| Literature DB >> 29712118 |
Julia Wirmer1, Till Kühn1, Harald Schwalbe1.
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.Entities:
Keywords: NMR spectroscopy; calcium; protein folding; structure elucidation
Year: 2001 PMID: 29712118 DOI: 10.1002/1521-3773(20011119)40:22<4248::AID-ANIE4248>3.0.CO;2-I
Source DB: PubMed Journal: Angew Chem Int Ed Engl ISSN: 1433-7851 Impact factor: 15.336