Of the globular proteins, cytochrome c (cyt c) has been used extensively as a model system for folding studies. Here we analyse the folding pathway of different cyt c proteins from prokaryotes and eukaryotes, and attempt to single out general correlations between structural determinants and folding mechanisms. Recent studies provide evidence that the folding pathway of several cyt c proteins involves the formation of a partially structured intermediate. Using state-of-the-art kinetic analysis on published data, we show that such a folding intermediate is an obligatory on-pathway species that might represent either a defined local minimum in the reaction coordinate or an unstable high-energy state. Available data also indicate that some esse...
pr. T ste ge way so that each higher energy partially unfolded form includes all of the *Correspondi...
The alkaline transition of cytochrome c is a model for protein structural switching in which the nor...
We have investigated the folding dynamics of Thermus thermophilus cytochrome c_(552) by time-resolve...
: Understanding the role of partially folded intermediate states in the folding mechanism of a prote...
Abstract Several investigators have highlighted a correlation between the basic features of the fold...
How a polypeptide chain folds into its final native structure as it comes off the ribosome is the fi...
Understanding the role of partially folded intermediate states in the folding mechanism of a protein...
Cytochrome c(551) (cyt c(551)) from Pseudomonas aeruginosa is a small protein (82 residues) that fol...
The folding mechanism of many proteins involves the population of partially organized structures en ...
The protein folding field has undoubtedly benefited from studies on the folding mechanism of c-type ...
AbstractBackground: Experimental and theoretical studies of protein folding suggest that the free-en...
For many proteins, compact states appear long before the rate-limiting step in formation of the nati...
Previous results indicate that the folding pathways of cytochrome c and other proteins progressively...
Kinetic studies of the early events in cytochrome c folding are reviewed with a focus on the evidenc...
Proteins may fold via parallel routes partitioned by the relative effect of solvent conditions on th...
pr. T ste ge way so that each higher energy partially unfolded form includes all of the *Correspondi...
The alkaline transition of cytochrome c is a model for protein structural switching in which the nor...
We have investigated the folding dynamics of Thermus thermophilus cytochrome c_(552) by time-resolve...
: Understanding the role of partially folded intermediate states in the folding mechanism of a prote...
Abstract Several investigators have highlighted a correlation between the basic features of the fold...
How a polypeptide chain folds into its final native structure as it comes off the ribosome is the fi...
Understanding the role of partially folded intermediate states in the folding mechanism of a protein...
Cytochrome c(551) (cyt c(551)) from Pseudomonas aeruginosa is a small protein (82 residues) that fol...
The folding mechanism of many proteins involves the population of partially organized structures en ...
The protein folding field has undoubtedly benefited from studies on the folding mechanism of c-type ...
AbstractBackground: Experimental and theoretical studies of protein folding suggest that the free-en...
For many proteins, compact states appear long before the rate-limiting step in formation of the nati...
Previous results indicate that the folding pathways of cytochrome c and other proteins progressively...
Kinetic studies of the early events in cytochrome c folding are reviewed with a focus on the evidenc...
Proteins may fold via parallel routes partitioned by the relative effect of solvent conditions on th...
pr. T ste ge way so that each higher energy partially unfolded form includes all of the *Correspondi...
The alkaline transition of cytochrome c is a model for protein structural switching in which the nor...
We have investigated the folding dynamics of Thermus thermophilus cytochrome c_(552) by time-resolve...