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Volumn 305, Issue 3, 2001, Pages 619-631

Achieving stability and conformational specificity in designed proteins via binary patterning

Author keywords

Binary patterning; Conformational specificity; Protein design; Protein stability; Random energy model

Indexed keywords

AMINO ACID SEQUENCE; ARTICLE; HYDROPHOBICITY; METHODOLOGY; PRIORITY JOURNAL; PROTEIN AGGREGATION; PROTEIN CONFORMATION; PROTEIN DOMAIN; PROTEIN STABILITY; THERMOSTABILITY;

EID: 0035910266     PISSN: 00222836     EISSN: None     Source Type: Journal    
DOI: 10.1006/jmbi.2000.4319     Document Type: Article
Times cited : (64)

References (40)
  • 7
    • 0028846974 scopus 로고
    • Binary patterning of polar and nonpolar amino acids in the sequences and structures of native proteins
    • (1995) Protein Sci. , vol.4 , pp. 2032-2039
    • West, M.W.1    Hecht, M.H.2
  • 9
    • 0034712651 scopus 로고    scopus 로고
    • Cooperative thermal denaturation of proteins designed by binary patterning of polar and nonpolar amino acids
    • (2000) Biochemistry , vol.39 , pp. 4603-4607
    • Roy, S.1    Hecht, M.H.2
  • 14
    • 0025317840 scopus 로고
    • Reverse hydrophobic effects relieved by amino-acid substitutions at a protein surface
    • (1990) Nature , vol.344 , pp. 363-364
    • Pakula, A.A.1    Sauer, R.T.2
  • 16
    • 0029008590 scopus 로고
    • A buried polar interaction imparts structural uniqueness in a designed heterodimeric coiled coil
    • (1995) Biochemistry , vol.34 , pp. 8642-8648
    • Lumb, K.J.1    Kim, P.S.2
  • 24
    • 0031932169 scopus 로고    scopus 로고
    • Protein aggregation: Folding aggregates, inclusion bodies and amyloid
    • (1998) Fold. Des. , vol.3
    • Fink, A.L.1
  • 27
    • 0021107965 scopus 로고
    • Solvent accessible surfaces of proteins and nucleic acids
    • (1983) Science , vol.221 , pp. 709-713
    • Connolly, M.L.1
  • 33
    • 0028212927 scopus 로고
    • Efficient rotamer elimination applied to protein side-chains and related spin-glasses
    • (1994) Biophys. J. , vol.66 , pp. 1335-1340
    • Goldstein, R.F.1
  • 34
    • 0001686478 scopus 로고    scopus 로고
    • Radical performance enhancements for combinatorial optimization algorithms based on the dead-end elimination theorem
    • (1998) J. Comput. Chem. , vol.19 , pp. 1505-1514
    • Gordon, D.B.1    Mayo, S.L.2
  • 37
  • 38
    • 0022555885 scopus 로고
    • Determination and analysis of urea and guanidine hydrochloride denaturation curves
    • (1986) Methods Enzymol. , vol.131 , pp. 266-280
    • Pace, N.C.1
  • 39
    • 0023697408 scopus 로고
    • Unfolding free-energy changes determined by the linear extrapolation method. 1. Unfolding of phenylmethanesulfonyl α-chymotrypsin using different denaturants
    • (1988) Biochemistry , vol.27 , pp. 8063-8068
    • Santoro, M.M.1    Bolen, D.W.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.