Carbon-13-NMR of peptides and proteins

Howarth, Oliver W.; Lilley, David M.J.

doi:10.1016/0079-6565(78)80001-6

Cited by 189 publications

(110 citation statements)

References 254 publications

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“…The prolines are in the trans conformation; this is evidenced by their CH" resonance position at 4.40 ppm (Table 1) and the 13CY at 26.3 ppm (not shown), which are typical values found for truns prolines (Howarth & Lilley, 1978;Dyson et al, 1988). The temperature dependence of amide resonances provides information about their involvement in hydrogen bond formation (Ohnishi & Urry, 1969); a free amide will have a temperature coefficient of -9 ppb/K, whereas values of -4 ppb/K or higher indicate hydrogen bond involvement.…”

Section: Turn Prediction In the Peptidesmentioning

confidence: 92%

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Structure characterization of the central repetitive domain of high molecular weight gluten proteins. I. Model studies using cyclic and linear peptides

et al. 1997

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The high molecular weight (HMW) proteins from wheat contain a repetitive domain that forms 60‐80% of their sequence. The consensus peptides PGQGQQ and GYYPTSPQQ form more than 90% of the domain; both are predicted to adopt /3‐turn structure. This paper describes the structural characterization of these consensus peptides and forms the basis for the structural characterization of the repetitive HMW domain, described in the companion paper. The cyclic peptides cyclo‐[PGQGQQPGQGQQ] (peptide 1), cyclo‐[GYYPTSPQQGA] (peptide 2), and cyclo‐[PGQGQQGYYPTSPQQ] (peptide 3) were prepared using a novel synthesis route. In addition, the linear peptides (PGQGQQ) (n = 1, 3, 5) were prepared. CD, FTIR, and NMR data demonstrated a type II /3‐turn structure at QPGQ in the cyclic peptide 1 that was also observed in the linear peptides (PGQGQQ). A type I /3‐turn was observed at YPTS and SPQQ in peptides 2 and 3, with additional /3‐turns of either type I or II at GAGY (peptide 2) and QQGY (peptide 3). The proline in YPTS showed considerable cis/trans isomerization, with up to 50% of the population in the cis‐conformation; the other prolines were more than 90% in the trans conformation. The conversion from trans to cis destroys the type I /3‐turn at YPTS, but leads to an increase in turn character at SPQQ and GAGY (peptide 2) or QQGY (peptide 3).

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Section: Turn Prediction In the Peptidesmentioning

confidence: 92%

“…given in Table 3), again indicating trandcis isomerization (Howarth & Lilley, 1978); the "Cy resonance of P7 is at 25.9 pprn in both conformations (not given in Table 3). The two conformations therefore originate from P4 cidtrans isomerization and will be referred to as the cis and trans conformation.…”

Section: Conformation Of Cyclo-gyyptspqqga (Peptide 2)mentioning

confidence: 99%

Structure characterization of the central repetitive domain of high molecular weight gluten proteins. I. Model studies using cyclic and linear peptides

et al. 1997

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“…The specific assignment was made using the difference in intensities to these haem methyl groups and confirmed via the carbon shifts measured from the HMQC spectrum (2,6CH -128.22ppm and 3,5CH -114.52 ppm) which are characteristic (Howarth and Lilley, 1978; Fig. 2).…”

Section: Resultsmentioning

confidence: 99%

Use of Paramagnetic NMR Probes for Structural Analysis in Cytochrome c₃ from Desulfovibrio Vulgaris

Salgueiro

Turner

Xavier

1997

European Journal of Biochemistry

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The dipolar field generated by each of the four haems in the tetrahaem ferricytochrome c, from Desulfovibrio vulgaris (Hildenborough) (c,DvH) is determined by means of a novel procedure. In this method the I3C chemical shifts of the nuclei directly bound to the haems are used to determine the inplane orientations of the rhombic perturbation in each of the four haems with respect to a model of molecular orbitals of e, symmetry which are subject to a rhombic perturbation [Turner, D. L., Salgueiro, C. A., Schenkels, P., LeGall, J. & Xavier, A. ) Biochim. Biophys. Acta 1246. These orientations, together with the components of the magnetic susceptibility tensors obtained from the EPR g values and the crystal structure of c,DvH, can be used to calculate the dipolar shifts induced by each haem throughout the protein. Thus the observed 13C paramagnetic shifts of the c,DvH haem substituents were fitted considering both the pseudocontact and contact shifts of each haem simultaneously. The dipolar shifts calculated by this method were tested against the observed dipolar shifts for some amino acid residues strategically placed in the protein and also for the haem propionate groups. The effect of considering the calculated dipolar extrinsic shifts on the behaviour of the chemical shifts of the haem methyl groups in the intermediate stages of oxidation at different pH values was also analysed. The several tests applied to the calculated dipolar shifts have shown that the method is extremely useful for predicting chemical shifts as an aid to complete proton assignment, and to add further constraints in the refinement of solution structures of paramagnetic proteins and hence to probe subtle structural rearrangements around the haem pocket.

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“…Random coil values obtained from linear hexapeptides in 1M urea at pH 5.0 and 25 C 56 were used to calculate Ca secondary shifts, using the values for protonated glutamate and aspartate. 57 …”

Section: Nmr Spectroscopymentioning

confidence: 99%

Charge neutralization and collapse of the C‐terminal tail of alpha‐synuclein at low pH

2009

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Alpha-synuclein (aS) is the primary component of Lewy bodies, the pathological hallmark of Parkinson's Disease. Aggregation of aS is thought to proceed from a primarily disordered state with nascent secondary structure through intermediate conformations to oligomeric forms and finally to mature amyloid fibrils. Low pH conditions lead to conformational changes associated with increased aS fibril formation. Here we characterize these structural and dynamic changes using solution state NMR measurements of secondary chemical shifts, relaxation parameters, residual dipolar couplings, and paramagnetic relaxation enhancement. We find that the neutralization of negatively charged side-chains eliminates electrostatic repulsion in the C-terminal tail of aS and leads to a collapse of this region at low pH. Hydrophobic contacts between the compact C-terminal tail and the NAC (non-amyloid-b component) region are maintained and may lead to the formation of a globular domain. Transient long-range contacts between the C-terminus of the protein and regions N-terminal to the NAC region are also preserved. Thus, the release of long-range contacts does not play a role in the increased aggregation of aS at low pH, which we instead attribute to the increased hydrophobicity of the protein.

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Carbon-13-NMR of peptides and proteins

Cited by 189 publications

References 254 publications

Structure characterization of the central repetitive domain of high molecular weight gluten proteins. I. Model studies using cyclic and linear peptides

Structure characterization of the central repetitive domain of high molecular weight gluten proteins. I. Model studies using cyclic and linear peptides

Use of Paramagnetic NMR Probes for Structural Analysis in Cytochrome c₃ from Desulfovibrio Vulgaris

Charge neutralization and collapse of the C‐terminal tail of alpha‐synuclein at low pH

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Carbon-13-NMR of peptides and proteins

Cited by 189 publications

References 254 publications

Structure characterization of the central repetitive domain of high molecular weight gluten proteins. I. Model studies using cyclic and linear peptides

Structure characterization of the central repetitive domain of high molecular weight gluten proteins. I. Model studies using cyclic and linear peptides

Use of Paramagnetic NMR Probes for Structural Analysis in Cytochrome c3 from Desulfovibrio Vulgaris

Charge neutralization and collapse of the C‐terminal tail of alpha‐synuclein at low pH

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Use of Paramagnetic NMR Probes for Structural Analysis in Cytochrome c₃ from Desulfovibrio Vulgaris