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Volumn 14, Issue 2, 2010, Pages 106-128

Theoretical analysis of the contributions made by CH••OH bonds to protein structure

Author keywords

[No Author keywords available]

Indexed keywords

BIOCHEMISTRY; PHYSICAL CHEMISTRY;

EID: 77949667902     PISSN: 13852728     EISSN: None     Source Type: Journal    
DOI: 10.2174/138527210790069884     Document Type: Review
Times cited : (18)

References (122)
  • 3
    • 33947451575 scopus 로고
    • Two hydrogen-bonded spiral configurations of the polypeptide chain
    • Pauling, L.; Corey, R. B. Two hydrogen-bonded spiral configurations of the polypeptide chain. J. Am. Chem. Soc., 1950, 72, 5349-5349.
    • (1950) J. Am. Chem. Soc. , vol.72 , pp. 5349-15349
    • Pauling, L.1    Corey, R.B.2
  • 4
    • 76549252207 scopus 로고
    • The structure of proteins: Two hydrogen-bonded helical configurations of the polypeptide chain
    • Pauling, L.; Corey, R. B.; Branson, H. R. The structure of proteins: Two hydrogen-bonded helical configurations of the polypeptide chain. Proc. Natl. Acad. Sci., USA, 1951, 37, 205-211.
    • (1951) Proc. Natl. Acad. Sci., USA , vol.37 , pp. 205-211
    • Pauling, L.1    Corey, R.B.2    Branson, H.R.3
  • 5
    • 77949487333 scopus 로고    scopus 로고
    • Fundamental Features of Hydrogen Bonds
    • Maksic, Z. B., Orville-Thomas, W. J., Eds; Elsevier: Amsterdam
    • Scheiner, S. Fundamental Features of Hydrogen Bonds. In Pauling's Legacy - Modern Modelling of the Chemical Bond; Maksic, Z. B., Orville-Thomas, W. J., Eds.; Elsevier: Amsterdam, 1997; Vol. 6; pp. 571-591.
    • (1997) Pauling's Legacy Modern Modelling of the Chemical Bond , vol.6 , pp. 571-591
    • Scheiner, S.1
  • 6
    • 0000573263 scopus 로고
    • Configurations of polypeptide chains with favored orientations around single bonds: Two new pleated sheets
    • Pauling, L.; Corey, R. B. Configurations of polypeptide chains with favored orientations around single bonds: Two new pleated sheets. Proc. Natl. Acad. Sci., USA, 1951, 37, 729-740.
    • (1951) Proc. Natl. Acad. Sci., USA , vol.37 , pp. 729-740
    • Pauling, L.1    Corey, R.B.2
  • 7
    • 34548682845 scopus 로고
    • The acetylene-water complex A matrix isolation study
    • Engdahl, A.; Nelander, B. The acetylene-water complex. A matrix isolation study. Chem. Phys. Lett., 1983, 100, 129-132.
    • (1983) Chem. Phys. Lett. , vol.100 , pp. 129-132
    • Engdahl, A.1    Nelander, B.2
  • 8
    • 0001705673 scopus 로고
    • Water-hydrocarbon interactions: Rotational spectroscopy and structure of the water-acetylene complex
    • Peterson, K. I.; Klemperer, W. Water-hydrocarbon interactions: Rotational spectroscopy and structure of the water-acetylene complex. J. Chem. Phys., 1984, 81, 3842-3845.
    • (1984) J. Chem. Phys. , vol.81 , pp. 3842-3845
    • Peterson, K.I.1    Klemperer, W.2
  • 10
    • 36549093522 scopus 로고
    • Pulsed-nozzle Fourier-transform microwave spectroscopy of the methyl cyanide-acetylene dimer
    • Howard, N. W.; Legon, A. C. Pulsed-nozzle, Fourier-transform microwave spectroscopy of the methyl cyanide-acetylene dimer. J. Chem. Phys., 1986, 85, 6898-6904.
