Document Detail

Protein thermostability: structure-based difference of amino acid between thermophilic and mesophilic proteins.
MedLine Citation:
PMID:  15246663     Owner:  NLM     Status:  MEDLINE    
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.
Seung Pil Pack; Young Je Yoo
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Publication Detail:
Type:  Comparative Study; Evaluation Studies; Journal Article; Research Support, Non-U.S. Gov't; Validation Studies    
Journal Detail:
Title:  Journal of biotechnology     Volume:  111     ISSN:  0168-1656     ISO Abbreviation:  J. Biotechnol.     Publication Date:  2004 Aug 
Date Detail:
Created Date:  2004-07-12     Completed Date:  2004-11-30     Revised Date:  2006-11-15    
Medline Journal Info:
Nlm Unique ID:  8411927     Medline TA:  J Biotechnol     Country:  Netherlands    
Other Details:
Languages:  eng     Pagination:  269-77     Citation Subset:  IM    
School of Chemical Engineering, Seoul National University, Seoul 151-742, South Korea.
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MeSH Terms
Amino Acid Sequence
Amino Acid Substitution
Bacterial Proteins / chemistry*
Enzyme Stability*
Euryarchaeota / metabolism*
Molecular Sequence Data
Protein Denaturation
Proteins / chemistry
Sequence Alignment*
Sequence Analysis, Protein / methods*
Sequence Homology, Amino Acid
Structure-Activity Relationship
Reg. No./Substance:
0/Bacterial Proteins; 0/Proteins

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