Proline Scanning Mutagenesis Reveals Non-Native Fold in the Molten Globule State of Equine β-Lactoglobulin†

Biochemistry ◽  
2006 ◽  
Vol 45 (51) ◽  
pp. 15468-15473 ◽  
Author(s):  
Kanako Nakagawa ◽  
Akihito Tokushima ◽  
Kazuo Fujiwara ◽  
Masamichi Ikeguchi
Author(s):  
Masamichi Ikeguchi ◽  
Shin-ichi Kato ◽  
Akio Shimizu ◽  
Shintaro Sugai

2010 ◽  
Vol 119 (4) ◽  
pp. 1550-1556 ◽  
Author(s):  
Laurette Tavel ◽  
Céline Moreau ◽  
Saïd Bouhallab ◽  
Eunice C.Y. Li-Chan ◽  
Elisabeth Guichard

Biochemistry ◽  
1999 ◽  
Vol 38 (14) ◽  
pp. 4455-4463 ◽  
Author(s):  
Kazuo Fujiwara ◽  
Munehito Arai ◽  
Akio Shimizu ◽  
Masamichi Ikeguchi ◽  
Kunihiro Kuwajima ◽  
...  

Biochemistry ◽  
1993 ◽  
Vol 32 (48) ◽  
pp. 13198-13203 ◽  
Author(s):  
Akio Shimizu ◽  
Masamichi Ikeguchi ◽  
Shintaro Sugai

1996 ◽  
Vol 257 (4) ◽  
pp. 877-885 ◽  
Author(s):  
Christian Rischel ◽  
Per Thyberg ◽  
Rudolf Rigler ◽  
Flemming M. Poulsen

1996 ◽  
Vol 10 (1) ◽  
pp. 102-109 ◽  
Author(s):  
Kunihiro Kuwajima

2009 ◽  
Vol 390 (10) ◽  
Author(s):  
Nandini Sarkar ◽  
Abhay Narain Singh ◽  
Vikash Kumar Dubey

Abstract We identified a molten globule-like intermediate of 2,5-diketo-d-gluconate reductase A (DKGR) at pH 2.5, which has a prominent β-sheet structure. The molten globule state of the protein shows amyloidogenic property >50 μm protein concentration. Interestingly, a 1:1 molar ratio of curcumin prevents amyloid formation as shown by the Thioflavin-T assay and atomic force microscopy. To the best of our knowledge, this is the first report on amyloid formation by an (α/β)8-barrel protein. The results presented here indicate that the molten globule state has an important role in amyloid formation and potential application of curcumin in protein biotechnology as well as therapeutics against amyloid diseases.


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