    • (1986) J. Chem. Phys. , vol.85 , pp. 6898-6904
    • Howard, N.W.1    Legon, A.C.2
  • 11
    • 0000527955 scopus 로고
    • Infrared matrix isolation study of hydrogen bonds involving C-H bonds: Alkynes with nitrogen bases
    • Jeng, M.-L. H.; DeLaat, A. M.; Ault, B. S. Infrared matrix isolation study of hydrogen bonds involving C-H bonds: Alkynes with nitrogen bases. J. Phys. Chem., 1989, 93, 3997-4000.
    • (1989) J. Phys. Chem. , vol.93 , pp. 3997-4000
    • Jeng, M.-L.1    DeLaat, A.M.2    Ault, B.S.3
  • 12
    • 0001859146 scopus 로고
    • ...acetylene complex
    • Legon, A. C. Nonlinear hydrogen bonds O...H-C and the role of secondary interactions. The rotational spectrum of the oxirane...acetylene complex. Chem. Phys. Lett., 1995, 247, 24-31.
    • (1995) Chem. Phys. Lett. , vol.247 , pp. 24-31
    • Legon, A.C.1
  • 13
    • 8144223487 scopus 로고    scopus 로고
    • A matrix isolation and ab initio study of the hydrogen bonded complexes of acetylene with pyridine
    • Sundararajan, K.; Sankaran, K.; Viswanathan, K. S. A matrix isolation and ab initio study of the hydrogen bonded complexes of acetylene with pyridine. J. Mol. Struct., 2005, 733, 187-192.
    • (2005) J. Mol. Struct. , vol.733 , pp. 187-192
    • Sundararajan, K.1    Sankaran, K.2    Viswanathan, K.S.3
  • 14
    • 0002361889 scopus 로고
    • Infrared absorption of the aldehydic C-H group
    • Pinchas, S. Infrared absorption of the aldehydic C-H group. Anal. Chem., 1955, 27, 2-6.
    • (1955) Anal. Chem. , vol.27 , pp. 2-6
    • Pinchas, S.1
  • 15
    • 0000516069 scopus 로고
    • Intramolecular hydrogen bonding in o-nitrobenzaldehyde and related compounds
    • Pinchas, S. Intramolecular hydrogen bonding in o-nitrobenzaldehyde and related compounds. J. Phys. Chem., 1963, 67, 1862-1865.
    • (1963) J. Phys. Chem. , vol.67 , pp. 1862-1865
    • Pinchas, S.1
  • 18
    • 0034318003 scopus 로고    scopus 로고
    • The structure of microsolvated benzene derivatives and the role of aromatic substituents
    • Brutschy, B. The structure of microsolvated benzene derivatives and the role of aromatic substituents. Chem. Rev., 2000, 100, 3891-3920.
    • (2000) Chem. Rev. , vol.100 , pp. 3891-3920
    • Brutschy, B.1
  • 21
    • 36849128641 scopus 로고
    • Proton magnetic resonance studies of chloroform in solution: Evidence for hydrogen bonding
    • Huggins, C. M.; Pimentel, G. C.; Shoolery, J. N. Proton magnetic resonance studies of chloroform in solution: Evidence for hydrogen bonding. J. Chem. Phys., 1955, 23, 1244-1247.
    • (1955) J. Chem. Phys. , vol.23 , pp. 1244-1247
    • Huggins, C.M.1    Pimentel, G.C.2    Shoolery, J.N.3
  • 22
    • 37049100198 scopus 로고
    • ···N complexes: Alcohol + ether and trichloromethane + amine systems
    • ···N complexes: Alcohol + ether and trichloromethane + amine systems. J. Chem. Soc., Faraday Trans. 2, 1976, 72, 693-699.
    • (1976) J. Chem. Soc., Faraday Trans. , vol.2 , Issue.72 , pp. 693-699
    • Hussein, M.A.1    Millen, D.J.2
  • 23
    • 0347136409 scopus 로고
    • Trihalogenomethane base complexes studied by vibrational spectroscopy in low-temperature matrices
    • Paulson, S. L.; Barnes, A. J. Trihalogenomethane - base complexes studied by vibrational spectroscopy in low-temperature matrices. J. Mol. Struct., 1982, 80, 151-158.
