Solution structure of micelle-bound H5 peptide (427–452): a primary structure corresponding to the pore forming region of the voltage dependent potassium channel

Kazuyasu Shindo, Hideo Takahashi, Kohki Shinozaki, Keiichiro Kami, Kazunori Anzai, Sannamu Lee, Haruhiko Aoyagi, Yutaka Kirino, Ichio Shimada

Research output: Contribution to journalArticle

3 Citations (Scopus)

Abstract

A 26-mer peptide with the sequence of the pore forming region (residues 427–452) of the Shaker K+ channel (H5 region) was chemically synthesized. Analyses by CD and two-dimensional 1H NMR spectroscopy were used to investigate the structure of the peptide bound to SDS micelles in solution, which are commonly used in biophysical studies. The tertiary structure of the peptide as a monomer was composed of an α-helix (431–438), a turn (439–442), and random coils (427–430, 443–452), and was very similar to that of the pore forming region of the native K+ channel from Streptomyces lividans determined by X-ray analysis [1]. This result suggests that even an isolated peptide forms a native-like conformation for residues from 431 to 442, depending on its intrinsic amino acid sequence and the surrounding environment.
Original languageEnglish
Pages (from-to)153-159
Number of pages7
JournalBiochimica et Biophysica Acta - Proteins and Proteomics
Volume1545
Issue number1
DOIs
Publication statusPublished - 2001

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Potassium Channels
Micelles
Peptides
Electric potential
Streptomyces lividans
X ray analysis
Nuclear magnetic resonance spectroscopy
Conformations
Amino Acid Sequence
Magnetic Resonance Spectroscopy
Monomers
X-Rays
Amino Acids

Cite this

Shindo, Kazuyasu ; Takahashi, Hideo ; Shinozaki, Kohki ; Kami, Keiichiro ; Anzai, Kazunori ; Lee, Sannamu ; Aoyagi, Haruhiko ; Kirino, Yutaka ; Shimada, Ichio. / Solution structure of micelle-bound H5 peptide (427–452): a primary structure corresponding to the pore forming region of the voltage dependent potassium channel. In: Biochimica et Biophysica Acta - Proteins and Proteomics. 2001 ; Vol. 1545, No. 1. pp. 153-159.
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title = "Solution structure of micelle-bound H5 peptide (427–452): a primary structure corresponding to the pore forming region of the voltage dependent potassium channel",
abstract = "A 26-mer peptide with the sequence of the pore forming region (residues 427–452) of the Shaker K+ channel (H5 region) was chemically synthesized. Analyses by CD and two-dimensional 1H NMR spectroscopy were used to investigate the structure of the peptide bound to SDS micelles in solution, which are commonly used in biophysical studies. The tertiary structure of the peptide as a monomer was composed of an α-helix (431–438), a turn (439–442), and random coils (427–430, 443–452), and was very similar to that of the pore forming region of the native K+ channel from Streptomyces lividans determined by X-ray analysis [1]. This result suggests that even an isolated peptide forms a native-like conformation for residues from 431 to 442, depending on its intrinsic amino acid sequence and the surrounding environment.",
author = "Kazuyasu Shindo and Hideo Takahashi and Kohki Shinozaki and Keiichiro Kami and Kazunori Anzai and Sannamu Lee and Haruhiko Aoyagi and Yutaka Kirino and Ichio Shimada",
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Solution structure of micelle-bound H5 peptide (427–452): a primary structure corresponding to the pore forming region of the voltage dependent potassium channel. / Shindo, Kazuyasu; Takahashi, Hideo; Shinozaki, Kohki; Kami, Keiichiro; Anzai, Kazunori; Lee, Sannamu; Aoyagi, Haruhiko; Kirino, Yutaka; Shimada, Ichio.

In: Biochimica et Biophysica Acta - Proteins and Proteomics, Vol. 1545, No. 1, 2001, p. 153-159.

Research output: Contribution to journalArticle

TY - JOUR

T1 - Solution structure of micelle-bound H5 peptide (427–452): a primary structure corresponding to the pore forming region of the voltage dependent potassium channel

AU - Shindo, Kazuyasu

AU - Takahashi, Hideo

AU - Shinozaki, Kohki

AU - Kami, Keiichiro

AU - Anzai, Kazunori

AU - Lee, Sannamu

AU - Aoyagi, Haruhiko

AU - Kirino, Yutaka

AU - Shimada, Ichio

PY - 2001

Y1 - 2001

N2 - A 26-mer peptide with the sequence of the pore forming region (residues 427–452) of the Shaker K+ channel (H5 region) was chemically synthesized. Analyses by CD and two-dimensional 1H NMR spectroscopy were used to investigate the structure of the peptide bound to SDS micelles in solution, which are commonly used in biophysical studies. The tertiary structure of the peptide as a monomer was composed of an α-helix (431–438), a turn (439–442), and random coils (427–430, 443–452), and was very similar to that of the pore forming region of the native K+ channel from Streptomyces lividans determined by X-ray analysis [1]. This result suggests that even an isolated peptide forms a native-like conformation for residues from 431 to 442, depending on its intrinsic amino acid sequence and the surrounding environment.

AB - A 26-mer peptide with the sequence of the pore forming region (residues 427–452) of the Shaker K+ channel (H5 region) was chemically synthesized. Analyses by CD and two-dimensional 1H NMR spectroscopy were used to investigate the structure of the peptide bound to SDS micelles in solution, which are commonly used in biophysical studies. The tertiary structure of the peptide as a monomer was composed of an α-helix (431–438), a turn (439–442), and random coils (427–430, 443–452), and was very similar to that of the pore forming region of the native K+ channel from Streptomyces lividans determined by X-ray analysis [1]. This result suggests that even an isolated peptide forms a native-like conformation for residues from 431 to 442, depending on its intrinsic amino acid sequence and the surrounding environment.

U2 - 10.1016/S0167-4838

DO - 10.1016/S0167-4838

M3 - Article

VL - 1545

SP - 153

EP - 159

JO - Biochimica et Biophysica Acta - Proteins and Proteomics

JF - Biochimica et Biophysica Acta - Proteins and Proteomics

SN - 1570-9639

IS - 1

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