메뉴 건너뛰기




Volumn 300, Issue 2, 2000, Pages 377-402

Effects of side-chain characteristics on stability and oligomerization state of a de novo-designed model coiled-coil: 20 Amino acid substitutions in position 'd'

Author keywords

De novo design; Hydrophobic core substitutions; Oligomerization states; Protein stability; Helical coiled coil

Indexed keywords

AMINO ACID; PROTEIN;

EID: 0034616959     PISSN: 00222836     EISSN: None     Source Type: Journal    
DOI: 10.1006/jmbi.2000.3866     Document Type: Article
Times cited : (214)

References (69)
  • 5
    • 85031604009 scopus 로고
    • A Manual of Methods for the Analytical Ultracentrifuge, Spinco Division of Beckman Instruments, Palo Alto, CA
    • (1969) , pp. 1-100
    • Chervenka, C.H.1
  • 7
    • 0008114412 scopus 로고
    • Proteins, Amino Acids, and Peptides as Ions and Dipolar Ions, Reinhold Publishing Corp., New York
    • (1943) , pp. 370-381
    • Cohn, E.J.1    Edsall, J.T.2
  • 18
    • 0026755510 scopus 로고
    • Contributions of the polar, uncharged amino acids to the stability of staphylococcal nuclease: Evidence for mutational effects on the free energy of the denatured state
    • (1992) Biochemistry , vol.31 , pp. 5717-5728
    • Green, S.M.1    Meeker, A.K.2    Shortle, D.3
  • 28
    • 0021719074 scopus 로고
    • Synthesis of a model protein of defined secondary and quaternary structure; effect of chain length on the stabilization and formation of two-stranded α-helical coiled-coils
    • (1984) J. Biol. Chem. , vol.259 , pp. 13253-13261
    • Lau, S.Y.M.1    Taneja, A.K.2    Hodges, R.S.3
  • 29
    • 0024507791 scopus 로고
    • Alternative packing arrangements in the hydrophobic core of λ repressor
    • (1989) Nature , vol.339 , pp. 31-36
    • Lim, W.A.1    Sauer, T.2
  • 30
    • 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
  • 44
    • 0022555885 scopus 로고
    • Determination and analysis of urea and guanidine hydrochloride denaturation curves
    • (1986) Methods Enzymol. , vol.131 , pp. 266-280
    • Pace, C.N.1
  • 47
    • 0023155210 scopus 로고
    • Tertiary templates for proteins. Use of packing criteria in the enumeration of allowed sequences for different structural classes
    • (1987) J. Mol. Biol. , vol.193 , pp. 775-791
    • Ponder, J.W.1    Richards, F.M.2
  • 54
    • 0024550047 scopus 로고
    • Probing the determinants of protein folding and stability with amino acid substitutions
    • (1989) J. Biol. Chem. , vol.264 , pp. 5315-5318
    • Shortle, D.1
  • 56
  • 60
    • 0033556283 scopus 로고    scopus 로고
    • De novo design of a model peptide sequence to examine the effects of single amino acid substitutions in the hydrophobic core on both stability and oligomerization state of coiled-coils
    • (1999) J. Mol. Biol. , vol.285 , pp. 785-803
    • Wagschal, K.1    Tripet, B.2    Hodges, R.S.3
  • 65
    • 0026650710 scopus 로고
    • Synthetic model proteins: The relative contribution of leucine residues at the nonequivalent positions of the 3-4 hydrophobic repeat to the stability of the two-stranded α-helical coiled-coil
    • (1992) Biochemistry , vol.31 , pp. 5739-5746
    • Zhou, N.E.1    Kay, C.M.2    Hodges, R.S.3
  • 66
  • 69
    • 0027475082 scopus 로고
    • Packing and hydrophobicity effects on protein folding and stability: Effects of beta-branched amino acids, valine and isoleucine, on the formation and stability of two-stranded α-helical coiled coils/ leucine zippers
    • (1993) Protein Sci. , vol.2 , pp. 383-394
    • Zhu, B.-Y.1    Zhou, N.E.2    Kay, C.M.3    Hodges, R.S.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.