Solid-state NMR detection of 14N-13C dipolar couplings between amino acid side groups provides constraints on amyloid fibril architecture

Chemistry

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https://doi.org/10.1002/mrc.2708
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Keywords

Amyloid, Carbon Isotopes, Molecular Structure, Nitrogen Isotopes, Nuclear Magnetic Resonance, Biomolecular

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Solid-state NMR detection of 14N-13C dipolar couplings between amino acid side groups provides constraints on amyloid fibril architecture. / Middleton, David A.
In: June 2002. ISSN 1460-4582, Vol. 49, No. 2, 02.2011, p. 65-9.

Research output: Contribution to Journal/Magazine › Journal article › peer-review

Bibtex

@article{961f6e82ed914a438b980f2e3d8cc324,

title = "Solid-state NMR detection of 14N-13C dipolar couplings between amino acid side groups provides constraints on amyloid fibril architecture",

abstract = "Solid-state nuclear magnetic resonance (SSNMR) is a powerful technique for the structural analysis of amyloid fibrils. With suitable isotope labelling patterns, SSNMR can provide constraints on the secondary structure, alignment and registration of β-strands within amyloid fibrils and identify the tertiary and quaternary contacts defining the packing of the β-sheet layers. Detection of (14)N-(13)C dipolar couplings may provide potentially useful additional structural constraints on β-sheet packing within amyloid fibrils but has not until now been exploited for this purpose. Here a frequency-selective, transfer of population in double resonance SSNMR experiment is used to detect a weak (14)N-(13)C dipolar coupling in amyloid-like fibrils of the peptide H(2)N-SNNFGAILSS-COOH, which was uniformly (13)C and (15)N labelled across the four C-terminal amino acids. The (14)N-(13)C interatomic distance between leucine and asparagine side groups is constrained between 2.4 and 3.8 {\AA}, which allows current structural models of the β-spine arrangement within the fibrils to be refined. This procedure could be useful for the general structural analysis of other proteins in condensed phases and environments, such as biological membranes.",

keywords = "Amyloid, Carbon Isotopes, Molecular Structure, Nitrogen Isotopes, Nuclear Magnetic Resonance, Biomolecular",

author = "Middleton, {David A}",

note = "Copyright {\textcopyright} 2011 John Wiley & Sons, Ltd.",

year = "2011",

month = feb,

doi = "10.1002/mrc.2708",

language = "English",

volume = "49",

pages = "65--9",

journal = "June 2002. ISSN 1460-4582",

issn = "0893-3200",

publisher = "American Psychological Association Inc.",

number = "2",

}

RIS

TY - JOUR

T1 - Solid-state NMR detection of 14N-13C dipolar couplings between amino acid side groups provides constraints on amyloid fibril architecture

AU - Middleton, David A

PY - 2011/2

Y1 - 2011/2

N2 - Solid-state nuclear magnetic resonance (SSNMR) is a powerful technique for the structural analysis of amyloid fibrils. With suitable isotope labelling patterns, SSNMR can provide constraints on the secondary structure, alignment and registration of β-strands within amyloid fibrils and identify the tertiary and quaternary contacts defining the packing of the β-sheet layers. Detection of (14)N-(13)C dipolar couplings may provide potentially useful additional structural constraints on β-sheet packing within amyloid fibrils but has not until now been exploited for this purpose. Here a frequency-selective, transfer of population in double resonance SSNMR experiment is used to detect a weak (14)N-(13)C dipolar coupling in amyloid-like fibrils of the peptide H(2)N-SNNFGAILSS-COOH, which was uniformly (13)C and (15)N labelled across the four C-terminal amino acids. The (14)N-(13)C interatomic distance between leucine and asparagine side groups is constrained between 2.4 and 3.8 Å, which allows current structural models of the β-spine arrangement within the fibrils to be refined. This procedure could be useful for the general structural analysis of other proteins in condensed phases and environments, such as biological membranes.

AB - Solid-state nuclear magnetic resonance (SSNMR) is a powerful technique for the structural analysis of amyloid fibrils. With suitable isotope labelling patterns, SSNMR can provide constraints on the secondary structure, alignment and registration of β-strands within amyloid fibrils and identify the tertiary and quaternary contacts defining the packing of the β-sheet layers. Detection of (14)N-(13)C dipolar couplings may provide potentially useful additional structural constraints on β-sheet packing within amyloid fibrils but has not until now been exploited for this purpose. Here a frequency-selective, transfer of population in double resonance SSNMR experiment is used to detect a weak (14)N-(13)C dipolar coupling in amyloid-like fibrils of the peptide H(2)N-SNNFGAILSS-COOH, which was uniformly (13)C and (15)N labelled across the four C-terminal amino acids. The (14)N-(13)C interatomic distance between leucine and asparagine side groups is constrained between 2.4 and 3.8 Å, which allows current structural models of the β-spine arrangement within the fibrils to be refined. This procedure could be useful for the general structural analysis of other proteins in condensed phases and environments, such as biological membranes.

KW - Amyloid

KW - Carbon Isotopes

KW - Molecular Structure

KW - Nitrogen Isotopes

KW - Nuclear Magnetic Resonance, Biomolecular

U2 - 10.1002/mrc.2708

DO - 10.1002/mrc.2708

M3 - Journal article

C2 - 21254226

VL - 49

SP - 65

EP - 69

JO - June 2002. ISSN 1460-4582

JF - June 2002. ISSN 1460-4582

SN - 0893-3200

IS - 2

ER -

Research

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