pH-dependent stability of the human ?-lactalbumin molten globule state: Contrasting roles of the 6?120 disulfide and the ?-subdomain at low and neutral pH

2003 ◽  
Vol 52 (2) ◽  
pp. 193-202 ◽  
Author(s):  
Jia-Cherng Horng ◽  
Stephen J. Demarest ◽  
Daniel P. Raleigh
Keyword(s):  
Molten Globule ◽  
Molten Globule State ◽  
Neutral Ph ◽  
Ph Dependent

scholarly journals pH-Dependent cooperativity and existence of a dry molten globule in the folding of a miniprotein BBL

2018 ◽  
Vol 20 (5) ◽  
pp. 3523-3530 ◽  
Author(s):  
Zhi Yue ◽  
Jana Shen
Keyword(s):  
Molecular Dynamics ◽  
Energy Barrier ◽  
Molten Globule ◽  
Free Energy Barrier ◽  
Molten Globule State ◽  
Constant Ph ◽  
Ph Dependent ◽  
Dynamics Simulations ◽  
Constant Ph Molecular Dynamics ◽  
Folding Free Energy

Constant pH molecular dynamics simulations of BBL reveals negligible folding free energy barrier that is pH dependent and a sparsely populated dry molten globule state.

Rupture of the Hydrogen Bond Linking Two Ω-Loops Induces the Molten Globule State at Neutral pH in Cytochromec†

Biochemistry ◽  
2003 ◽  
Vol 42 (24) ◽  
pp. 7604-7610 ◽  
Author(s):  
Federica Sinibaldi ◽  
M. Cristina Piro ◽  
Barry D. Howes ◽  
Giulietta Smulevich ◽  
Franca Ascoli ◽  
...  
Keyword(s):  
Hydrogen Bond ◽  
Molten Globule ◽  
Molten Globule State ◽  
Neutral Ph

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

Structural Characterization of the Molten Globule State of Apomyoglobin by Limited Proteolysis and HPLC-Mass Spectrometry†

Biochemistry ◽  
2005 ◽  
Vol 44 (20) ◽  
pp. 7490-7496 ◽  
Author(s):  
Yeoun Jin Kim ◽  
Young A Kim ◽  
Nokyoung Park ◽  
Hyeon S. Son ◽  
Kwang S. Kim ◽  
...  
Keyword(s):  
Mass Spectrometry ◽  
Structural Characterization ◽  
Molten Globule ◽  
Limited Proteolysis ◽  
Molten Globule State

Molten globule state of human placental cystatin (HPC) at low pH conditions and the effects of trifluoroethanol (TFE) and methanol

2006 ◽  
Vol 84 (2) ◽  
pp. 126-134 ◽  
Author(s):  
Fouzia Rashid ◽  
Sandeep Sharma ◽  
M A Baig ◽  
Bilqees Bano
Keyword(s):  
Conformational Changes ◽  
Tertiary Structure ◽  
Molten Globule ◽  
Structural Features ◽  
Cd Spectroscopy ◽  
Native State ◽  
Molten Globule State ◽  
Fluorescence Measurements ◽  
Helical Content ◽  
Human Placental Cystatin

Acid-induced conformational changes were studied in human placental cystatin (HPC) in terms of circular dichroism (CD) spectroscopy, the binding of hydrophobic dye 1-anilinonapthalene-8-sulphonic acid (ANS), and intrinsic fluorescence measurements. Our results show the formation of an acid-induced molten globule state at pH 2.0, with significant secondary and tertiary interactions that resemble the native state, exposed hydrophobic regions and the effects of trifluoroethanol (TFE) and methanol in conversion of the acid-denatured state of HPC to the alcohol-induced state, which is characterized by increased helical content, disrupted tertiary structure, and the absence of hydrophobic clusters. Alcohol-induced formation of α-helical structures at pH 2.0 is evident from the increase in the ellipticity values at 222 nm, with native-like secondary structural features at 40% TFE. The increase in helical content was observed up to 80% TFE concentration. The ability of TFE (40%) to refold acid-denatured HPC to native-state conformation is also supported by intrinsic and ANS fluorescence measurements.Key words: human placental cystatin, molten globule, acid-induced state, trifluoroethanol, methanol, CD spectroscopy, ANS fluorescence, pH, protein folding.

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