메뉴 건너뛰기




Volumn 37, Issue 3, 2003, Pages 440-445

A Comparative Analysis of Interhelical Polar Interactions of Various α-Helix Packings in Proteins

Author keywords

Hydrogen bond; Packing of helices; Salt bridge

Indexed keywords

GLOBULAR PROTEIN; HYDROGEN; LEUCINE ZIPPER PROTEIN;

EID: 0038124516     PISSN: 00268933     EISSN: None     Source Type: Journal    
DOI: 10.1023/A:1024299629832     Document Type: Article
Times cited : (2)

References (25)
  • 1
    • 0000920828 scopus 로고
    • The packing of α-helices: Simple coiled-coils
    • Crick F.H.C. 1953. The packing of α-helices: simple coiled-coils. Acta Crystallogr. 6, 689-697.
    • (1953) Acta Crystallogr. , vol.6 , pp. 689-697
    • Crick, F.H.C.1
  • 2
    • 0343063933 scopus 로고
    • Structure of proteins: Packing of α-helices and pleated sheets
    • Chothia C., Levitt M., Richardson D. 1977. Structure of proteins: packing of α-helices and pleated sheets. Proc. Natl. Acad. Sci. USA. 74, 4130-4134.
    • (1977) Proc. Natl. Acad. Sci. USA , vol.74 , pp. 4130-4134
    • Chothia, C.1    Levitt, M.2    Richardson, D.3
  • 4
    • 0017876485 scopus 로고
    • Packing of α-helices: Geometrical constraints and contact areas
    • Richmond T.J., Richards F.M. 1978. Packing of α-helices: geometrical constraints and contact areas. J. Mol. Biol. 119, 537-555.
    • (1978) J. Mol. Biol. , vol.119 , pp. 537-555
    • Richmond, T.J.1    Richards, F.M.2
  • 5
    • 0024279564 scopus 로고
    • General architecture of the α-helical globule
    • Murzin A.G., Finkelstein A.V. 1988. General architecture of the α-helical globule. J. Mol. Biol. 204, 749-769.
    • (1988) J. Mol. Biol. , vol.204 , pp. 749-769
    • Murzin, A.G.1    Finkelstein, A.V.2
  • 6
    • 0029867179 scopus 로고    scopus 로고
    • Principles of helix-helix packing in proteins: The helical lattice super-position model
    • Walther D., Eisenhaber F., Argos P. 1996. Principles of helix-helix packing in proteins: the helical lattice super-position model. J. Mol. Biol. 255, 536-553.
    • (1996) J. Mol. Biol. , vol.255 , pp. 536-553
    • Walther, D.1    Eisenhaber, F.2    Argos, P.3
  • 7
    • 0017780710 scopus 로고
    • Stereochemistry of packing of α-helices and of the β-structure in a compact globule
    • Efimov A. V. 1977. Stereochemistry of packing of α-helices and of the β-structure in a compact globule. Dokl. Akad. Nauk SSSR. 235, 699-702.
    • (1977) Dokl. Akad. Nauk SSSR , vol.235 , pp. 699-702
    • Efimov, A.V.1
  • 8
    • 0018792414 scopus 로고
    • Packing of α-helices in globular proteins. Layer-structure of globin hydrophobic cores
    • Efimov A. V. 1979. Packing of α-helices in globular proteins. Layer-structure of globin hydrophobic cores. J. Mol. Biol. 134, 23-40.
    • (1979) J. Mol. Biol. , vol.134 , pp. 23-40
    • Efimov, A.V.1
  • 9
    • 0020111370 scopus 로고
    • On the role of connections in the formation of protein structures containing four helices
    • Efimov A. V. 1982. On the role of connections in the formation of protein structures containing four helices. Mol. Biol. 16, 271-281.
    • (1982) Mol.Biol. , vol.16 , pp. 271-281
    • Efimov, A.V.1
  • 10
    • 0030271515 scopus 로고    scopus 로고
    • Coiled coils: New structures and new functions
    • Lupas A. 1996. Coiled coils: new structures and new functions. Trends Biochem. Sci. 21, 375-382.
    • (1996) Trends Biochem. Sci. , vol.21 , pp. 375-382
    • Lupas, A.1
  • 11
    • 0033429687 scopus 로고    scopus 로고
    • Complementary packing of α-helices in proteins
    • Efimov A.V. 1999. Complementary packing of α-helices in proteins. FEBS Lett. 463, 3-6.
    • (1999) FEBS Lett. , vol.463 , pp. 3-6
    • Efimov, A.V.1
  • 12
    • 0025974401 scopus 로고
    • Structure of α-α-hairpins with short connections
    • Efimov A.V. 1991. Structure of α-α-hairpins with short connections. Protein Engineering. 4, 245-250.
    • (1991) Protein Engineering , vol.4 , pp. 245-250
    • Efimov, A.V.1
  • 13
    • 0027428284 scopus 로고
    • Standard structures in proteins
    • Efimov A.V. 1993. Standard structures in proteins. Progr. Biophys. Mol. Biol. 60, 201-239.
    • (1993) Progr. Biophys. Mol. Biol. , vol.60 , pp. 201-239
    • Efimov, A.V.1
  • 14
    • 16944366990 scopus 로고    scopus 로고
    • Buried polar residues and structural specificity in the GCN4 leucine zipper
    • Gonzáles L., Jr., Woolfson D.N., Alber T. 1996. Buried polar residues and structural specificity in the GCN4 leucine zipper. Nature Struct. Biol. 3, 1011-1018.
    • (1996) Nature Struct. Biol. , vol.3 , pp. 1011-1018
    • Gonzáles Jr., L.1    Woolfson, D.N.2    Alber, T.3
  • 15
    • 0032497322 scopus 로고    scopus 로고