    • (1982) J. Mol. Struct. , vol.80 , pp. 151-158
    • Paulson, S.L.1    Barnes, A.J.2
  • 25
    • 85082728058 scopus 로고
    • Triformylmethane: an efficient preparation, some derivatives, and spectra
    • Budesinsky, M.; Fiedler, P.; Arnold, Z. Triformylmethane: an efficient preparation, some derivatives, and spectra. Synthesis, 1989, 858-860.
    • (1989) Synthesis , pp. 858-860
    • Budesinsky, M.1    Fiedler, P.2    Arnold, Z.3
  • 28
    • 33644752931 scopus 로고
    • The structure of fibrous proteins
    • Huggins, M. L. The structure of fibrous proteins. Chem. Rev., 1943, 32, 195-218.
    • (1943) Chem. Rev. , vol.32 , pp. 195-218
    • Huggins, M.L.1
  • 29
    • 0010738156 scopus 로고
    • ···O=C in proteins
    • ···O=C in proteins. Science, 1967, 158, 530-531.
    • (1967) Science , vol.158 , pp. 530-531
    • Krimm, S.1
  • 30
    • 0014381820 scopus 로고
    • Interchain hydrogen bonds via bound water molecules in the collagen triple helix
    • Ramachandran, G. N.; Chandrasekharan, R. Interchain hydrogen bonds via bound water molecules in the collagen triple helix. Biopolymers, 1968, 6, 1649-1658.
    • (1968) Biopolymers , vol.6 , pp. 1649-1658
    • Ramachandran, G.N.1    Chandrasekharan, R.2
  • 31
    • 33846209943 scopus 로고
    • A survey of hydrogen bond geometries in the crystal structures of amino acids
    • Jeffrey, G. A.; Maluszynska, H. A survey of hydrogen bond geometries in the crystal structures of amino acids. Int. J. Biol. Macromol., 1982, 4, 173-185.
    • (1982) Int. J. Biol. Macromol. , vol.4 , pp. 173-185
    • Jeffrey, G.A.1    Maluszynska, H.2
  • 32
    • 84977299028 scopus 로고
    • ···N interactions in determining molecular packing and conformation
    • ···N interactions in determining molecular packing and conformation. Acta Cryst., 1984, B40, 159-165.
    • (1984) Acta Cryst , vol.B40 , pp. 159-165
    • Berkovitch-Yellin, Z.1    Leiserowitz, L.2
  • 33
    • 0024588625 scopus 로고
    • Conformation and hydrogen bonding of N-formylmethionyl peptides II. Crystal and molecular structure of N-formyl-L-methionyl-L-phenylalanine
    • Parthasarathy, R.; Fridey, S. M.; Srikrishnan, T. Conformation and hydrogen bonding of N-formylmethionyl peptides. II. Crystal and molecular structure of N-formyl-L-methionyl-L-phenylalanine. Int. J. Peptide Protein Res., 1989, 33, 308-312.
    • (1989) Int. J. Peptide Protein Res. , vol.33 , pp. 308-312
    • Parthasarathy, R.1    Fridey, S.M.2    Srikrishnan, T.3
  • 34
    • 37849045152 scopus 로고    scopus 로고
    • Are aromatic carbon donor hydrogen bonds linear in proteins? Proteins Struct
    • Nanda, V.; Schmiedekamp, A. Are aromatic carbon donor hydrogen bonds linear in proteins? Proteins Struct. Func. Genetics, 2008, 70, 489-497.
    • (2008) Func. Genetics , vol.70 , pp. 489-497
    • Nanda, V.1    Schmiedekamp, A.2
  • 35
    • 0042667013 scopus 로고    scopus 로고
    • Stereospecific interactions of proline residues in protein structures and complexes
    • Bhattacharyya, R.; Charkabarti, P. Stereospecific interactions of proline residues in protein structures and complexes. J. Mol. Biol., 2003, 331, 925-940.
