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Volumn 1, Issue 1, 1986, Pages 23-33

The design and production of semisynthetic ribonucleases with increased thermostability by incorporation of S‐peptide analogues with enhanced helical stability

Author keywords

framework model of folding; peptide helix; protein stability

Indexed keywords

C PEPTIDE; RIBONUCLEASE;

EID: 0023036230     PISSN: 08873585     EISSN: 10970134     Source Type: Journal    
DOI: 10.1002/prot.340010106     Document Type: Article
Times cited : (95)

References (39)
  • 4
    • 0021145557 scopus 로고
    • Disulfide bond engineered into T4 lysozyme: stabilization of protein toward thermal inactivation
    • (1984) Science , vol.226 , pp. 555-557
    • Perry, L.J.1    Wetzel, R.2
  • 17
    • 84872631302 scopus 로고
    • A spectrophotometric method for the measurement of ribonuclease activity
    • (1946) J. Biol. Chem. , vol.164 , pp. 563-568
    • Kunitz, M.1
  • 34
    • 84985698770 scopus 로고
    • An equilibrium folding intermediate detected in the thermal unfolding transition of ribonuclease S by circular dichroism
    • (1981) Biopolymers , vol.20 , pp. 1459-1480
    • Labhardt, A.M.1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.