Chapter 2 NMR Studies of Protein Folding. Folding Studies of Calcium-Binding Lysozyme and α-Lactalbumin

Mineyuki Mizuguchi; Tomoyasu Aizawa; Keiichi Kawano; Makoto Demura

doi:10.1016/S0066-4103(08)00202-0

Chapter 2 NMR Studies of Protein Folding. Folding Studies of Calcium-Binding Lysozyme and α-Lactalbumin

Mineyuki Mizuguchi^*, Tomoyasu Aizawa, Keiichi Kawano, Makoto Demura

^*Corresponding author for this work

Structural Biology

Research output: Chapter in Book/Report/Conference proceeding › Chapter › peer-review

2 Scopus citations

Abstract

NMR is a powerful tool for characterizing the structure and dynamics of proteins at the site-specific level. A variety of NMR techniques can be applied to study various conformational states during the folding process, including the highly unfolded, partially folded, and native states. One particularly powerful method is the combination of NMR with hydrogen-deuterium exchange to indicate the formation of hydrogen bonds in proteins. Examples of the application of a variety of NMR methods to the protein folding studies of α-lactalbumin and c-type lysozyme are presented.

Original language	English
Title of host publication	Annual Reports on NMR Spectroscopy
Editors	Graham Webb
Pages	53-76
Number of pages	24
DOIs	https://doi.org/10.1016/S0066-4103(08)00202-0
State	Published - 2009

Publication series

Name	Annual Reports on NMR Spectroscopy
Volume	65
ISSN (Print)	0066-4103

Keywords

Alpha-lactalbumin
Calcium-binding lysozyme
Folding process
Hydrogen-deuterium exchange
Molten globule

ASJC Scopus subject areas

Atomic and Molecular Physics, and Optics
Spectroscopy

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10.1016/S0066-4103(08)00202-0

Cite this

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abstract = "NMR is a powerful tool for characterizing the structure and dynamics of proteins at the site-specific level. A variety of NMR techniques can be applied to study various conformational states during the folding process, including the highly unfolded, partially folded, and native states. One particularly powerful method is the combination of NMR with hydrogen-deuterium exchange to indicate the formation of hydrogen bonds in proteins. Examples of the application of a variety of NMR methods to the protein folding studies of α-lactalbumin and c-type lysozyme are presented.",

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Chapter 2 NMR Studies of Protein Folding. Folding Studies of Calcium-Binding Lysozyme and α-Lactalbumin. / Mizuguchi, Mineyuki; Aizawa, Tomoyasu; Kawano, Keiichi et al.
Annual Reports on NMR Spectroscopy. ed. / Graham Webb. 2009. p. 53-76 (Annual Reports on NMR Spectroscopy; Vol. 65).

Research output: Chapter in Book/Report/Conference proceeding › Chapter › peer-review

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AU - Kawano, Keiichi

AU - Demura, Makoto

PY - 2009

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KW - Alpha-lactalbumin

KW - Calcium-binding lysozyme

KW - Folding process

KW - Hydrogen-deuterium exchange

KW - Molten globule

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Chapter 2 NMR Studies of Protein Folding. Folding Studies of Calcium-Binding Lysozyme and α-Lactalbumin

Abstract

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Keywords

ASJC Scopus subject areas

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