Studies of the molten globule state of ferredoxin: Structural characterization and implications on protein folding and iron-sulfur center assembly

2007 ◽  
Vol 68 (3) ◽  
pp. 606-616 ◽  
Author(s):  
Sónia S. Leal ◽  
Cláudio M. Gomes
Biochemistry ◽  
2005 ◽  
Vol 44 (20) ◽  
pp. 7490-7496 ◽  
Author(s):  
Yeoun Jin Kim ◽  
Young A Kim ◽  
Nokyoung Park ◽  
Hyeon S. Son ◽  
Kwang S. Kim ◽  
...  

Our recent experiments on the molten globule state and other protein folding intermediates lead to following conclusions: (i) the molten globule is separated by intramolecular first-order phase transitions from the native and unfolded states and therefore is a specific thermodynamic state of protein molecules; (ii) the novel equilibrium folding intermediate (the ‘pre-molten globule’ state) exists which can be similar to the ‘burst’ kinetic intermediate of protein folding; (iii) proteins denature and release their non-polar ligands at moderately low pH and moderately low dielectric constant, i.e. under conditions which may be related to those near membranes.


2017 ◽  
Vol 112 (3) ◽  
pp. 485a-486a ◽  
Author(s):  
Benjamin Selmke ◽  
Chen Nickolaus ◽  
Peter Borbat ◽  
Jack H. Freed ◽  
Wolfgang E. Trommer

FEBS Letters ◽  
1997 ◽  
Vol 417 (1) ◽  
pp. 92-96 ◽  
Author(s):  
David Eliezer ◽  
Patricia A. Jennings ◽  
H.Jane Dyson ◽  
Peter E. Wright

FEBS Letters ◽  
1990 ◽  
Vol 262 (1) ◽  
pp. 20-24 ◽  
Author(s):  
O.B. Ptitsyn ◽  
R.H. Pain ◽  
G.V. Semisotnov ◽  
E. Zerovnik ◽  
O.I. Razgulyaev

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