메뉴 건너뛰기




Volumn 285, Issue 4, 1999, Pages 1735-1747

Asparagine and glutamine: Using hydrogen atom contacts in the choice of side-chain amide orientation

Author keywords

Asn Gln flips; Hydrogen atom placement; Hydrogen bond network; Side chain amide orientation; Small probe contact dots

Indexed keywords

AMIDE; ASPARAGINE; GLUTAMINE; HISTIDINE; HYDROGEN; METHIONINE;

EID: 0033614004     PISSN: 00222836     EISSN: None     Source Type: Journal    
DOI: 10.1006/jmbi.1998.2401     Document Type: Article
Times cited : (1233)

References (28)
  • 1
    • 0030584665 scopus 로고    scopus 로고
    • The crystal structure of endoglucanase CelA, a family 8 glycosyl hydrolase from Clostridium thermocellum
    • Alzari P. M., Souchon H., Dominguez R. The crystal structure of endoglucanase CelA, a family 8 glycosyl hydrolase from Clostridium thermocellum. Structure. 4:1996;265-275.
    • (1996) Structure , vol.4 , pp. 265-275
    • Alzari, P.M.1    Souchon, H.2    Dominguez, R.3
  • 2
    • 36849097253 scopus 로고
    • Molecular charge distributions and chemical bonding. II. First-row diatomic hydrides, AH
    • Bader R. F. W., Keaveny I., Cade P. E. Molecular charge distributions and chemical bonding. II. First-row diatomic hydrides, AH. J. Chem. Phys. 47:1967;3381-3402.
    • (1967) J. Chem. Phys. , vol.47 , pp. 3381-3402
    • Bader, R.F.W.1    Keaveny, I.2    Cade, P.E.3
  • 3
    • 0026520305 scopus 로고
    • A method for determining the positions of polar hydrogens added to a protein structure that maximizes protein hydrogen bonding
    • Bass M. B., Hopkins D. F., Jaquysh W. A. N., Ornstein R. L. A method for determining the positions of polar hydrogens added to a protein structure that maximizes protein hydrogen bonding. Proteins: Struct. Funct. Genet. 12:1992;266-277.
    • (1992) Proteins: Struct. Funct. Genet. , vol.12 , pp. 266-277
    • Bass, M.B.1    Hopkins, D.F.2    Jaquysh, W.A.N.3    Ornstein, R.L.4
  • 4
    • 0002775934 scopus 로고
    • Interaction models for water in relation to protein hydration
    • B. Pullman. D. Reidel Publishing Company, Boston
    • Berendsen H. J. C., Postma J. P. M., van Gunsteren W. F., Hermans J. Interaction models for water in relation to protein hydration. Pullman B. Intermolecular Forces. 1981;331-342 D. Reidel Publishing Company, Boston.
    • (1981) Intermolecular Forces , pp. 331-342
    • Berendsen, H.J.C.1    Postma, J.P.M.2    Van Gunsteren, W.F.3    Hermans, J.4
  • 6
    • 0023643147 scopus 로고
    • The high-resolution X-ray crystal structure of the complex formed between subtilisin Carlsberg and eglin c, an elastase inhibitor from the leech, Hirudo medicinalis
    • Bode W., Papamokos E., Musil D. The high-resolution X-ray crystal structure of the complex formed between subtilisin Carlsberg and eglin c, an elastase inhibitor from the leech, Hirudo medicinalis. Eur. J. Biochem. 166:1987;673-692.
    • (1987) Eur. J. Biochem. , vol.166 , pp. 673-692
    • Bode, W.1    Papamokos, E.2    Musil, D.3
  • 8
    • 0021107965 scopus 로고
    • Solvent-accessible surfaces of proteins and nucleic acids
    • Connolly M. L. Solvent-accessible surfaces of proteins and nucleic acids. Science. 221:1983;709-713.
    • (1983) Science , vol.221 , pp. 709-713
    • Connolly, M.L.1
  • 9
    • 0028978764 scopus 로고
    • The occurrence of C-H ··· O hydrogen bonds in proteins
    • Derewenda Z. S., Lee L., Derewenda U. The occurrence of C-H ··· O hydrogen bonds in proteins. J. Mol. Biol. 252:1995;248-262.
    • (1995) J. Mol. Biol. , vol.252 , pp. 248-262
    • Derewenda, Z.S.1    Lee, L.2    Derewenda, U.3
  • 10
    • 0016804680 scopus 로고
    • The molecular structure of a dimer composed of the variable portions of the Bence-Jones protein REI refined at 2.0-Å resolution
    • Epp O., Lattman E. E., Schiffer M., Huber R., Palm W. The molecular structure of a dimer composed of the variable portions of the Bence-Jones protein REI refined at 2.0-Å resolution. Biochemistry. 14:1975;4943-4952.
    • (1975) Biochemistry , vol.14 , pp. 4943-4952
    • Epp, O.1    Lattman, E.E.2    Schiffer, M.3    Huber, R.4    Palm, W.5
  • 11
    • 0029664970 scopus 로고    scopus 로고
    • The 1.5-Å resolution crystal structure of bacterial luciferase in low salt conditions
    • Fisher A. J., Thompson T. B., Thoden J. B., Baldwin T. O., Rayment I. The 1.5-Å resolution crystal structure of bacterial luciferase in low salt conditions. J. Biol. Chem. 271:1996;21956-21968.
    • (1996) J. Biol. Chem. , vol.271 , pp. 21956-21968
