Sequential resonance assignment from two-dimensional inter- and intra-residue 15N-1H correlation spectra

Arto Annila (Corresponding Author), P. Permi

Research output: Contribution to journalArticleScientificpeer-review

1 Citation (Scopus)

Abstract

Sequential assignment of amide resonances in proteins and peptides can conveniently be derived from twodimensional inter-residue 15Ni1HN(i−1) and intra-residue 15Ni 1HNi correlation spectra. The inter-residue  15Ni –1HN(i−1)correlation spectrum is generated by recording the 15Ni frequency evolution indirectly and subsequently transferring the magnetization to 1HN(i−1) of the preceding residue for direct detection. The flow of coherence is established by the (H)N(COCAHA)-TOCSY pulse sequence. Following the path from intra-residue correlation via inter-residue correlation to the next intra-residue correlation results in sequential assignment in two dimensions. This kind of assignment protocol is most amenable to re-establishing sequential assignments of target proteins perturbed by binding of ligands or alternatively signals of peptide ligands can be traced in studies of structure–function relationships by NMR.
Original languageEnglish
Pages (from-to)179-181
Number of pages3
JournalMagnetic Resonance in Chemistry
Volume39
Issue number4
Publication statusPublished - 2001
MoE publication typeA1 Journal article-refereed

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Peptides
Ligands
Proteins
Protein Sorting Signals
Amides
Magnetization
Nuclear magnetic resonance

Cite this

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title = "Sequential resonance assignment from two-dimensional inter- and intra-residue 15N-1H correlation spectra",
abstract = "Sequential assignment of amide resonances in proteins and peptides can conveniently be derived from twodimensional inter-residue 15Ni –1HN(i−1) and intra-residue 15Ni –1HNi correlation spectra. The inter-residue  15Ni –1HN(i−1)correlation spectrum is generated by recording the 15Ni frequency evolution indirectly and subsequently transferring the magnetization to 1HN(i−1) of the preceding residue for direct detection. The flow of coherence is established by the (H)N(COCAHA)-TOCSY pulse sequence. Following the path from intra-residue correlation via inter-residue correlation to the next intra-residue correlation results in sequential assignment in two dimensions. This kind of assignment protocol is most amenable to re-establishing sequential assignments of target proteins perturbed by binding of ligands or alternatively signals of peptide ligands can be traced in studies of structure–function relationships by NMR.",
author = "Arto Annila and P. Permi",
year = "2001",
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journal = "Magnetic Resonance in Chemistry",
issn = "0749-1581",
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Sequential resonance assignment from two-dimensional inter- and intra-residue 15N-1H correlation spectra. / Annila, Arto (Corresponding Author); Permi, P.

In: Magnetic Resonance in Chemistry, Vol. 39, No. 4, 2001, p. 179-181.

Research output: Contribution to journalArticleScientificpeer-review

TY - JOUR

T1 - Sequential resonance assignment from two-dimensional inter- and intra-residue 15N-1H correlation spectra

AU - Annila, Arto

AU - Permi, P.

PY - 2001

Y1 - 2001

N2 - Sequential assignment of amide resonances in proteins and peptides can conveniently be derived from twodimensional inter-residue 15Ni –1HN(i−1) and intra-residue 15Ni –1HNi correlation spectra. The inter-residue  15Ni –1HN(i−1)correlation spectrum is generated by recording the 15Ni frequency evolution indirectly and subsequently transferring the magnetization to 1HN(i−1) of the preceding residue for direct detection. The flow of coherence is established by the (H)N(COCAHA)-TOCSY pulse sequence. Following the path from intra-residue correlation via inter-residue correlation to the next intra-residue correlation results in sequential assignment in two dimensions. This kind of assignment protocol is most amenable to re-establishing sequential assignments of target proteins perturbed by binding of ligands or alternatively signals of peptide ligands can be traced in studies of structure–function relationships by NMR.

AB - Sequential assignment of amide resonances in proteins and peptides can conveniently be derived from twodimensional inter-residue 15Ni –1HN(i−1) and intra-residue 15Ni –1HNi correlation spectra. The inter-residue  15Ni –1HN(i−1)correlation spectrum is generated by recording the 15Ni frequency evolution indirectly and subsequently transferring the magnetization to 1HN(i−1) of the preceding residue for direct detection. The flow of coherence is established by the (H)N(COCAHA)-TOCSY pulse sequence. Following the path from intra-residue correlation via inter-residue correlation to the next intra-residue correlation results in sequential assignment in two dimensions. This kind of assignment protocol is most amenable to re-establishing sequential assignments of target proteins perturbed by binding of ligands or alternatively signals of peptide ligands can be traced in studies of structure–function relationships by NMR.

M3 - Article

VL - 39

SP - 179

EP - 181

JO - Magnetic Resonance in Chemistry

JF - Magnetic Resonance in Chemistry

SN - 0749-1581

IS - 4

ER -