Entropy calculations on the molten globule state of a protein: Side-chain entropies of α-lactalbumin

2001 ◽  
Vol 46 (2) ◽  
pp. 215-224 ◽  
Author(s):  
Heiko Schäfer ◽  
Lorna J. Smith ◽  
Alan E. Mark ◽  
Wilfred F. van Gunsteren
Keyword(s):  
Molten Globule ◽  
Side Chain ◽  
Molten Globule State

Side Chain Accessibility and Dynamics in the Molten Globule State of α-Lactalbumin:  A19F-NMR Study

Biochemistry ◽  
2000 ◽  
Vol 39 (2) ◽  
pp. 372-380 ◽  
Author(s):  
Ping Bai ◽  
Li Luo ◽  
Zheng-yu Peng
Keyword(s):  
Molten Globule ◽  
Side Chain ◽  
Molten Globule State ◽  
Nmr Study

Unfolding of the molten globule state of .alpha.-lactalbumin studied by proton NMR

Biochemistry ◽  
1993 ◽  
Vol 32 (48) ◽  
pp. 13198-13203 ◽  
Author(s):  
Akio Shimizu ◽  
Masamichi Ikeguchi ◽  
Shintaro Sugai
Keyword(s):  
Molten Globule ◽  
Proton Nmr ◽  
Molten Globule State ◽  
Alpha Lactalbumin

Time-resolved Fluorescence Studies of the Molten Globule State of Apomyoglobin

1996 ◽  
Vol 257 (4) ◽  
pp. 877-885 ◽  
Author(s):  
Christian Rischel ◽  
Per Thyberg ◽  
Rudolf Rigler ◽  
Flemming M. Poulsen
Keyword(s):  
Molten Globule ◽  
Time Resolved Fluorescence ◽  
Time Resolved ◽  
Molten Globule State ◽  
Fluorescence Studies

scholarly journals The molten globule state of α‐lactalbumin

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

Effect of curcumin on amyloidogenic property of molten globule-like intermediate state of 2,5-diketo-d-gluconate reductase A

2009 ◽  
Vol 390 (10) ◽  
Author(s):  
Nandini Sarkar ◽  
Abhay Narain Singh ◽  
Vikash Kumar Dubey
Keyword(s):  
Protein Concentration ◽  
Molten Globule ◽  
Molar Ratio ◽  
Amyloid Formation ◽  
Molten Globule State ◽  
Force Microscopy ◽  
Atomic Force ◽  
Sheet Structure ◽  
Amyloid Diseases ◽  
Β Sheet

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.

Thermodynamic and Structural Properties of the Acid Molten Globule State of Horse Cytochromec

Biochemistry ◽  
2011 ◽  
Vol 50 (15) ◽  
pp. 3116-3126 ◽  
Author(s):  
Shigeyoshi Nakamura ◽  
Yasutaka Seki ◽  
Etsuko Katoh ◽  
Shun-ichi Kidokoro
Keyword(s):  
Structural Properties ◽  
Molten Globule ◽  
Molten Globule State
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