    • Fisher, A.J.1    Thompson, T.B.2    Thoden, J.B.3    Baldwin, T.O.4    Rayment, I.5
  • 13
    • 0016399124 scopus 로고
    • Energy functions for peptides and proteins. I. Derivation of a consistent force field including the hydrogen bond from amide crystals
    • Hagler A. T., Huler E., Lifson S. Energy functions for peptides and proteins. I. Derivation of a consistent force field including the hydrogen bond from amide crystals. J. Am. Chem. Soc. 96:1974;5319-5327.
    • (1974) J. Am. Chem. Soc. , vol.96 , pp. 5319-5327
    • Hagler, A.T.1    Huler, E.2    Lifson, S.3
  • 14
    • 0030442990 scopus 로고    scopus 로고
    • Positioning hydrogen atoms by optimizing hydrogen-bond networks in protein structures
    • Hooft R. W. W., Sander C., Vriend G. Positioning hydrogen atoms by optimizing hydrogen-bond networks in protein structures. Proteins: Struct. Funct. Genet. 26:1996;363-376.
    • (1996) Proteins: Struct. Funct. Genet. , vol.26 , pp. 363-376
    • Hooft, R.W.W.1    Sander, C.2    Vriend, G.3
  • 15
    • 0028233375 scopus 로고
    • Crystal structure of toxin II from the scorpion Androctonus australis Hector refined at 1.3 Å resolution
    • Housset D., Habersetzer-Rochat C., Astier J.-P., Fontecilla-Camps J. C. Crystal structure of toxin II from the scorpion Androctonus australis Hector refined at 1.3 Å resolution. J. Mol. Biol. 239:1994;88-103.
    • (1994) J. Mol. Biol. , vol.239 , pp. 88-103
    • Housset, D.1    Habersetzer-Rochat, C.2    Astier, J.-P.3    Fontecilla-Camps, J.C.4
  • 16
    • 84889120137 scopus 로고
    • Improved methods for building protein models in electron density maps and the location of errors in these models
    • Jones T. A., Zou J.-Y., Cowan S. W., Kjeldgaard M. Improved methods for building protein models in electron density maps and the location of errors in these models. Acta Crystallog. sect. A. 47:1991;110-119.
    • (1991) Acta Crystallog. Sect. a , vol.47 , pp. 110-119
    • Jones, T.A.1    Zou, J.-Y.2    Cowan, S.W.3    Kjeldgaard, M.4
  • 17
    • 0020004138 scopus 로고
    • 551from Pseudomonas aeruginosa refined at 1.6 Å resolution and comparison of the two redox forms
    • 551from Pseudomonas aeruginosa refined at 1.6 Å resolution and comparison of the two redox forms. J. Mol. Biol. 156:1982;389-409.
    • (1982) J. Mol. Biol. , vol.156 , pp. 389-409
    • Matsuura, Y.1    Takano, T.2    Dickerson, R.E.3
  • 18
    • 0029017638 scopus 로고
    • The application of hydrogen bonding analysis in X-ray crystallography to help orientate asparagine, glutamine and histidine side chains
    • McDonald I. K., Thornton J. M. The application of hydrogen bonding analysis in X-ray crystallography to help orientate asparagine, glutamine and histidine side chains. Protein Eng. 8:1994;217-224.
    • (1994) Protein Eng. , vol.8 , pp. 217-224
    • McDonald, I.K.1    Thornton, J.M.2
  • 20
    • 0027049243 scopus 로고
    • The kinemage: A tool for scientific illustration
    • Richardson D. C., Richardson J. S. The kinemage: a tool for scientific illustration. Protein Sci. 1:1992;3-9.
    • (1992) Protein Sci. , vol.1 , pp. 3-9
    • Richardson, D.C.1    Richardson, J.S.2
  • 21
    • 0028288709 scopus 로고
    • Kinemages: Simple macromolecular graphics for interactive teaching and publication
    • Richardson D. C., Richardson J. S. Kinemages: simple macromolecular graphics for interactive teaching and publication. Trends Biochem. Sci. 19:1994;135-138.
    • (1994) Trends Biochem. Sci. , vol.19 , pp. 135-138
    • Richardson, D.C.1    Richardson, J.S.2
  • 22
    • 0029061966 scopus 로고
    • The Escherichia coli malonyl-CoA:acyl carrier protein transacylase at 1.5-Å resolution
    • Serre L., Verbree E. C., Dauter Z., Stuitje A. R., Derewenda Z. S. The Escherichia coli malonyl-CoA:acyl carrier protein transacylase at 1.5-Å resolution. J. Biol. Chem. 270:1995;12961-12964.
    • (1995) J. Biol. Chem. , vol.270 , pp. 12961-12964
    • Serre, L.1    Verbree, E.C.2    Dauter, Z.3    Stuitje, A.R.4    Derewenda, Z.S.5
  • 25
    • 0029646113 scopus 로고
    • The crystal structures of the oligopeptide-binding protein OppA complexed with tripeptide and tetrapeptide ligands
    • Tame J. R. H., Dodson E. J., Murshudov G., Higgins C. F., Wilkinson A. J. The crystal structures of the oligopeptide-binding protein OppA complexed with tripeptide and tetrapeptide ligands. Structure. 3:1995;1395-1406.
    • (1995) Structure , vol.3 , pp. 1395-1406
    • Tame, J.R.H.1    Dodson, E.J.2    Murshudov, G.3    Higgins, C.F.4    Wilkinson, A.J.5


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.