    • (2003) J. Mol. Biol. , vol.331 , pp. 925-940
    • Bhattacharyya, R.1    Charkabarti, P.2
  • 36
    • 0344667436 scopus 로고    scopus 로고
    • ···O hydrogen bond stabilized polypeptide chain reversal at the Cterminus of designed peptide helices. Structural characterization of three decapeptides
    • ···O hydrogen bond stabilized polypeptide chain reversal at the C-terminus of designed peptide helices. Structural characterization of three decapeptides. J. Am. Chem. Soc., 2003, 125, 15065-15075.
    • (2003) J. Am. Chem. Soc. , vol.125 , pp. 15065-15075
    • Aravinda, S.1    Shamala, N.2    Bandyopadhyay, A.3    Balaram, P.4
  • 37
    • 0141923130 scopus 로고    scopus 로고
    • C-H---O hydrogen bonds in β-sheetlike networks: Combined xray crystallography and high-pressure infrared study
    • Lee, K. M.; Chang, H.-C.; Jiang, J.-C.; Chen, J. C. C.; Kao, H.-E.; Lin, S. H.; Lin, I. J. B. C-H---O hydrogen bonds in β-sheetlike networks: Combined x-ray crystallography and high-pressure infrared study. J. Am. Chem. Soc., 2003, 125, 12358-12364.
    • (2003) J. Am. Chem. Soc. , vol.125 , pp. 12358-12364
    • Lee, K.M.1    Chang, H.-C.2    Jiang, J.-C.3    Chen, J.C.C.4    Kao, H.-E.5    Lin, S.H.6    Lin, I.J.B.7
  • 39
    • 0036296028 scopus 로고    scopus 로고
    • Twist and shear in β-sheets and β-ribbons
    • Ho, B. K.; Curmi, P. M. G. Twist and shear in β-sheets and β-ribbons. J. Mol. Biol., 2002, 317, 291-308.
    • (2002) J. Mol. Biol. , vol.317 , pp. 291-308
    • Ho, B.K.1    Curmi, P.M.G.2
  • 40
    • 0037019829 scopus 로고    scopus 로고
    • ···O hydrogen bonds at protein-protein interfaces
    • ···O hydrogen bonds at protein-protein interfaces. J. Biol. Chem., 2002, 277, 37732-37740.
    • (2002) J. Biol. Chem. , vol.277 , pp. 37732-37740
    • Jiang, L.1    Lai, L.2
  • 42
    • 4043082646 scopus 로고    scopus 로고
    • ···O hydrogen bonds in α-helices and helix termini in globular proteins
    • ···O hydrogen bonds in α-helices and helix termini in globular proteins. Proteins Struct. Func. Genetics, 2004, 56, 768-781.
    • (2004) Proteins Struct. Func. Genetics. , vol.56 , pp. 768-781
    • Manikandan, K.1    Ramakumar, S.2
  • 43
    • 58149265266 scopus 로고    scopus 로고
    • Geometrical preferences of the hydrogen bonds on protein-ligand binding interface derived from statistical surveys and quantum mechanics
    • Liu, Z.; Wang, G.; Li, Z.; Wang, R. Geometrical preferences of the hydrogen bonds on protein-ligand binding interface derived from statistical surveys and quantum mechanics. J. Chem. Theor. Comput., 2008, 4, 1959-1973.
    • (2008) J. Chem. Theor. Comput. , vol.4 , pp. 1959-1973
    • Liu, Z.1    Wang, G.2    Li, Z.3    Wang, R.4
  • 44
    • 0036711448 scopus 로고    scopus 로고
    • ··O hydrogen bonds in the nuclear receptor RAR# A potential tool for drug selectivity
    • ··O hydrogen bonds in the nuclear receptor RAR# - A potential tool for drug selectivity. Structure, 2002, 10, 1197-1204.
