A Two-Process Model Describes the Hydrogen Exchange Behavior of Cytochromecin the Molten Globule State with Various Extents of Acetylation†

Biochemistry ◽  
2001 ◽  
Vol 40 (32) ◽  
pp. 9623-9630 ◽  
Author(s):  
Zbigniew Szewczuk ◽  
Yasuo Konishi ◽  
Yuji Goto
Keyword(s):  
Process Model ◽  
Hydrogen Exchange ◽  
Molten Globule ◽  
Molten Globule State

Conformational Dynamics of the GdmHCl-Induced Molten Globule State of Creatine Kinase Monitored by Hydrogen Exchange and Mass Spectrometry

Biochemistry ◽  
2004 ◽  
Vol 43 (17) ◽  
pp. 5045-5054 ◽  
Author(s):  
Hortense Mazon ◽  
Olivier Marcillat ◽  
Eric Forest ◽  
David L. Smith ◽  
Christian Vial
Keyword(s):  
Mass Spectrometry ◽  
Creatine Kinase ◽  
Hydrogen Exchange ◽  
Molten Globule ◽  
Conformational Dynamics ◽  
Molten Globule State

Structure and stability of the molten globule state of guinea pig .alpha.-lactalbumin: A hydrogen exchange study

Biochemistry ◽  
1993 ◽  
Vol 32 (21) ◽  
pp. 5681-5691 ◽  
Author(s):  
Chia Lin Chyan ◽  
Claire Wormald ◽  
Christopher M. Dobson ◽  
Philip A. Evans ◽  
Jean Baum
Keyword(s):  
Guinea Pig ◽  
Hydrogen Exchange ◽  
Molten Globule ◽  
Molten Globule State ◽  
Structure And Stability ◽  
Exchange Study ◽  
Alpha Lactalbumin

scholarly journals Hydrogen exchange study of folding intermediate and molten globule state of canine milk lysozyme

2000 ◽  
Vol 40 (supplement) ◽  
pp. S160
Author(s):  
Y. Kobashigawa ◽  
M Mizuguchi ◽  
M. Demura ◽  
T. Koshiba ◽  
S. Tsuda ◽  
...  
Keyword(s):  
Hydrogen Exchange ◽  
Molten Globule ◽  
Folding Intermediate ◽  
Molten Globule State ◽  
Exchange 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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