Protein thermostability: structure-based difference of amino acid between thermophilic and mesophilic proteins.
Structural distributions of each amino acid were compared between 20 pairs of thermophilic and mesophilic proteins to obtain thermostable factors. Five kinds of residual structure states such as fully-exposed, exposed, partially exposed (or partially buried), buried, well-buried states were considered for analyzing the structural patterns of amino acids. The statistical tests revealed that lower frequency in partially exposed state of SER, lower frequency in exposed state and higher frequency in well-buried state of ALA, higher frequency in buried state of GLU, higher frequency in exposed state of ARG, etc. could be critical factors related with protein thermostability.
Pack
Seung Pil
SP
School of Chemical Engineering, Seoul National University, Seoul 151-742, South Korea.
Yoo
Young Je
YJ
D000595:Amino Acid Sequence; D019943:Amino Acid Substitution; D001426:Bacterial Proteins / Q000737:chemistry*; D004795:Enzyme Stability; D019605:Euryarchaeota / Q000378:metabolism*; D008969:Molecular Sequence Data; D011489:Protein Denaturation; D011506:Proteins / Q000737:chemistry; D016415:Sequence Alignment; D020539:Sequence Analysis, Protein / Q000379:methods*; D017386:Sequence Homology, Amino Acid; D013329:Structure-Activity Relationship
D001426:Bacterial Proteins; D011506:Proteins