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 journalArticle

48 Citations (Scopus)

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 languageEnglish
Pages (from-to)5780-5785
Number of pages6
JournalAngewandte Chemie - International Edition
Volume43
Issue number43
DOIs
Publication statusPublished - Nov 5 2004

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Mutagenesis
Muramidase
Nuclear magnetic resonance spectroscopy
Enzymes
Modulation
Proteins

All Science Journal Classification (ASJC) codes

  • Catalysis
  • Chemistry(all)

Cite this

Modulation of compactness and long-range interactions of unfolded lysozyme by single point mutations. / Wirmer, Julia; Schlörb, Christian; Klein-Seetharaman, Judith; Hirano, Ryoma; Ueda, Tadashi; Imoto, Taiji; Schwalbe, Harald.

In: Angewandte Chemie - International Edition, Vol. 43, No. 43, 05.11.2004, p. 5780-5785.

Research output: Contribution to journalArticle

Wirmer, Julia ; Schlörb, Christian ; Klein-Seetharaman, Judith ; Hirano, Ryoma ; Ueda, Tadashi ; Imoto, Taiji ; Schwalbe, Harald. / Modulation of compactness and long-range interactions of unfolded lysozyme by single point mutations. In: Angewandte Chemie - International Edition. 2004 ; Vol. 43, No. 43. pp. 5780-5785.
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