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Volumn 206, Issue 2, 1989, Pages 397-406

Engineering protein thermal stability. Sequence statistics point to residue substitutions in α-helices

Author keywords

[No Author keywords available]

Indexed keywords

AMINO ACID; BACTERIAL PROTEIN; FUNGAL PROTEIN; PROTEIN;

EID: 0024974452     PISSN: 00222836     EISSN: None     Source Type: Journal    
DOI: 10.1016/0022-2836(89)90488-9     Document Type: Article
Times cited : (284)

References (52)
  • 52
    • 0023413575 scopus 로고
    • Note added in proof. An examination of the first and second base positions in the nucleotide codons for the amino acids involved in the Table 3 exchanges showed that the G and C content of the protein coding DNA in thermophiles would be increased from eight of the ten amino acid substitutions. The remaining two (Gly to Ala and Ser to Thr) are neutral with respect to the G + C composition. Thus, the residue exchanges not only thermally stabilize the protein but also the DNA by increasing the number of hydrogen bonds through G · C base pairs. The authors are grateful to Chris Sander who suggested examination of this issue.
    • (1987) Biological Chemistry Hoppe-Seyler , vol.368 , pp. 1167-1177
    • Zülli1    Weber2    Zuber3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.