    • (2002) Structure , vol.10 , pp. 1197-1204
    • Klaholz, B.P.1    Moras, D.2
  • 45
    • 0346458811 scopus 로고    scopus 로고
    • ···O hydrogen bonds in protein-ligand complexes: Strong and weak interactions in molecular recognitions
    • ···O hydrogen bonds in protein-ligand complexes: Strong and weak interactions in molecular recognitions. Proteins, 2004, 54, 247-259.
    • (2004) Proteins , vol.54 , pp. 247-259
    • Sarkhel, S.1    Desiraju, G.R.2
  • 46
    • 33847366247 scopus 로고    scopus 로고
    • Strong and weak hydrogen bonds in the protein-ligand interface
    • Panigrahi, S. K.; Desiraju, G. R. Strong and weak hydrogen bonds in the protein-ligand interface. Proteins, 2007, 67, 128-141.
    • (2007) Proteins , vol.67 , pp. 128-141
    • Panigrahi, S.K.1    Desiraju, G.R.2
  • 48
    • 44049094995 scopus 로고    scopus 로고
    • Hydrogen-bonding and packing features of membrane proteins: Functional implications
    • Hildebrand, P. W.; Günther, S.; Goede, A.; Forrest, L.; Frömmel, C.; Preissner, R. Hydrogen-bonding and packing features of membrane proteins: Functional implications. Biophys. J., 2008, 94, 1945-1953.
    • (2008) Biophys. J. , vol.94 , pp. 1945-1953
    • Hildebrand, P.W.1    Günther, S.2    Goede, A.3    Forrest, L.4    Frömmel, C.5    Preissner, R.6
  • 49
    • 4143085058 scopus 로고    scopus 로고
    • Folding of helical membrane proteins: The role of polar GxxxG-like and proline motifs
    • Senes, A.; Engel, D. E.; DeGrado, W. F. Folding of helical membrane proteins: The role of polar, GxxxG-like and proline motifs. Curr. Opin. Struct. Biol., 2004, 14, 465-479.
    • (2004) Curr. Opin. Struct. Biol. , vol.14 , pp. 465-479
    • Senes, A.1    Engel, D.E.2    DeGrado, W.F.3
  • 50
    • 38949159124 scopus 로고    scopus 로고
    • middot;middot;middot;O=C hydrogen bonds in transmembrane protein
    • middot;middot;middot;O=C hydrogen bonds in transmembrane protein. J. Phys. Chem. B, 2008, 112, 1041-1048.
    • (2008) J. Phys. Chem. B , vol.112 , pp. 1041-1048
    • Park, H.1    Yoon, J.2    Seok, C.3
  • 51
    • 0037183788 scopus 로고    scopus 로고
    • middot;middot;middot;O hydrogen bond stabilized polypeptide chain reversal motif at the C terminus of helices in proteins
    • middot;middot;middot;O hydrogen bond stabilized polypeptide chain reversal motif at the C terminus of helices in proteins. J. Mol. Biol., 2002, 322, 871-880.
    • (2002) J. Mol. Biol. , vol.322 , pp. 871-880
    • Babu, M.M.1    Singh, S.K.2    Balaram, P.3
  • 53
    • 1842635588 scopus 로고    scopus 로고
    • The PDZ2 domain of syntenin at ultra-high resolution: Bridging the gap between macromolecular and small molecule crystallography
    • Kang, B. S.; Devedjiev, Y.; Derewenda, U.; Derewenda, Z. S. The PDZ2 domain of syntenin at ultra-high resolution: Bridging the gap between macromolecular and small molecule crystallography. J. Mol. Biol., 2004, 338, 483-493.
    • (2004) J. Mol. Biol. , vol.338 , pp. 483-493
    • Kang, B.S.1    Devedjiev, Y.2    Derewenda, U.3    Derewenda, Z.S.4
  • 57
    • 0037059067 scopus 로고    scopus 로고
    • ···O H-bonding between Phe and Glu side chains in α-helical peptides
    • ···O H-bonding between Phe and Glu side chains in α-helical peptides. Biophys. Chem., 2002, 101-102, 267-279.
