Literature DB >> 29712118

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

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.
Copyright © 2001 WILEY-VCH Verlag GmbH, Weinheim, Fed. Rep. of Germany.

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


  2 in total

1.  Light-Induced Uncaging for Time-Resolved Observations of Biochemical Reactions by MAS NMR Spectroscopy.

Authors:  Julian de Mos; Andreas Jakob; Johanna Becker-Baldus; Alexander Heckel; Clemens Glaubitz
Journal:  Chemistry       Date:  2020-05-13       Impact factor: 5.236

2.  Refolding of Cold-Denatured Barstar Induced by Radio-Frequency Heating: A New Method to Study Protein Folding by Real-Time NMR Spectroscopy.

Authors:  György Pintér; Harald Schwalbe
Journal:  Angew Chem Int Ed Engl       Date:  2020-09-25       Impact factor: 15.336

  2 in total

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