with the conventional interpretation that the deshielding originates from a red shift in the C=S HOMO-LUMO n + T* transition.Key words: chemical shift tensors, solid-state I3C NMR, carbonyls, thiocarbonyls, ab initio calculations.RksumC : Utilisant les deplacements chimiques dipolaires de la spectroscopie RMN du I3c 2i I'ttat solide, on a determine exptrimentalement les tenseurs des dtplacements chimiques du carbone des groupes carbonyle et thiocarbonyle des acttamide, thioacetamide, thioacttanilide, 4'-mCthoxyacCtanilide et 4'-mCthoxythioacttanilide. On a trouvt que les amplitudes des trois principales composantes des tenseurs des dtplacements chimiques du carbone presentent des variations importantes entre les fonctions carbonyles et thiocarbonyles. Toutefois, en opposition avec les conclusions tirkes 2i partir d'une ttude comparative anttrieure impliquant la benzophenone et la thiobenzophtnone, on a trouvt que les orientations des principaux axes de rtftrence de ces tenseurs des dCsplacements chimiques sont semblables. Ces resultats exptrimentaux representent les premihres caractkrisations complktes du tenseur du dtplacement chimique des thiocarbonyles organiques. Les rtsultats de nos calculs ab initio GIAO et LORG des tenseurs d'tcran chimique du carbone dans les formaldthyde, thiofomaldChyde, formamide, thiofomamide ainsi qu'acttamide et thioacttamide sont en accord qualitatif avec les rtsultats expCrimentaux. Les observations faites dans le present travail fournissent des bases concluantes qui permettent d'attribuer le deblindage bien connu du noyau du carbone dans le groupe C=S par rapport au C=O 2i une diminution de l'energie associee B une e...

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“…For this reason, we have studied NMR methodologies for obtaining information about the hydrogen-bonded structure of peptides and polypeptides in the solid state through the observation of solid state NMR chemical shifts. Then, we have elucidated the relationship between the hydrogen-bond lengths and solid state NMR chemical shifts of 13 C [4][5][6][7][8], 15 N [9,10] and 17 O [11][12][13] nuclei from the experimental and theoretical aspects. From these systematic works, it has been obtained that the observation of the main-chain chemical shifts leads to the determination of the hydrogen-bond length in solid peptides and polypeptides including proteins.…”

Section: Introductionmentioning

confidence: 99%

Proton NMR Chemical Shift Behavior of Hydrogen-Bonded Amide Proton of Glycine-Containing Peptides and Polypeptides as Studied by ab initio MO Calculation

Hori

Yamauchi

Kuroki

et al. 2002

IJMS

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Hydrogen-bonding effect on carbon-13 NMR chemical shifts of L-alanine residue carbonyl carbons of peptides in the solid state

Cited by 138 publications

References 0 publications

Local Structure and Anisotropic Backbone Dynamics from Cross‐Correlated NMR Relaxation in Proteins

Local Structure and Anisotropic Backbone Dynamics from Cross‐Correlated NMR Relaxation in Proteins

A solid-state ¹³C NMR and theoretical investigation of carbonyl and thiocarbonyl carbon chemical shift tensors

Proton NMR Chemical Shift Behavior of Hydrogen-Bonded Amide Proton of Glycine-Containing Peptides and Polypeptides as Studied by ab initio MO Calculation

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Hydrogen-bonding effect on carbon-13 NMR chemical shifts of L-alanine residue carbonyl carbons of peptides in the solid state

Cited by 138 publications

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Local Structure and Anisotropic Backbone Dynamics from Cross‐Correlated NMR Relaxation in Proteins

Local Structure and Anisotropic Backbone Dynamics from Cross‐Correlated NMR Relaxation in Proteins

A solid-state 13C NMR and theoretical investigation of carbonyl and thiocarbonyl carbon chemical shift tensors

Proton NMR Chemical Shift Behavior of Hydrogen-Bonded Amide Proton of Glycine-Containing Peptides and Polypeptides as Studied by ab initio MO Calculation

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A solid-state ¹³C NMR and theoretical investigation of carbonyl and thiocarbonyl carbon chemical shift tensors