Solution Structure of the D/E Helix Linker of Skeletal Troponin-C

As Studied by Circular Dichroism and Two-Dimensional NMR Spectroscopy

Weon Tae Lee, N. Rama Krishna, G. M. Anatharamaiah, Herbert C. Cheung

Research output: Contribution to journalArticle

Abstract

We have synthesized a 17-residue peptide with the amino acid sequence RQMKEDAKGKSEEELAD corresponding to residues 84-100 of chicken skeletal troponin C. This stretch of the protein sequence is in the middle one-third of the 32-residue 9-turn α-helix that connects the two globular domains of the dumbell-shaped molecule and includes the D/E linker helix. We describe here the solution conformation of the helix linker as studied by circular dichroism (CD) and two-dimensional nuclear magnetic resonance (2-D NMR) spectroscopy. The NOE connectivities together with the vicinal 3J coupling constants suggest that the peptide exists in a fast conformational equilibrium among several secondary structures: a nascent helix near the N-terminus, a helix, and a substational population of extended and random coil forms. In addition, two interresidue α-α NOEs are observed suggesting a bent structure with a bend that includes the single glycine in position 92. These results are consistent with the ideas that in neutral solution the D/E linker region of the central helix in troponin C can adopt a helical conformation and the central helix may have a segmental flexibility around Gly 92.

Original languageEnglish
Pages (from-to)57-62
Number of pages6
JournalBulletin of the Korean Chemical Society
Volume19
Issue number1
Publication statusPublished - 1998 Jan 20

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Troponin C
Nuclear magnetic resonance spectroscopy
Conformations
Peptides
Glycine
Nuclear magnetic resonance
Amino Acids
Molecules
Proteins
Circular Dichroism

All Science Journal Classification (ASJC) codes

  • Chemistry(all)

Cite this

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title = "Solution Structure of the D/E Helix Linker of Skeletal Troponin-C: As Studied by Circular Dichroism and Two-Dimensional NMR Spectroscopy",
abstract = "We have synthesized a 17-residue peptide with the amino acid sequence RQMKEDAKGKSEEELAD corresponding to residues 84-100 of chicken skeletal troponin C. This stretch of the protein sequence is in the middle one-third of the 32-residue 9-turn α-helix that connects the two globular domains of the dumbell-shaped molecule and includes the D/E linker helix. We describe here the solution conformation of the helix linker as studied by circular dichroism (CD) and two-dimensional nuclear magnetic resonance (2-D NMR) spectroscopy. The NOE connectivities together with the vicinal 3JNα coupling constants suggest that the peptide exists in a fast conformational equilibrium among several secondary structures: a nascent helix near the N-terminus, a helix, and a substational population of extended and random coil forms. In addition, two interresidue α-α NOEs are observed suggesting a bent structure with a bend that includes the single glycine in position 92. These results are consistent with the ideas that in neutral solution the D/E linker region of the central helix in troponin C can adopt a helical conformation and the central helix may have a segmental flexibility around Gly 92.",
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Solution Structure of the D/E Helix Linker of Skeletal Troponin-C : As Studied by Circular Dichroism and Two-Dimensional NMR Spectroscopy. / Lee, Weon Tae; Krishna, N. Rama; Anatharamaiah, G. M.; Cheung, Herbert C.

In: Bulletin of the Korean Chemical Society, Vol. 19, No. 1, 20.01.1998, p. 57-62.

Research output: Contribution to journalArticle

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AB - We have synthesized a 17-residue peptide with the amino acid sequence RQMKEDAKGKSEEELAD corresponding to residues 84-100 of chicken skeletal troponin C. This stretch of the protein sequence is in the middle one-third of the 32-residue 9-turn α-helix that connects the two globular domains of the dumbell-shaped molecule and includes the D/E linker helix. We describe here the solution conformation of the helix linker as studied by circular dichroism (CD) and two-dimensional nuclear magnetic resonance (2-D NMR) spectroscopy. The NOE connectivities together with the vicinal 3JNα coupling constants suggest that the peptide exists in a fast conformational equilibrium among several secondary structures: a nascent helix near the N-terminus, a helix, and a substational population of extended and random coil forms. In addition, two interresidue α-α NOEs are observed suggesting a bent structure with a bend that includes the single glycine in position 92. These results are consistent with the ideas that in neutral solution the D/E linker region of the central helix in troponin C can adopt a helical conformation and the central helix may have a segmental flexibility around Gly 92.

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