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Millisecond Time Resolved Photo-CIDNP NMR Reveals a Non-Native Folding Intermediate on the Ion-Induced Refolding Pathway of Bovine α-Lactalbumin

2001; Wiley; Volume: 40; Issue: 22 Linguagem: Inglês

10.1002/1521-3773(20011119)40

1521-3773

Julia Wirmer, Till Kühn, Harald Schwalbe,

Protein Structure and Dynamics

Angewandte Chemie International EditionVolume 40, Issue 22 p. 4248-4251 Communication Millisecond Time Resolved Photo-CIDNP NMR Reveals a Non-Native Folding Intermediate on the Ion-Induced Refolding Pathway of Bovine α-Lactalbumin Julia Wirmer, Julia Wirmer Department of Chemistry and MIT/Harvard Center for Magnetic Resonance at the Francis Bitter Magnet Laboratory Massachusetts Institute of Technology 77 Massachusetts Avenue, Cambridge MA 02139, USA, Present address: Zentrum für Biologische Magnetische Resonanz Institut für Organische Chemie Universität Frankfurt Marie-Curie-Str. 11 60439 Frankfurt, Germany, Fax: (+49) 697-9829515Search for more papers by this authorTill Kühn, Till Kühn Department of Chemistry and MIT/Harvard Center for Magnetic Resonance at the Francis Bitter Magnet Laboratory Massachusetts Institute of Technology 77 Massachusetts Avenue, Cambridge MA 02139, USA, Present address: Zentrum für Biologische Magnetische Resonanz Institut für Organische Chemie Universität Frankfurt Marie-Curie-Str. 11 60439 Frankfurt, Germany, Fax: (+49) 697-9829515Search for more papers by this authorHarald Schwalbe Prof. Dr., Harald Schwalbe Prof. Dr. schwalb@mit.edu Department of Chemistry and MIT/Harvard Center for Magnetic Resonance at the Francis Bitter Magnet Laboratory Massachusetts Institute of Technology 77 Massachusetts Avenue, Cambridge MA 02139, USA, Present address: Zentrum für Biologische Magnetische Resonanz Institut für Organische Chemie Universität Frankfurt Marie-Curie-Str. 11 60439 Frankfurt, Germany, Fax: (+49) 697-9829515Search for more papers by this author Julia Wirmer, Julia Wirmer Department of Chemistry and MIT/Harvard Center for Magnetic Resonance at the Francis Bitter Magnet Laboratory Massachusetts Institute of Technology 77 Massachusetts Avenue, Cambridge MA 02139, USA, Present address: Zentrum für Biologische Magnetische Resonanz Institut für Organische Chemie Universität Frankfurt Marie-Curie-Str. 11 60439 Frankfurt, Germany, Fax: (+49) 697-9829515Search for more papers by this authorTill Kühn, Till Kühn Department of Chemistry and MIT/Harvard Center for Magnetic Resonance at the Francis Bitter Magnet Laboratory Massachusetts Institute of Technology 77 Massachusetts Avenue, Cambridge MA 02139, USA, Present address: Zentrum für Biologische Magnetische Resonanz Institut für Organische Chemie Universität Frankfurt Marie-Curie-Str. 11 60439 Frankfurt, Germany, Fax: (+49) 697-9829515Search for more papers by this authorHarald Schwalbe Prof. Dr., Harald Schwalbe Prof. Dr. schwalb@mit.edu Department of Chemistry and MIT/Harvard Center for Magnetic Resonance at the Francis Bitter Magnet Laboratory Massachusetts Institute of Technology 77 Massachusetts Avenue, Cambridge MA 02139, USA, Present address: Zentrum für Biologische Magnetische Resonanz Institut für Organische Chemie Universität Frankfurt Marie-Curie-Str. 11 60439 Frankfurt, Germany, Fax: (+49) 697-9829515Search for more papers by this author First published: 16 November 2001 https://doi.org/10.1002/1521-3773(20011119)40:22 3.0.CO;2-ICitations: 31 We thank the Massachusetts Institute of Technology (start-up funds (H.S.) and Rosenblith stipend (J.W.)), the Karl Winnacker Foundation (H.S.), the Fonds der Chemischen Industrie (H.S., J.W.) and BMBF (J.W.), as well as the DFG (H.S., Schw701/3-1) for financial support. We thank Dr. D. Blechschmidt for helpful discussions. CIDNP=chemically induced dynamic nuclear polarization. Read the full textAboutPDF ToolsRequest permissionExport citationAdd to favoritesTrack citation ShareShare Give accessShare full text accessShare full-text accessPlease review our Terms and Conditions of Use and check box below to share full-text version of article.I have read and accept the Wiley Online Library Terms and Conditions of UseShareable LinkUse the link below to share a full-text version of this article with your friends and colleagues. Learn more.Copy URL Share a linkShare onFacebookTwitterLinked InRedditWechat Abstract Aspects of the structure of the intermediate populated after 200 ms in the Ca2+-induced refolding of α-lactalbumin have been derived by time-resolved photo-CIDNP NMR methods. Refolding at constant denaturant concentration was initiated by laser-induced ion release from photolabile chelators. The NMR data demonstrated that part of the polypeptide chain in the β-domain of α-lactalbumin samples adopt non-native conformations while a hydrophobic core of the α-domain is already formed (see picture). Citing Literature Volume40, Issue22November 19, 2001Pages 4248-4251 RelatedInformation