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Volumn 10, Issue 7, 2002, Pages 961-971

Structural and thermodynamic characterization of the DNA binding properties of a triple alanine mutant of MATα2

Author keywords

Crystal structure; Homeodomain; Isothermal titration calorimetry; MAT 2; Protein DNA interactions; Transcription

Indexed keywords

ALANINE; DNA BINDING PROTEIN; PROTEIN; PROTEIN MATALPHA2; PROTEIN MCM1; UNCLASSIFIED DRUG; DNA; HOMEODOMAIN PROTEIN; REPRESSOR PROTEIN;

EID: 0036651455     PISSN: 09692126     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0969-2126(02)00790-6     Document Type: Article
Times cited : (11)

References (30)
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    • Mak, A.1    Johnson, A.D.2
  • 8
    • 0027527069 scopus 로고
    • Yeast a1 and alpha 2 homeodomain proteins form a DNA-binding activity with properties distinct from those of either protein
    • (1993) J. Mol. Biol. , vol.233 , pp. 359-371
    • Goutte, C.1    Johnson, A.D.2
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    • Side-chain conformational entropy in protein unfolded states
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* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.