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Volumn 2014, Issue , 2014, Pages

Prediction and analysis of surface hydrophobic residues in tertiary structure of proteins

Author keywords

[No Author keywords available]

Indexed keywords

PROTEIN; PROTEIN SURFACE HYDROPHOBIC RESIDUE; SOLVENT; UNCLASSIFIED DRUG; DNA DIRECTED DNA POLYMERASE BETA;

EID: 84896265719     PISSN: None     EISSN: 1537744X     Source Type: Journal    
DOI: 10.1155/2014/971258     Document Type: Article
Times cited : (65)

References (29)
  • 1
    • 0025370815 scopus 로고
    • Dominant forces in protein folding
    • DOI 10.1021/bi00483a001
    • Dill K. A., Dominant forces in protein folding. Biochemistry 1990 29 31 7133 7155 2-s2.0-0025370815 (Pubitemid 20230041)
    • (1990) Biochemistry , vol.29 , Issue.31 , pp. 7133-7155
    • Dill, K.A.1
  • 2
    • 0008863560 scopus 로고
    • Some factors in the interpretation of protein denaturation
    • 2-s2.0-0008863560 10.1016/S0065-3233(08)60608-7
    • Kauzmann W., Some factors in the interpretation of protein denaturation. Advances in Protein Chemistry 1959 14 1 63 2-s2.0-0008863560 10.1016/S0065-3233(08)60608-7
    • (1959) Advances in Protein Chemistry , vol.14 , pp. 1-63
    • Kauzmann, W.1
  • 3
    • 85021467943 scopus 로고
    • Structure and function of haemoglobin: II. Some relations between polypeptide chain configuration and amino acid sequence
    • 10.1016/S0022-2836(65)80134-6
    • Perutz M. F., Kendrew J. C., Watson H. C., Structure and function of haemoglobin: II. some relations between polypeptide chain configuration and amino acid sequence. Journal of Molecular Biology 1965 13 3 669 678 10.1016/S0022-2836(65)80134-6
    • (1965) Journal of Molecular Biology , vol.13 , Issue.3 , pp. 669-678
    • Perutz, M.F.1    Kendrew, J.C.2    Watson, H.C.3
  • 5
    • 0016606973 scopus 로고
    • Structural invariants in protein folding
    • 2-s2.0-0016606973
    • Chothia C., Structural invariants in protein folding. Nature 1975 254 5498 304 308 2-s2.0-0016606973
    • (1975) Nature , vol.254 , Issue.5498 , pp. 304-308
    • Chothia, C.1
  • 6
    • 0022412192 scopus 로고
    • Hydrophobicity of amino acid residues in globular proteins
    • Rose G. D., Geselowitz A. R., Lesser G. J., Hydrophobicity of amino acid residues in globular proteins. Science 1985 229 4716 834 838 2-s2.0-0022412192 (Pubitemid 16246583)
    • (1985) Science , vol.229 , Issue.4716 , pp. 834-838
    • Rose, G.D.1    Geselowitz, A.R.2    Lesser, G.J.3
  • 7
    • 0026076664 scopus 로고
    • Extracting hydrophobic free energies from experimental data: Relationship to protein folding and theoretical models
    • 2-s2.0-0026076664
    • Sharp K. A., Nicholls A., Friedman R., Honig B., Extracting hydrophobic free energies from experimental data: relationship to protein folding and theoretical models. Biochemistry 1991 30 40 9686 9697 2-s2.0-0026076664
    • (1991) Biochemistry , vol.30 , Issue.40 , pp. 9686-9697
    • Sharp, K.A.1    Nicholls, A.2    Friedman, R.3    Honig, B.4
  • 8
    • 4544246089 scopus 로고    scopus 로고
    • Mutation of exposed hydrophobic amino acids to arginine to increase protein stability
    • 2-s2.0-4544246089 10.1186/1471-2091-5-1
    • Strub C., Alies C., Lougarre A., Ladurantie C., Czaplicki J., Fournier D., Mutation of exposed hydrophobic amino acids to arginine to increase protein stability. BMC Biochemistry 2004 5, article 9 1 6 2-s2.0-4544246089 10.1186/1471-2091-5-1
    • (2004) BMC Biochemistry , vol.59 , pp. 1-6
    • Strub, C.1    Alies, C.2    Lougarre, A.3    Ladurantie, C.4    Czaplicki, J.5    Fournier, D.6
  • 9
    • 33646030668 scopus 로고    scopus 로고
    • Role of solvent accessibility in structure based drug design
    • Gromiha M. M., Ahmad S., Role of solvent accessibility in structure based drug design. Current Computer-Aided Drug Design 2005 1 223 235
