Different packing of external residues can explain differences in the thermostability of proteins from thermophilic and mesophilic organisms.
Anna V. GlyakinaSergiy O. GarbuzynskiyMichail Yu. LobanovOxana V. GalzitskayaPublished in: Bioinform. (2007)
Keyphrases
- physicochemical properties
- amino acids
- protein sequences
- protein structure
- protein function
- amino acid sequences
- protein folding
- biological processes
- amino acid composition
- protein structure alignment
- statistically significant
- protein protein interactions
- molecular biology
- secondary structure
- protein protein
- computational methods
- protein structure prediction
- protein chains
- phylogenetic trees
- contact map
- protein structural
- computational biology
- experimentally determined
- protein interaction networks
- dna sequences
- sequence analysis
- coarse grained
- metabolic pathways
- predicting protein
- human genome
- sequence alignment
- binding sites
- gene ontology
- functional modules
- sequenced genomes
- high throughput