    • (2002) Biophys. Chem. , vol.101-102 , pp. 267-279
    • Shi, Z.1    Olson, C.A.2    Bell, A.J.3    Kallenbach, N.R.4
  • 58
    • 85200277550 scopus 로고
    • Smith, D. A., Ed.; American Chemical Society: Washington, D.C
    • Modeling the Hydrogen Bond; Smith, D. A., Ed.; American Chemical Society: Washington, D.C., 1994; Vol. 569, pp. 300.
    • (1994) Modeling the Hydrogen Bond , vol.569 , pp. 300
  • 59
    • 0003840283 scopus 로고    scopus 로고
    • A Theoretical Perspective; Oxford University Press: New York
    • Scheiner, S. Hydrogen Bonding. A Theoretical Perspective; Oxford University Press: New York, 1997.
    • (1997) Hydrogen Bonding
    • Scheiner, S.1
  • 60
    • 33749516863 scopus 로고    scopus 로고
    • Grabowski, S. J., Ed.; Springer: Dordrecht
    • Hydrogen Bonding - New Insights; Grabowski, S. J., Ed.; Springer: Dordrecht, 2006.
    • (2006) Hydrogen Bonding New Insights
  • 62
    • 0034317323 scopus 로고    scopus 로고
    • Blue-shifting hydrogen bonds
    • Hobza, P.; Havlas, Z. Blue-shifting hydrogen bonds. Chem. Rev., 2000, 100, 4253-4264.
    • (2000) Chem. Rev. , vol.100 , pp. 4253-4264
    • Hobza, P.1    Havlas, Z.2
  • 63
    • 0000718312 scopus 로고    scopus 로고
    • ···O Hydrogen Bonding
    • Hargittai, M., Hargittai, I., Eds.; JAI Press: Stamford, CT
    • ···O Hydrogen Bonding. In Advances in Molecular Structure Research; Hargittai, M., Hargittai, I., Eds.; JAI Press: Stamford, CT, 2000; Vol. 6; pp. 159-207.
    • (2000) Advances in Molecular Structure Research , vol.6 , pp. 159-207
    • Scheiner, S.1
  • 64
    • 0034697472 scopus 로고    scopus 로고
    • Weak hydrogen bonds: Theoretical studies
    • Calhorda, M. J. Weak hydrogen bonds: Theoretical studies. Chem. Commun., 2000, 801-809.
    • (2000) Chem. Commun. , pp. 801-809
    • Calhorda, M.J.1
  • 65
    • 85134276642 scopus 로고    scopus 로고
    • The CH--O Hydrogen Bond. A Historical Account
    • Dykstra, C. E., Frenking, G., Kim, K. S., Scuseria, G. E., Eds.; Elsevier: Amsterdam
    • Scheiner, S. The CH--O Hydrogen Bond. A Historical Account. In Theory and Applications of Computational Chemistry: The First 40 Years; Dykstra, C. E., Frenking, G., Kim, K. S., Scuseria, G. E., Eds.; Elsevier: Amsterdam, 2005; pp. 831-857.
    • (2005) Theory and Applications of Computational Chemistry: The First 40 Years , pp. 831-857
    • Scheiner, S.1
  • 66
    • 84890205395 scopus 로고    scopus 로고
    • ··X Hydrogen Bonds to Biomolecular Structure
    • Grabowski, S. J., Ed.; Springer
    • ··X Hydrogen Bonds to Biomolecular Structure. In Hydrogen Bonding - New Insights; Grabowski, S. J., Ed.; Springer, 2006; pp. 263-292.
    • (2006) Hydrogen Bonding New Insights , pp. 263-292
    • Scheiner, S.1
  • 67
    • 44049087258 scopus 로고    scopus 로고
    • Anion-arene adducts: C-H hydrogen bonding, anion-Π interaction, and carbon bonding motifs
    • Hay, B. P.; Bryantsev, V. S. Anion-arene adducts: C-H hydrogen bonding, anion-Π interaction, and carbon bonding motifs. Chem. Commun., 2008, 2417-2428.
