scholarly journals The Cold Denatured State of the C-terminal Domain of Protein L9 Is Compact and Contains Both Native and Non-native Structure

2010 ◽  
Vol 132 (13) ◽  
pp. 4669-4677 ◽  
Author(s):  
Bing Shan ◽  
Sebastian McClendon ◽  
Carla Rospigliosi ◽  
David Eliezer ◽  
Daniel P. Raleigh
Keyword(s):  
Native Structure ◽  
Denatured State ◽  
Terminal Domain

Folding mechanism of the C‐terminal domain of nucleophosmin: residual structure in the denatured state and its pathophysiological significance

2009 ◽  
Vol 23 (8) ◽  
pp. 2360-2365 ◽  
Author(s):  
Flavio Scaloni ◽  
Stefano Gianni ◽  
Luca Federici ◽  
Brunangelo Falini ◽  
Maurizio Brunori
Keyword(s):  
Denatured State ◽  
Residual Structure ◽  
Folding Mechanism ◽  
Terminal Domain

Mapping the structures of transition states and intermediates in folding: delineation of pathways at high resolution

1995 ◽  
Vol 348 (1323) ◽  
pp. 11-15 ◽  
Keyword(s):  
Secondary Structure ◽  
Protein Engineering ◽  
Transition State ◽  
Transition States ◽  
Native Structure ◽  
Denatured State ◽  
Chymotrypsin Inhibitor 2 ◽  
Rate Determining Step ◽  
Framework Model ◽  
Individual Domain

The structures of all the intermediates and transition states, from the unfolded state to the native structure, are being determined at the level of individual residues in the folding pathways of barnase and chymotrypsin inhibitor 2 (CI2), using a combination of protein engineering and nuclear magnetic resonance methods. Barnase appears to refold according to a classical framework model in which elements of secondary structure are flickeringly present in the denatured state, consolidate as the reaction proceeds and, when nearly fully formed, dock in the rate-determining step. Unlike barnase, CI2 folds without a kinetically significant folding intermediate. The transition state for its formation has no fully formed elements of secondary structure, and the transition state is like an expanded form of the native structure. CI2 probably represents the folding of an individual domain in a larger protein, whereas barnase represents the folding of a multi-domain protein. The protein engineering methods are being extended to map the pathway in the presence of molecular chaperones. There are parallels between the folding of barnase when bound to GroEL and in solution.

Sign in / Sign up

Export Citation Format

Share Document