Folding minimal sequences: the lower bound for sequence complexity of globular proteins
| Autor: | Zoran Obradovic, Pedro Romero, A.K. Dunker |
|---|---|
| Rok vydání: | 1999 |
| Předmět: |
Protein Folding
Protein Conformation Globular protein Entropy Biophysics Minimal sequence Ligands Bioinformatics Biochemistry Upper and lower bounds src Homology Domains Combinatorics 03 medical and health sciences Structural Biology Genetics Side chain Animals Humans Entropy (information theory) Amino Acids Molecular Biology 030304 developmental biology Mathematics chemistry.chemical_classification Quantitative Biology::Biomolecules 0303 health sciences 030302 biochemistry & molecular biology Proteins Complexity Cell Biology Models Chemical chemistry Bundle Protein folding Alphabet Alphabet size |
| Zdroj: | FEBS Letters. 462:363-367 |
| ISSN: | 0014-5793 |
| Popis: | Alphabet size and informational entropy, two formal measures of sequence complexity, are herein applied to two prior studies on the folding of minimal proteins. These measures show a designed four-helix bundle to be unlike its natural counterparts but rather more like a coiled-coil dimer. Segments from a simplified sarc homology 3 domain and more than 2 000 000 segments from globular proteins both have lower bounds for alphabet size of 10 and for entropy near 2.9. These values are therefore suggested to be necessary and sufficient for folding into globular proteins having both rigid side chain packing and biological function. |
| Databáze: | OpenAIRE |
| Externí odkaz: |
|
Plný text