Structural and kinetic characterization of early folding events in β-lactoglobulin

By K. Kuwata, R. Shastry, Hong Cheng, M. Hoshino, C. Batt, Y. Goto, H. Roder. Nature Structural Biology, 2001

145 citations recorded by the source corpus.

Subfields: Food Science, Materials Chemistry, Molecular Biology

View Paper: https://www.semanticscholar.org/paper/0fab6948844abfd4e588b5de083939760de91e39

How researchers see this paper

The researchers whose trusted networks rank it highest, strongest advocate first. Every researcher gets a different order.

In Food Science

1. Christopher M. Dobson

In Materials Chemistry

1. D. Hamada
2. Christopher M. Dobson
3. D. Selkoe

In Molecular Biology

1. D. Hamada
2. Christopher M. Dobson
3. Michele Vendruscolo
4. Tuomas P. J. Knowles
5. Fabrizio Chiti
6. D. Selkoe

Citations in the corpus

• A kinetic study of β‐lactoglobulin amyloid fibril formation promoted by urea (2002, background): “…of the protein during refolding has been found to form non-native -helical structures (Hamada et al. 1996; Kuwajima et al. 1996; Hamada and Goto 1997) in the vicinity of the amino-terminal region of the sequence, a region corresponding to the A-strand in the native structure (Kuwata et al. 2001).”