scholarly journals Evidence for close side-chain packing in an early protein folding intermediate previously assumed to be a molten globule

2014 ◽  
Vol 111 (41) ◽  
pp. 14746-14751 ◽  
Author(s):  
L. E. Rosen ◽  
K. B. Connell ◽  
S. Marqusee

One of the mysteries in protein folding is how folding intermediates direct a protein to its unique final structure. To address this question, we have studied the molten globule formed by the α-helical domain of α-lactalbumin (α-LA) and demonstrated that it has a native-like tertiary fold, even in the absence of rigid, extensive side chain packing. These studies suggest that the role of molten globule intermediates in protein folding is to maintain an approximate native backbone topology while still allowing minor structural rearrangements to occur.


2010 ◽  
Vol 132 (6) ◽  
pp. 065105 ◽  
Author(s):  
Satoshi Yasuda ◽  
Takashi Yoshidome ◽  
Hiraku Oshima ◽  
Ryota Kodama ◽  
Yuichi Harano ◽  
...  

Biochemistry ◽  
1996 ◽  
Vol 35 (17) ◽  
pp. 5538-5549 ◽  
Author(s):  
Wilfredo Colón ◽  
Gülnur A. Elöve ◽  
L. Paul Wakem ◽  
Fred Sherman ◽  
Heinrich Roder

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