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Volumn 31, Issue 13, 2003, Pages 3345-3348

NCl: A server to identify non-canonical interactions in protein structures

Author keywords

[No Author keywords available]

Indexed keywords

PEPTIDE; PROTEIN; AMINO ACID;

EID: 0042622395     PISSN: 03051048     EISSN: None     Source Type: Journal    
DOI: 10.1093/nar/gkg528     Document Type: Article
Times cited : (81)

References (37)
  • 4
    • 0025663105 scopus 로고
    • Strength and co-operativity of contributions of surface salt bridges to protein stability
    • Horovitz,A., Serrano,L., Avron,B., Bycroft,M. and Fersht,A. (1990) Strength and co-operativity of contributions of surface salt bridges to protein stability. J. Mol. Biol., 216, 1031-1044.
    • (1990) J. Mol. Biol. , vol.216 , pp. 1031-1044
    • Horovitz, A.1    Serrano, L.2    Avron, B.3    Bycroft, M.4    Fersht, A.5
  • 5
    • 0030059689 scopus 로고    scopus 로고
    • Forces contributing to the conformational stability of proteins
    • Pace,C.N., Shirley,B.A., McNutt,M. and Gajiwala,K. (1996) Forces contributing to the conformational stability of proteins. FASEB J., 10, 75-83.
    • (1996) FASEB J. , vol.10 , pp. 75-83
    • Pace, C.N.1    Shirley, B.A.2    McNutt, M.3    Gajiwala, K.4
  • 6
    • 0025370815 scopus 로고
    • Dominant forces in protein folding
    • Dill,K.A. (1990) Dominant forces in protein folding. Biochemistry, 29, 7133-7155.
    • (1990) Biochemistry , vol.29 , pp. 7133-7155
    • Dill, K.A.1
  • 7
    • 0029002720 scopus 로고
    • The hydrophobic effect in protein folding
    • Lins,L. and Brasseur,R. (1995) The hydrophobic effect in protein folding. FASEB J., 9, 535-540.
    • (1995) FASEB J. , vol.9 , pp. 535-540
    • Lins, L.1    Brasseur, R.2
  • 8
    • 0001531477 scopus 로고
    • The effect of ortho substitution on the absorption of the OH group of phenol in the infrared
    • Wulf,O.R., Liddel,U. and Hendricks,S.B. (1936) The effect of ortho substitution on the absorption of the OH group of phenol in the infrared. J. Am. Chem. Soc., 58, 2287-2293.
    • (1936) J. Am. Chem. Soc. , vol.58 , pp. 2287-2293
    • Wulf, O.R.1    Liddel, U.2    Hendricks, S.B.3
  • 9
    • 37049046236 scopus 로고
    • Hydroxyl-benzene hydrogen bonding. An X-ray study
    • McPhail,A.T. and Sim,G.A. (1965) Hydroxyl-benzene hydrogen bonding. An X-ray study. Chem. Commun., 124-125.
    • (1965) Chem. Commun. , pp. 124-125
    • McPhail, A.T.1    Sim, G.A.2
  • 10
    • 36949064021 scopus 로고
    • The C-H⋯O hydrogen bonds in crystals
    • Sutor,D.J. (1962) The C-H⋯O hydrogen bonds in crystals. Nature, 195, 68-69.
    • (1962) Nature , vol.195 , pp. 68-69
    • Sutor, D.J.1
  • 13
    • 0037183788 scopus 로고    scopus 로고
    • A C-H⋯O hydrogen bond stabilized polypeptide chain reversal motif at the C terminus of helices in proteins
    • Madan Babu,M., Kumar Singh,S. and Balaram,P. (2002) A C-H⋯O hydrogen bond stabilized polypeptide chain reversal motif at the C terminus of helices in proteins. J. Mol. Biol., 322, 871-880.
    • (2002) J. Mol. Biol. , vol.322 , pp. 871-880
    • Madan Babu, M.1    Kumar Singh, S.2    Balaram, P.3
  • 14
    • 0032509022 scopus 로고    scopus 로고
    • C-H⋯O hydrogen bond involving proline residues in alpha-helices
    • Chakrabarti,P. and Chakrabarti,S. (1998) C-H⋯O hydrogen bond involving proline residues in alpha-helices. J. Mol. Biol., 284, 867-873.
    • (1998) J. Mol. Biol. , vol.284 , pp. 867-873
    • Chakrabarti, P.1    Chakrabarti, S.2
  • 15
    • 0035979146 scopus 로고    scopus 로고
    • The C-H⋯O hydrogen bond: A determinant of stability and specificity in transmembrane helix interactions
    • Senes,A., Ubarretxena-Belandia,I. and Engelman,D.M. (2001) The C-H⋯O hydrogen bond: a determinant of stability and specificity in transmembrane helix interactions. Proc. Natl Acad. Sci. USA, 98, 9056-9061.
    • (2001) Proc. Natl. Acad. Sci. USA , vol.98 , pp. 9056-9061
    • Senes, A.1    Ubarretxena-Belandia, I.2    Engelman, D.M.3
  • 16
    • 0030582683 scopus 로고    scopus 로고
    • Crystallographic evidence for C-H⋯O=C hydrogen bonds in a collagen triple helix
    • Bella,J. and Berman,H.M. (1996) Crystallographic evidence for C-H⋯O=C hydrogen bonds in a collagen triple helix. J. Mol. Biol., 264, 734-742.
    • (1996) J. Mol. Biol. , vol.264 , pp. 734-742
    • Bella, J.1    Berman, H.M.2
  • 17
    • 0033579558 scopus 로고    scopus 로고
