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Volumn 11, Issue 1, 2002, Pages 27-35

N-terminal contributions of the γ-subunit of fetal hemoglobin to its tetramer strength: Remote effects at subunit contacts

Author keywords

Hemoglobin; Long range interaction; Site directed mutagenesis

Indexed keywords

AMINO ACID; ASPARTIC ACID; DIMER; GLUTAMINE; GLYCINE; HEMOGLOBIN A; HEMOGLOBIN F; LEUCINE; OXYGEN; PHENYLALANINE; PROLINE; PROTEIN SUBUNIT; PROTEINASE; TETRAMER; VALINE;

EID: 0036135327     PISSN: 09618368     EISSN: None     Source Type: Journal    
DOI: 10.1110/ps.ps.30602     Document Type: Article
Times cited : (15)

References (18)
  • 9
    • 0035852826 scopus 로고    scopus 로고
    • The acetylation state of human fetal hemoglobin modulates the strength of its subunit interactions: Long-range effects and implications for histone interactions in the nucleosome
    • (2001) Biochemistry , vol.40 , pp. 1635-1639
    • Manning, L.R.1    Manning, J.M.2
  • 12
  • 16


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.