    • (2008) Chem. Commun. , pp. 2417-2428
    • Hay, B.P.1    Bryantsev, V.S.2
  • 68
    • 55349091366 scopus 로고    scopus 로고
    • Carbon-donated hydrogen bonding. Electrostatics, frequency shifts, directionality, and bifurcation
    • Compaan, K.; Vergenz, R.; Schleyer, P. V. R.; Arreguin, I. Carbon-donated hydrogen bonding. Electrostatics, frequency shifts, directionality, and bifurcation. Int. J. Quantum Chem., 2008, 108, 2914-2923.
    • (2008) Int. J. Quantum Chem. , vol.108 , pp. 2914-2923
    • Compaan, K.1    Vergenz, R.2    Schleyer, P.V.R.3    Arreguin, I.4
  • 69
    • 33751251674 scopus 로고    scopus 로고
    • An ab initio benchmark study of hydrogen bonded formamide dimers
    • Frey, J. A.; Leutwyler, S. An ab initio benchmark study of hydrogen bonded formamide dimers. J. Phys. Chem. A, 2006, 110, 12512-12518.
    • (2006) J. Phys. Chem. A , vol.110 , pp. 12512-12518
    • Frey, J.A.1    Leutwyler, S.2
  • 70
    • 28844501708 scopus 로고    scopus 로고
    • Liquid NMA: A surprisingly realistic model for hydrogen bonding motifs in proteins
    • Whitfield, T. W.; Martyna, G. J.; Allison, S.; Bates, S. P.; Crain, J. Liquid NMA: A surprisingly realistic model for hydrogen bonding motifs in proteins. Chem. Phys. Lett., 2005, 414, 210-214.
    • (2005) Chem. Phys. Lett. , vol.414 , pp. 210-214
    • Whitfield, T.W.1    Martyna, G.J.2    Allison, S.3    Bates, S.P.4    Crain, J.5
  • 71
    • 4344640628 scopus 로고    scopus 로고
    • Density functional theory study of the hydrogen-bonding interaction of 1:1 complexes of alanine with water
    • Zhang, H.; Zhou, Z.; Shi, Y. Density functional theory study of the hydrogen-bonding interaction of 1:1 complexes of alanine with water. J. Phys. Chem. A, 2004, 108, 6735-6743.
    • (2004) J. Phys. Chem. A , vol.108 , pp. 6735-6743
    • Zhang, H.1    Zhou, Z.2    Shi, Y.3
  • 72
    • 33645818759 scopus 로고    scopus 로고
    • Coexistence of dihydrogen, blueand red-shifting hydrogen bonds in an ultrasmall system: Valine
    • Yu, W.; Lin, Z.; Huang, Z. Coexistence of dihydrogen, blueand red-shifting hydrogen bonds in an ultrasmall system: Valine. ChemPhysChem., 2006, 7, 828-830.
    • (2006) ChemPhysChem , vol.7 , pp. 828-830
    • Yu, W.1    Lin, Z.2    Huang, Z.3
  • 73
    • 0035971221 scopus 로고    scopus 로고
    • ··O hydrogen bond of amino acid residues
    • ··O hydrogen bond of amino acid residues. J. Biol. Chem., 2001, 276, 9832-9837.
    • (2001) J. Biol. Chem. , vol.276 , pp. 9832-9837
    • Scheiner, S.1    Kar, T.2    Gu, Y.3
  • 74
    • 84961977359 scopus 로고    scopus 로고
    • Conformational studies into N-methylation of alanine diamide models: A quantitative approach
    • Siodlak, D.; Gajewska, M.; Macedowska, A.; Rzeszotarska, B. Conformational studies into N-methylation of alanine diamide models: A quantitative approach. J. Mol. Struct. [Theochem], 2006, 775, 47-59.
    • (2006) J. Mol. Struct. [Theochem] , vol.775 , pp. 47-59
    • Siodlak, D.1    Gajewska, M.2    Macedowska, A.3    Rzeszotarska, B.4
  • 75
    • 5544301524 scopus 로고    scopus 로고
    • Solvation effects on alanine dipeptide: A MP2/ccpVTZ//MP2/6-31Gstudy of [Φ,Ψ] energy maps and conformers in the gas phase, ether, and water
    • Wang, Z.-X.; Duan, Y. Solvation effects on alanine dipeptide: A MP2/cc-pVTZ//MP2/6-31Gstudy of [Φ,Ψ] energy maps and conformers in the gas phase, ether, and water. J. Comput. Chem., 2004, 25, 1699-1716.