    • A buried polar interaction can direct the relative orientation of helices in a coiled coil
    • Oakley M.G., Kim P.S. 1998. A buried polar interaction can direct the relative orientation of helices in a coiled coil. Biochemistry. 37, 12603-12610.
    • (1998) Biochemistry , vol.37 , pp. 12603-12610
    • Oakley, M.G.1    Kim, P.S.2
  • 16
    • 0029008590 scopus 로고
    • A buried polar interaction imparts structural uniqueness in a designed heterodimeric coiled coil
    • Lumb K.J., Kim P.S. 1995. A buried polar interaction imparts structural uniqueness in a designed heterodimeric coiled coil. Biochemistry. 34, 8642-8648.
    • (1995) Biochemistry , vol.34 , pp. 8642-8648
    • Lumb, K.J.1    Kim, P.S.2
  • 17
    • 0032720311 scopus 로고    scopus 로고
    • The role of position a in determining the stability and oligomerization state of α-helical coiled coils: 20 Amino acid stability coefficients in the hydrophobic core of proteins
    • Wagschal K., Tripet B., Lavigne P., Mant C., Hodges R.S. 1999. The role of position a in determining the stability and oligomerization state of α-helical coiled coils: 20 amino acid stability coefficients in the hydrophobic core of proteins. Protein Sci. 8, 2312-2329.
    • (1999) Protein Sci. , vol.8 , pp. 2312-2329
    • Wagschal, K.1    Tripet, B.2    Lavigne, P.3    Mant, C.4    Hodges, R.S.5
  • 18
    • 0034616959 scopus 로고    scopus 로고
    • 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"
    • Tripet B., Wagschal K., Lavigne P., Mant C., Hodges R.S. 2000. 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". J. Mol. Biol. 300, 377-402.
    • (2000) J. Mol. Biol. , vol.300 , pp. 377-402
    • Tripet, B.1    Wagschal, K.2    Lavigne, P.3    Mant, C.4    Hodges, R.S.5
  • 19
    • 0028303384 scopus 로고
    • A thermodynamic scale for leucine zipper stability and dimerization specificity: e and g interhelical interactions
    • Krylov D., Mikhailenko I., Vinson C. 1994. A thermodynamic scale for leucine zipper stability and dimerization specificity: e and g interhelical interactions. EMBO J. 13, 2849-2861.
    • (1994) EMBO J. , vol.13 , pp. 2849-2861
    • Krylov, D.1    Mikhailenko, I.2    Vinson, C.3
  • 20
    • 0032514952 scopus 로고    scopus 로고
    • Orientation, positional, additivity, and oligomerization-state effects of interhelical ion pairs in α-helical coiled-coils
    • Kohn W.D., Kay C.M., Hodges R.S. 1998. Orientation, positional, additivity, and oligomerization-state effects of interhelical ion pairs in α-helical coiled-coils. J. Mol. Biol. 283, 993-1012.
    • (1998) J. Mol. Biol. , vol.283 , pp. 993-1012
    • Kohn, W.D.1    Kay, C.M.2    Hodges, R.S.3
  • 21
    • 0036110130 scopus 로고    scopus 로고
    • A systematic analysis of buried polar side chains and their interactions in α-helical proteins
    • Kondratova M.S., Efimov A.V. 2002. A systematic analysis of buried polar side chains and their interactions in α-helical proteins. Mol.Biol. 36, 144-151.
    • (2002) Mol.Biol. , vol.36 , pp. 144-151
    • Kondratova, M.S.1    Efimov, A.V.2
  • 22
    • 0028961335 scopus 로고
    • SCOP: A structural classification of proteins database for the investigation of sequences and structures
    • Murzin A.G., Brenner S.E., Hubbard T., Chothia C. 1995. SCOP: a structural classification of proteins database for the investigation of sequences and structures. J. Mol. Biol. 247, 536-540.
    • (1995) J. Mol. Biol. , vol.247 , pp. 536-540
    • Murzin, A.G.1    Brenner, S.E.2    Hubbard, T.3    Chothia, C.4
  • 23
    • 0030442990 scopus 로고    scopus 로고
    • Positioning hydrogen atoms by optimizing hydrogen-bond networks in protein structures
    • Hooft R.W.W., Sander C., Vriend G. 1996. Positioning hydrogen atoms by optimizing hydrogen-bond networks in protein structures. Proteins. 26, 363-376.
    • (1996) Proteins , vol.26 , pp. 363-376
    • Hooft, R.W.W.1    Sander, C.2    Vriend, G.3
  • 24
    • 0029154811 scopus 로고
    • Native-like and structurally characterized designed α-helical bundles
    • Betz S.F., Bryson J.W., De Grado W.F. 1995. Native-like and structurally characterized designed α-helical bundles. Curr. Opin. Struct. Biol. 5, 457-463.
    • (1995) Curr. Opin. Struct. Biol. , vol.5 , pp. 457-463
    • Betz, S.F.1    Bryson, J.W.2    De Grado, W.F.3
  • 25
    • 0029083811 scopus 로고
    • Predicting oligomerization states of coiled coils
    • Woolfson D.N., Alber T. 1995. Predicting oligomerization states of coiled coils. Protein Sci. 4, 1596-1607.
    • (1995) Protein Sci. , vol.4 , pp. 1596-1607
    • Woolfson, D.N.1    Alber, T.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.