    • (2005) Current Computer - Aided Drug Design , vol.1 , pp. 223-235
    • Gromiha, M.M.1    Ahmad, S.2
  • 10
    • 1442310611 scopus 로고    scopus 로고
    • Improvement in prediction of solvent accessibility by probability profiles
    • Gianese G., Bossa F., Pascarella S., Improvement in prediction of solvent accessibility by probability profiles. Protein Engineering 2003 16 12 987 992 2-s2.0-1442310611 (Pubitemid 38281749)
    • (2003) Protein Engineering , vol.16 , Issue.12 , pp. 987-992
    • Gianese, G.1    Bossa, F.2    Pascarella, S.3
  • 11
    • 0028109886 scopus 로고
    • Conservation and prediction of solvent accessibility in protein families
    • DOI 10.1002/prot.340200303
    • Rost B., Sander C., Conservation and prediction of solvent accessibility in protein families. Proteins 1994 20 3 216 226 2-s2.0-0028109886 10.1002/prot.340200303 (Pubitemid 24378913)
    • (1994) Proteins: Structure, Function and Genetics , vol.20 , Issue.3 , pp. 216-226
    • Rost, B.1    Sander, C.2
  • 12
    • 0029889988 scopus 로고    scopus 로고
    • PHD: Predicting one-dimensional protein structure by profile-based neural networks
    • 2-s2.0-0029889988
    • Rost B., PHD: Predicting one-dimensional protein structure by profile-based neural networks. Methods in Enzymology 1996 266 525 539 2-s2.0-0029889988
    • (1996) Methods in Enzymology , vol.266 , pp. 525-539
    • Rost, B.1
  • 13
    • 0035189668 scopus 로고    scopus 로고
    • New method for accurate prediction of solvent accessibility from protein sequence
    • Li X., Pan X. M., New method for accurate prediction of solvent accessibility from protein sequence. Proteins 2001 42 1 1 5
    • (2001) Proteins , vol.42 , Issue.1 , pp. 1-5
    • Li, X.1    Pan, X.M.2
  • 15
    • 0037103004 scopus 로고    scopus 로고
    • Prediction of protein solvent accessibility using Support Vector Machines
    • DOI 10.1002/prot.10176
    • Yuan Z., Burrage K., Mattick J. S., Prediction of protein solvent accessibility using support vector machines. Proteins 2002 48 3 566 570 2-s2.0-0037103004 10.1002/prot.10176 (Pubitemid 34810420)
    • (2002) Proteins: Structure, Function and Genetics , vol.48 , Issue.3 , pp. 566-570
    • Yuan, Z.1    Burrage, K.2    Mattick, J.S.3
  • 16
    • 35748959334 scopus 로고    scopus 로고
    • PIQSI: Protein quaternary structure investigation
    • DOI 10.1016/j.str.2007.09.019, PII S0969212607003760
    • Levy E. D., PiQSi: protein quaternary structure investigation. Structure 2007 15 11 1364 1367 2-s2.0-35748959334 10.1016/j.str.2007.09.019 (Pubitemid 350051933)
    • (2007) Structure , vol.15 , Issue.11 , pp. 1364-1367
    • Levy, E.D.1
  • 19
    • 0015222647 scopus 로고
    • The interpretation of protein structures: Estimation of static accessibility
    • 2-s2.0-0015222647
    • Lee B., Richards F. M., The interpretation of protein structures: estimation of static accessibility. Journal of Molecular Biology 1971 55 3 379 400 2-s2.0-0015222647
    • (1971) Journal of Molecular Biology , vol.55 , Issue.3 , pp. 379-400
    • Lee, B.1    Richards, F.M.2
  • 20
    • 0025912338 scopus 로고
    • Molecular recognition. Conformational analysis of limited proteolytic sites and serine proteinase protein inhibitors
    • 2-s2.0-0025912338
    • Hubbard S. J., Campbell S. F., Thornton J. M., Molecular recognition. conformational analysis of limited proteolytic sites and serine proteinase protein inhibitors. Journal of Molecular Biology 1991 220 2 507 530 2-s2.0-0025912338
    • (1991) Journal of Molecular Biology , vol.220 , Issue.2 , pp. 507-530
    • Hubbard, S.J.1    Campbell, S.F.2    Thornton, J.M.3
  • 21
    • 0030581145 scopus 로고    scopus 로고
    • The use of amino acid patterns of classified helices and strands in secondary structure prediction
