Determination of a precise interatomic distance in a helical peptide by REDOR NMR

Marshall, Garland R.; Beusen, Denise D.; Kociolek, Karol; Redlinski, Adam S.; Lepławy, M. T.; Pan, Yong; Schaefer, Jacob

doi:10.1021/ja00159a009

Cited by 98 publications

(64 citation statements)

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“…In these REDOR experiments, the 13 C nuclei in the vicinity of 15 N nuclei lose their signals in the 13 C MAS spectrum with 13 C-15 N dipolar dephasing. In a control REDOR experiment for uniformly 13 C-and 15 N-labelled l-alanine 24 , a signal for 13 C α that is directly bonded to 15 NH 3 + decreased by 78%, compared with the control spectrum without 13 C-15 N dipolar dephasing. In the same study, signals for -CO 2 − and -CH 3 , which are two bonds away from 15 N, decreased by only 6 and 8%, respectively.…”

Section: Methodsmentioning

confidence: 90%

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Chemical structures of hydrazine-treated graphene oxide and generation of aromatic nitrogen doping

et al. 2012

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Chemically modified graphene platelets, produced via graphene oxide, show great promise in a variety of applications due to their electrical, thermal, barrier and mechanical properties. understanding the chemical structures of chemically modified graphene platelets will aid in the understanding of their physical properties and facilitate development of chemically modified graphene platelet chemistry. Here we use 13 C and 15 n solid-state nuclear magnetic resonance spectroscopy and X-ray photoelectron spectroscopy to study the chemical structure of 15 nlabelled hydrazine-treated 13 C-labelled graphite oxide and unlabelled hydrazine-treated graphene oxide, respectively. These experiments suggest that hydrazine treatment of graphene oxide causes insertion of an aromatic n 2 moiety in a five-membered ring at the platelet edges and also restores graphitic networks on the basal planes. Furthermore, density-functional theory calculations support the formation of such n 2 structures at the edges and help to elucidate the influence of the aromatic n 2 moieties on the electronic structure of chemically modified graphene platelets.

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Section: Methodsmentioning

confidence: 90%

“…The 13 C atoms associated with 15 N atoms lose their signal in the 13 C MAS spectrum with 13 C-15 N dephasing. Subtraction of Figure 2b from Figure 2a shows NMR signals of the 13 C atoms that are one or at most two bonds away from 15 N atoms 24 . The resulting difference spectrum, shown in Figure 2c, reveals a new spectral feature around 150 p.p.m.…”

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confidence: 99%

Chemical structures of hydrazine-treated graphene oxide and generation of aromatic nitrogen doping

et al. 2012

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“…Such methods promise to provide a rich source of information for the complex macromolecules in these motionally anisotropic environments (5,6). Magic-angle spinning (MAS) is frequently employed to generate the spectral resolution required in these methods, to distinguish resonances from individually labeled sites, which may then be used to yield very limited but rather precise information on spatial geometry in specific segments of the macromolecule (7,8).…”

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confidence: 99%

NMR observation of substrate in the binding site of an active sugar-H+ symport protein in native membranes.

Spooner

Rutherford²,

Watts³

et al. 1994

Proc. Natl. Acad. Sci. U.S.A.

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NMR methods have been adopted to observe directly the characteristics of substrate binding to the galactose-H+ symport protein GaIP, in its native environment, the inner membranes of Escherichia coli. Sedimented innermembrane vesicles containing the GaiP protein, overexpressed to levels above 50% of total protein, were analyzed by 13C magic-angle spinning NMR, when in their normal "fluid" state and with incorporated D-[1-'3C]glucose. Using conditions of cross-polarization intended to discriminate bound substrate alone, it was possible to detect as little as 250 nmol of substrate added to the membranes containing about 0.5 Amol (=26 mg) of GalP protein. Such-high measuring sensitivity was possible from the fluid membranes by virtue of their motional contributions to rapid relaxation recovery of the observed nuclei and due to a high-resolution response that approached the static field inhomogeneity in these experiments. This good spectral resolution showed that the native state of the membranes presents a substrate binding environment with high structural homogeneity. Inhibitors of the GaIP protein, cytochalasin B and forskolin, which are specific, and D-galactose, but not L-galactose, prevent or suppress detection of the 13C-labeled glucose substrate, confirming that the observed signal was due to specific interactions with the GalP protein. This specific substrate binding exhibits a preference for the j-anomer of D-glucose and substrate translocation is determined to be slow, on the 10-2 s time scale. The work describes a straightforward NMR approach, which achieves high sensitivity, selectivity, and resolution for nuclei associated with complex membrane proteins and which may be combined with other NMR methodologies to yield additional structural information on the binding site for the current transport system without isolating it from its native membrane environment.

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“…10, right). The REDOR difference grows to about 0.6 after only 48 rotor cycles, which indicates that most of the glycyl carbonyl labels are within 5 A (Gullion and Schaefer 1989b;Marshall et al 1990) of the cross-linked lysyl lsN-labeled side-chain. That is, the glycyl bridges must be in a compact conformation.…”

Section: Redor Of the Pentaglycyl Bridgementioning

confidence: 99%

REDOR NMR of Biological Solids: From Protein Binding Sites to Bacterial Cell Walls

Schaefer¹

1998

Recent Trends in Molecular Recognition

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Determination of a precise interatomic distance in a helical peptide by REDOR NMR

Cited by 98 publications

References 0 publications

Chemical structures of hydrazine-treated graphene oxide and generation of aromatic nitrogen doping

Chemical structures of hydrazine-treated graphene oxide and generation of aromatic nitrogen doping

NMR observation of substrate in the binding site of an active sugar-H+ symport protein in native membranes.

REDOR NMR of Biological Solids: From Protein Binding Sites to Bacterial Cell Walls

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