Modulation of compactness and long-range interactions of unfolded lysozyme by single point mutations

Julia Wirmer; Christian Schlörb; Judith Klein-Seetharaman; Ryoma Hirano; Tadashi Ueda; Taiji Imoto; Harald Schwalbe

doi:10.1002/anie.200460907

Modulation of compactness and long-range interactions of unfolded lysozyme by single point mutations

Julia Wirmer, Christian Schlörb, Judith Klein-Seetharaman, Ryoma Hirano, Tadashi Ueda, Taiji Imoto, Harald Schwalbe

Research output: Contribution to journal › Article › peer-review

55 Scopus citations

Abstract

The non-native states of the model protein hen lysozyme (native state shown in picture) were investigated by using site-directed mutagenesis in combination with high-resolution NMR spectroscopy. The disruptions of the interactions between hydrophobic clusters by single point mutations dramatically alter the overall compactness of the unfolded state: single point mutations can turn a compact unfolded state into an extended state.

Original language	English (US)
Pages (from-to)	5780-5785
Number of pages	6
Journal	Angewandte Chemie - International Edition
Volume	43
Issue number	43
DOIs	https://doi.org/10.1002/anie.200460907
State	Published - Nov 5 2004
Externally published	Yes

Keywords

Biophysics
Lysozyme
Mutagenesis
NMR spectroscopy
Protein folding

ASJC Scopus subject areas

Catalysis
General Chemistry

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10.1002/anie.200460907

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AU - Ueda, Tadashi

AU - Imoto, Taiji

AU - Schwalbe, Harald

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KW - Biophysics

KW - Lysozyme

KW - Mutagenesis

KW - NMR spectroscopy

KW - Protein folding

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Modulation of compactness and long-range interactions of unfolded lysozyme by single point mutations

Abstract

Keywords

ASJC Scopus subject areas

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