    • C-H·O hydrogen bonds in minor groove of A-tracts in DNA double helices
    • Ghosh,A. and Bansal,M. (1999) C-H·O hydrogen bonds in minor groove of A-tracts in DNA double helices. J. Mol. Biol., 294, 1149-1158.
    • (1999) J. Mol. Biol. , vol.294 , pp. 1149-1158
    • Ghosh, A.1    Bansal, M.2
  • 18
    • 0033103478 scopus 로고    scopus 로고
    • Structure of acetylcholinesterase complexed with E2020: Implications for the design of new anti-alzheimer drugs
    • Kryger,G., Silman,I. and Sussman,J.L. (1999) Structure of acetylcholinesterase complexed with E2020: implications for the design of new anti-alzheimer drugs. Structure, 7, 297-307.
    • (1999) Structure , vol.7 , pp. 297-307
    • Kryger, G.1    Silman, I.2    Sussman, J.L.3
  • 21
    • 0027398886 scopus 로고
    • The (i, i + 4) Phe-His interaction studied in an alanine-based alpha-helix
    • Armstrong,K.M., Fairman,R. and Baldwin,R.L. (1993) The (i, i + 4) Phe-His interaction studied in an alanine-based alpha-helix. J. Mol. Biol., 230, 284-291.
    • (1993) J. Mol. Biol. , vol.230 , pp. 284-291
    • Armstrong, K.M.1    Fairman, R.2    Baldwin, R.L.3
  • 22
    • 0037019829 scopus 로고    scopus 로고
    • C-H⋯O hydrogen bonds at protein-protein interfaces
    • Jiang,L. and Lai,L. (2002) C-H⋯O hydrogen bonds at protein-protein interfaces. J. Biol. Chem., 277, 37732-37740.
    • (2002) J. Biol. Chem. , vol.277 , pp. 37732-37740
    • Jiang, L.1    Lai, L.2
  • 23
    • 0035971221 scopus 로고    scopus 로고
    • Strength of the C-H⋯O hydrogen bond of amino acid residues
    • Scheiner,S., Kar,T. and Gu,Y. (2001) Strength of the C-H⋯O hydrogen bond of amino acid residues. J. Biol. Chem., 276, 9832-9837.
    • (2001) J. Biol. Chem. , vol.276 , pp. 9832-9837
    • Scheiner, S.1    Kar, T.2    Gu, Y.3
  • 25
    • 0024292833 scopus 로고
    • Aromatic rings act as hydrogen bond acceptors
    • Levitt,M. and Perutz,M.F. (1988) Aromatic rings act as hydrogen bond acceptors. J. Mol. Biol., 201, 751-754.
    • (1988) J. Mol. Biol. , vol.201 , pp. 751-754
    • Levitt, M.1    Perutz, M.F.2
  • 26
    • 0000192455 scopus 로고    scopus 로고
    • An ab initio and data mining study on aromatic-amide interactions
    • Duan,G., Smith,V.H.Jr. and Weaver,D.F. (1999) An ab initio and data mining study on aromatic-amide interactions. Chem. Phys. Lett., 310, 323-332.
    • (1999) Chem. Phys. Lett. , vol.310 , pp. 323-332
    • Duan, G.1    Smith Jr., V.H.2    Weaver, D.F.3
  • 27
    • 0035910278 scopus 로고    scopus 로고
    • Hydrogen bonds with pi-acceptors in proteins: Frequencies and role in stabilizing local 3D structures
    • Steiner,T. and Koellner,G. (2001) Hydrogen bonds with pi-acceptors in proteins: frequencies and role in stabilizing local 3D structures. J. Mol. Biol., 305, 535-557.
    • (2001) J. Mol. Biol. , vol.305 , pp. 535-557
    • Steiner, T.1    Koellner, G.2
  • 28
    • 0028978764 scopus 로고
    • The occurrence of C-H⋯O hydrogen bonds in proteins
    • Derewenda,Z.S., Lee,L. and Derewenda,U. (1995) The occurrence of C-H⋯O hydrogen bonds in proteins. J. Mol. Biol., 252, 248-262.
    • (1995) J. Mol. Biol. , vol.252 , pp. 248-262
    • Derewenda, Z.S.1    Lee, L.2    Derewenda, U.3
  • 31
    • 0037487158 scopus 로고    scopus 로고
    • Significance of aromatic-backbone amide interactions in protein structure
    • Toth,G., Watts,C.R., Murphy,R.F. and Lovas,S. (2001) Significance of aromatic-backbone amide interactions in protein structure. Proteins, 43, 373-381.
    • (2001) Proteins , vol.43 , pp. 373-381
    • Toth, G.1    Watts, C.R.2    Murphy, R.F.3    Lovas, S.4
  • 36
    • 0033614004 scopus 로고    scopus 로고
    • Asparagine and glutamine: Using hydrogen atom contacts in the choice of sidechain amide orientation
    • Word,J.M., Lovell,S.C., Richardson,J.S. and Richardson,D.C. (1999) Asparagine and glutamine: using hydrogen atom contacts in the choice of sidechain amide orientation. J. Mol. Biol., 285, 1735-1747.
    • (1999) J. Mol. Biol. , vol.285 , pp. 1735-1747
    • Word, J.M.1    Lovell, S.C.2    Richardson, J.S.3    Richardson, D.C.4
  • 37
    • 0037314097 scopus 로고    scopus 로고
    • Matrix2png: A utility for visualizing matrix data
    • Pavlidis,P. and Noble,W.S. (2003) Matrix2png: a utility for visualizing matrix data. Bioinformatics, 19, 295-296.
    • (2003) Bioinformatics , vol.19 , pp. 295-296
    • Pavlidis, P.1    Noble, W.S.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.