    • DOI 10.1006/jmbi.1996.0397
    • Zhu Z.-Y., Blundell T. L., The use of amino acid patterns of classified helices and strands in secondary structure prediction. Journal of Molecular Biology 1996 260 2 261 276 2-s2.0-0030581145 10.1006/jmbi.1996.0397 (Pubitemid 26245364)
    • (1996) Journal of Molecular Biology , vol.260 , Issue.2 , pp. 261-276
    • Zhu, Z.-Y.1    Blundell, T.L.2
  • 22
    • 0028999471 scopus 로고
    • Automatic recognition of hydrophobic clusters and their correlation with protein folding units
    • 2-s2.0-0028999471
    • Zehfus M. H., Automatic recognition of hydrophobic clusters and their correlation with protein folding units. Protein Science 1995 4 6 1188 1202 2-s2.0-0028999471
    • (1995) Protein Science , vol.4 , Issue.6 , pp. 1188-1202
    • Zehfus, M.H.1
  • 23
    • 3342888069 scopus 로고    scopus 로고
    • Empirical analysis of protein insertions and deletions determining parameters for the correct placement of gaps in protein sequence alignments
    • DOI 10.1016/j.jmb.2004.05.045, PII S0022283604006151
    • Chang M. S. S., Benner S. A., Empirical analysis of protein insertions and deletions determining parameters for the correct placement of gaps in protein sequence alignments. Journal of Molecular Biology 2004 341 2 617 631 2-s2.0-3342888069 10.1016/j.jmb.2004.05.045 (Pubitemid 38987792)
    • (2004) Journal of Molecular Biology , vol.341 , Issue.2 , pp. 617-631
    • Chang, M.S.S.1    Benner, S.A.2
  • 24
    • 0030931016 scopus 로고    scopus 로고
    • Mutation matrices and physical-chemical properties: Correlations and implications
    • DOI 10.1002/ (SICI)1097-0134(199703)27: 3<336: :AID-PROT2>3.0.CO;2- B
    • Koshi J. M., Goldstein R. A., Mutation matrices and physical- chemicalproperties: correlations and implications. Proteins 1997 27 3 336 344 (Pubitemid 27149286)
    • (1997) Proteins: Structure, Function and Genetics , vol.27 , Issue.3 , pp. 336-344
    • Koshi, J.M.1    Goldstein, R.A.2
  • 25
    • 0033533387 scopus 로고    scopus 로고
    • Core-directed protein design. II. Rescue of a multiply mutated and destabilized variant of ubiquitin
    • DOI 10.1021/bi990766f
    • Finucane M. D., Woolfson D. N., Core-directed protein design. II. rescue of a multiply mutated and destabilized variant of ubiquitin. Biochemistry 1999 38 36 11613 11623 2-s2.0-0033533387 10.1021/bi990766f (Pubitemid 29431916)
    • (1999) Biochemistry , vol.38 , Issue.36 , pp. 11613-11623
    • Finucane, M.D.1    Woolfson, D.N.2
  • 27
    • 0030690133 scopus 로고    scopus 로고
    • Deciphering protein sequence information through hydrophobic cluster analysis (HCA): Current status and perspectives
    • DOI 10.1007/s000180050082
    • Callebaut I., Labesse G., Durand P., Poupon A., Canard L., Chomilier J., Henrissat B., Mornon J. P., Deciphering protein sequence information through hydrophobic cluster analysis (HCA): current status and perspectives. Cellular and Molecular Life Sciences 1997 53 8 621 645 2-s2.0-0030690133 10.1007/s000180050082 (Pubitemid 27458280)
    • (1997) Cellular and Molecular Life Sciences , vol.53 , Issue.8 , pp. 621-645
    • Callebaut, I.1    Labesse, G.2    Durand, P.3    Poupon, A.4    Canard, L.5    Chomilier, J.6    Henrissat, B.7    Mornon, J.P.8
  • 28
    • 0023657949 scopus 로고
    • Hydrophobic cluster analysis: An efficient new way to compare and analyse amino acid sequences
    • 2-s2.0-0023657949
    • Gaboriaud C., Bissery V., Benchetrit T., Mornon J. P., Hydrophobic cluster analysis: an efficient new way to compare and analyse amino acid sequences. FEBS Letters 1987 224 1 149 155 2-s2.0-0023657949
    • (1987) FEBS Letters , vol.224 , Issue.1 , pp. 149-155
    • Gaboriaud, C.1    Bissery, V.2    Benchetrit, T.3    Mornon, J.P.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.