Packing-based difference of structural features between thermophilic and mesophilic proteins.
Twenty pairs of thermophilic and mesophilic proteins were compared in terms of residue packing distribution to obtain structural features related to protein thermostability. Based on residue packing concept, structural features of residues such as residue packing distribution, inner/outer position, secondary structure and water solvation were investigated. The statistical tests revealed that higher frequency in well-packed state of residues, lower frequency in exposed state and higher frequency in well-packed state of inner positioned residues, and higher frequency in well-packed state of 3/10 helix residues could be general structural features thermophilic proteins have.
Pack
Seung Pil
SP
School of Chemical Engineering, Seoul National University, Seoul 151-742, Republic of Korea.
Yoo
Young Je
YJ
D019843:Archaeal Proteins / Q000737:chemistry*; D001426:Bacterial Proteins / Q000737:chemistry*; D017510:Protein Folding; D017433:Protein Structure, Secondary; D013816:Thermodynamics
D019843:Archaeal Proteins; D001426:Bacterial Proteins