Unknown

Dataset Information

0

Prediction of protein folding rates from the amino acid sequence-predicted secondary structure.


ABSTRACT: We present a method for predicting folding rates of proteins from their amino acid sequences only, or rather, from their chain lengths and their helicity predicted from their sequences. The method achieves 82% correlation with experiment over all 64 "two-state" and "multistate" proteins (including two artificial peptides) studied up to now.

SUBMITTER: Ivankov DN 

PROVIDER: S-EPMC428451 | biostudies-literature | 2004 Jun

REPOSITORIES: biostudies-literature

altmetric image

Publications

Prediction of protein folding rates from the amino acid sequence-predicted secondary structure.

Ivankov Dmitry N DN   Finkelstein Alexei V AV  

Proceedings of the National Academy of Sciences of the United States of America 20040607 24


We present a method for predicting folding rates of proteins from their amino acid sequences only, or rather, from their chain lengths and their helicity predicted from their sequences. The method achieves 82% correlation with experiment over all 64 "two-state" and "multistate" proteins (including two artificial peptides) studied up to now. ...[more]

Similar Datasets

| S-EPMC1538837 | biostudies-literature
| S-EPMC2441995 | biostudies-literature
| S-EPMC41034 | biostudies-other
| S-EPMC2863059 | biostudies-literature
| S-EPMC2567998 | biostudies-literature
| S-EPMC9106047 | biostudies-literature
| S-EPMC1153285 | biostudies-other
| S-EPMC5408826 | biostudies-other
| S-EPMC1933209 | biostudies-literature
| S-EPMC4047675 | biostudies-literature