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Volumn 337, Issue 5, 2004, Pages 1195-1205

Amino acid propensities are position-dependent throughout the length of α-helices

Author keywords

de novo design; Fractional solvent accessibility; Helix capping; Hydrophobicity; Position dependent propensity

Indexed keywords

AMINO ACID;

EID: 1842523274     PISSN: 00222836     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.jmb.2004.02.004     Document Type: Article
Times cited : (68)

References (26)
  • 1
    • 0018110116 scopus 로고
    • Prediction of the secondary structure of proteins from their amino acid sequence
    • Chou P.Y., Fasman G.D. Prediction of the secondary structure of proteins from their amino acid sequence. Advan. Enzymol. Relat. Areas Mol. Biol. 47:1978;45-148.
    • (1978) Advan. Enzymol. Relat. Areas Mol. Biol. , vol.47 , pp. 45-148
    • Chou, P.Y.1    Fasman, G.D.2
  • 2
    • 0027212028 scopus 로고
    • Design of helix ends. Amino acid preferences, hydrogen bonding and electrostatic interactions
    • Dasgupta S., Bell J.A. Design of helix ends. Amino acid preferences, hydrogen bonding and electrostatic interactions. Int. J. Pept. Protein Res. 41:1993;499-511.
    • (1993) Int. J. Pept. Protein Res. , vol.41 , pp. 499-511
    • Dasgupta, S.1    Bell, J.A.2
  • 3
    • 0028016389 scopus 로고
    • Structure prediction of proteins - Where are we now?
    • Rost B., Sander C. Structure prediction of proteins - where are we now? Curr. Opin. Biotechnol. 5:1994;372-380.
    • (1994) Curr. Opin. Biotechnol. , vol.5 , pp. 372-380
    • Rost, B.1    Sander, C.2
  • 4
    • 0029188711 scopus 로고
    • Predicting the conformation of proteins from sequences. Progress and future progress
    • Benner S.A. Predicting the conformation of proteins from sequences. Progress and future progress. J. Mol. Recognit. 8:1995;9-28.
    • (1995) J. Mol. Recognit. , vol.8 , pp. 9-28
    • Benner, S.A.1
  • 5
    • 0029155035 scopus 로고
    • Helix design, prediction and stability
    • Munoz V., Serrano L. Helix design, prediction and stability. Curr. Opin. Biotechnol. 6:1995;382-386.
    • (1995) Curr. Opin. Biotechnol. , vol.6 , pp. 382-386
    • Munoz, V.1    Serrano, L.2
  • 6
    • 0029302287 scopus 로고
    • Structure prediction. How good are we?
    • Russell R.B., Sternberg M.J. Structure prediction. How good are we? Curr. Biol. 5:1995;488-490.
    • (1995) Curr. Biol. , vol.5 , pp. 488-490
    • Russell, R.B.1    Sternberg, M.J.2
  • 7
    • 0028815464 scopus 로고
    • Protein structure prediction: Recognition of primary, secondary, and tertiary structural features from amino acid sequence
    • Eisenhaber F., Persson B., Argos P. Protein structure prediction: recognition of primary, secondary, and tertiary structural features from amino acid sequence. Crit. Rev. Biochem. Mol. Biol. 30:1995;1-94.
    • (1995) Crit. Rev. Biochem. Mol. Biol. , vol.30 , pp. 1-94
    • Eisenhaber, F.1    Persson, B.2    Argos, P.3
  • 8
    • 0024290488 scopus 로고
    • Helix signals in proteins
    • Presta L.G., Rose G.D. Helix signals in proteins. Science. 240:1988;1632-1641.
    • (1988) Science , vol.240 , pp. 1632-1641
    • Presta, L.G.1    Rose, G.D.2
  • 9
    • 0029020484 scopus 로고
    • N- and C-capping preferences for all 20 amino acids in alpha-helical peptides
    • Doig A.J., Baldwin R.L. N- and C-capping preferences for all 20 amino acids in alpha-helical peptides. Protein Sci. 4:1995;1325-1336.
    • (1995) Protein Sci. , vol.4 , pp. 1325-1336
    • Doig, A.J.1    Baldwin, R.L.2
  • 10
    • 0035106699 scopus 로고    scopus 로고
    • Effect of the N1 residue on the stability of the alpha-helix for all 20 amino acids
    • Cochran D.A., Penel S., Doig A.J. Effect of the N1 residue on the stability of the alpha-helix for all 20 amino acids. Protein Sci. 10:2001;463-470.
    • (2001) Protein Sci. , vol.10 , pp. 463-470
    • Cochran, D.A.1    Penel, S.2    Doig, A.J.3
  • 11
    • 0034974668 scopus 로고    scopus 로고
    • Effect of the N2 residue on the stability of the alpha-helix for all 20 amino acids
    • Cochran D.A., Doig A.J. Effect of the N2 residue on the stability of the alpha-helix for all 20 amino acids. Protein Sci. 10:2001;1305-1311.
    • (2001) Protein Sci. , vol.10 , pp. 1305-1311
    • Cochran, D.A.1    Doig, A.J.2
  • 12
    • 0032101291 scopus 로고    scopus 로고
    • Dissecting alpha-helices: Position-specific analysis of alpha-helices in globular proteins
    • Kumar S., Bansal M. Dissecting alpha-helices: position-specific analysis of alpha-helices in globular proteins. Proteins: Struct. Funct. Genet. 31:1998;460-476.
