Unknown

Dataset Information

0

Structure-Based Prediction of Protein-Folding Transition Paths.


ABSTRACT: We propose a general theory to describe the distribution of protein-folding transition paths. We show that transition paths follow a predictable sequence of high-free-energy transient states that are separated by free-energy barriers. Each transient state corresponds to the assembly of one or more discrete, cooperative units, which are determined directly from the native structure. We show that the transition state on a folding pathway is reached when a small number of critical contacts are formed between a specific set of substructures, after which folding proceeds downhill in free energy. This approach suggests a natural resolution for distinguishing parallel folding pathways and provides a simple means to predict the rate-limiting step in a folding reaction. Our theory identifies a common folding mechanism for proteins with diverse native structures and establishes general principles for the self-assembly of polymers with specific interactions.

SUBMITTER: Jacobs WM 

PROVIDER: S-EPMC5018131 | biostudies-literature | 2016 Sep

REPOSITORIES: biostudies-literature

altmetric image

Publications

Structure-Based Prediction of Protein-Folding Transition Paths.

Jacobs William M WM   Shakhnovich Eugene I EI  

Biophysical journal 20160901 5


We propose a general theory to describe the distribution of protein-folding transition paths. We show that transition paths follow a predictable sequence of high-free-energy transient states that are separated by free-energy barriers. Each transient state corresponds to the assembly of one or more discrete, cooperative units, which are determined directly from the native structure. We show that the transition state on a folding pathway is reached when a small number of critical contacts are form  ...[more]

Similar Datasets

| S-EPMC3529084 | biostudies-literature
| S-EPMC3092838 | biostudies-literature
| S-EPMC8670488 | biostudies-literature
| S-EPMC10600234 | biostudies-literature
| S-EPMC10513300 | biostudies-literature
| S-EPMC2656149 | biostudies-literature
| S-EPMC3207166 | biostudies-literature
| S-EPMC6486767 | biostudies-literature
| S-EPMC2863059 | biostudies-literature
| S-EPMC3691887 | biostudies-literature