    • (1998) Proteins: Struct. Funct. Genet. , vol.31 , pp. 460-476
    • Kumar, S.1    Bansal, M.2
  • 13
    • 0028205447 scopus 로고
    • Enlarged representative set of protein structures
    • Hobohm U., Sander C. Enlarged representative set of protein structures. Protein Sci. 3:1994;522-524.
    • (1994) Protein Sci. , vol.3 , pp. 522-524
    • Hobohm, U.1    Sander, C.2
  • 14
    • 0032488824 scopus 로고    scopus 로고
    • Stereochemical punctuation marks in protein structures: Glycine and proline containing helix stop signals
    • Gunasekaran K., Nagarajaram H.A., Ramakrishnan C., Balaram P. Stereochemical punctuation marks in protein structures: glycine and proline containing helix stop signals. J. Mol. Biol. 275:1998;917-932.
    • (1998) J. Mol. Biol. , vol.275 , pp. 917-932
    • Gunasekaran, K.1    Nagarajaram, H.A.2    Ramakrishnan, C.3    Balaram, P.4
  • 17
    • 0021762736 scopus 로고
    • Alpha secondary structures generate weak but recurrent periodicity in proteins
    • Wuilmart C., Urbain J. Alpha secondary structures generate weak but recurrent periodicity in proteins. Eur. J. Biochem. 139:1984;35-40.
    • (1984) Eur. J. Biochem. , vol.139 , pp. 35-40
    • Wuilmart, C.1    Urbain, J.2
  • 18
    • 0024290472 scopus 로고
    • Amino acid preferences for specific locations at the ends of alpha helices
    • Richardson J.S., Richardson D.C. Amino acid preferences for specific locations at the ends of alpha helices. Science. 240:1988;1648-1652.
    • (1988) Science , vol.240 , pp. 1648-1652
    • Richardson, J.S.1    Richardson, D.C.2
  • 19
    • 0030005250 scopus 로고    scopus 로고
    • Solvation energies of amino acid side chains and backbone in a family of host-guest pentapeptides
    • Wimley W.C., Creamer T.P., White S.H. Solvation energies of amino acid side chains and backbone in a family of host-guest pentapeptides. Biochemistry. 35:1996;5109-5124.
    • (1996) Biochemistry , vol.35 , pp. 5109-5124
    • Wimley, W.C.1    Creamer, T.P.2    White, S.H.3
  • 20
    • 0019065166 scopus 로고
    • Local hydrophobicity stabilizes secondary structures in proteins
    • Kanehisa M.I., Tsong T.Y. Local hydrophobicity stabilizes secondary structures in proteins. Biopolymers. 19:1980;1617-1628.
    • (1980) Biopolymers , vol.19 , pp. 1617-1628
    • Kanehisa, M.I.1    Tsong, T.Y.2
  • 21
    • 0023972269 scopus 로고
    • Prediction of protein helix content from an autocorrelation analysis of sequence hydrophobicities
    • Horne D.S. Prediction of protein helix content from an autocorrelation analysis of sequence hydrophobicities. Biopolymers. 27:1988;451-477.
    • (1988) Biopolymers , vol.27 , pp. 451-477
    • Horne, D.S.1
  • 22
    • 0000499414 scopus 로고
    • Prediction of secondary structure of proteins by means of hydrophobicity profiles
    • Cid H., Bunster M., Arriagada E., Campos M. Prediction of secondary structure of proteins by means of hydrophobicity profiles. FEBS Letters. 150:1982;247-254.
    • (1982) FEBS Letters , vol.150 , pp. 247-254
    • Cid, H.1    Bunster, M.2    Arriagada, E.3    Campos, M.4
  • 23
    • 0024351832 scopus 로고
    • Prediction of protein helices with a derivative of the strip-of-helix hydrophobicity algorithm
    • Reyes V.E., Phillips L., Humphreys R.E., Lew R.A. Prediction of protein helices with a derivative of the strip-of-helix hydrophobicity algorithm. J. Biol. Chem. 264:1989;12854-12858.
    • (1989) J. Biol. Chem. , vol.264 , pp. 12854-12858
    • Reyes, V.E.1    Phillips, L.2    Humphreys, R.E.3    Lew, R.A.4
  • 24
    • 0020997912 scopus 로고
    • Dictionary of protein secondary structure: Pattern recognition of hydrogen-bonded and geometrical features
    • Kabsch W., Sander C. Dictionary of protein secondary structure: pattern recognition of hydrogen-bonded and geometrical features. Biopolymers. 22:1983;2577-2637.
    • (1983) Biopolymers , vol.22 , pp. 2577-2637
    • Kabsch, W.1    Sander, C.2
  • 25
    • 0019072784 scopus 로고
    • Solvent accessibility, protein surfaces, and protein folding
    • Lesk A.M., Chothia C. Solvent accessibility, protein surfaces, and protein folding. Biophys. J. 32:1980;35-47.
    • (1980) Biophys. J. , vol.32 , pp. 35-47
    • Lesk, A.M.1    Chothia, C.2
  • 26
    • 0030691777 scopus 로고    scopus 로고
    • C-capping and helix stability: The Pro C-capping motif
    • Prieto J., Serrano L. C-capping and helix stability: the Pro C-capping motif. J. Mol. Biol. 274:1997;276-288.
    • (1997) J. Mol. Biol. , vol.274 , pp. 276-288
    • Prieto, J.1    Serrano, L.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.