    • (2004) J. Comput. Chem. , vol.25 , pp. 1699-1716
    • Wang, Z.-X.1    Duan, Y.2
  • 76
    • 67650034436 scopus 로고    scopus 로고
    • Amide I bands of terminally blocked alanine in solutions investigated by infrared spectroscopy and density functional theory calculation: Hydrogen-bonding interactions and solvent effects
    • Lee, M.-E.; Lee, S. Y.; Joo, S.-W.; Chu, K.-H. Amide I bands of terminally blocked alanine in solutions investigated by infrared spectroscopy and density functional theory calculation: Hydrogen-bonding interactions and solvent effects. J. Phys. Chem. B, 2009, 113, 6894-6897.
    • (2009) J. Phys. Chem. B , vol.113 , pp. 6894-6897
    • Lee, M.-E.1    Lee, S.Y.2    Joo, S.-W.3    Chu, K.-H.4
  • 77
    • 34248634865 scopus 로고    scopus 로고
    • QTAIM study of the closed-shell interactions in peptide secondary structures: A cluster treatment of oligoand polyalanines
    • Vener, M. V.; Egorova, A. N.; Fomin, D. P.; Tsirelson, V. G. QTAIM study of the closed-shell interactions in peptide secondary structures: A cluster treatment of oligo-and polyalanines. Chem. Phys. Lett., 2007, 440, 279-285.
    • (2007) Chem. Phys. Lett. , vol.440 , pp. 279-285
    • Vener, M.V.1    Egorova, A.N.2    Fomin, D.P.3    Tsirelson, V.G.4
  • 78
    • 34548438089 scopus 로고    scopus 로고
    • A density functional theory study of the hydrogen bond interactions in glycine dimers
    • Carvalho, M. F. d.; Mosquera, R. A.; Rivelino, R. A density functional theory study of the hydrogen bond interactions in glycine dimers. Chem. Phys. Lett., 2007, 445, 117-124.
    • (2007) Chem. Phys. Lett. , vol.445 , pp. 117-124
    • Carvalho, M.F.D.1    Mosquera, R.A.2    Rivelino, R.3
  • 79
    • 36048964831 scopus 로고    scopus 로고
    • Accurate ab initio study on the hydrogen-bond pairs in protein secondary structures
    • Wang, Z.-X.; Wu, C.; Lei, H.; Duan, Y. Accurate ab initio study on the hydrogen-bond pairs in protein secondary structures. J. Chem. Theor. Comput., 2007, 3, 1527 - 1537.
    • (2007) J. Chem. Theor. Comput. , vol.3 , pp. 1527-1537
    • Wang, Z.-X.1    Wu, C.2    Lei, H.3    Duan, Y.4
  • 80
    • 9944222091 scopus 로고    scopus 로고
    • ···O=C hydrogen bonds involving proline residues in helices
    • ···O=C hydrogen bonds involving proline residues in helices. J. Phys. Chem. B, 2004, 108, 18065-18072.
    • (2004) J. Phys. Chem. B , vol.108 , pp. 18065-18072
    • Guo, H.1    Beahm, R.F.2    Guo, H.3
  • 81
    • 34548280871 scopus 로고    scopus 로고
    • Bader's electron density analysis of hydrogen bonding in secondary structural elements of proteins
    • Parthasarathi, R.; Raman, S. S.; Subramanian, V.; Ramasami, T. Bader's electron density analysis of hydrogen bonding in secondary structural elements of proteins. J. Phys. Chem. A, 2007, 111, 7141-7148.
    • (2007) J. Phys. Chem. A , vol.111 , pp. 7141-7148
    • Parthasarathi, R.1    Raman, S.S.2    Subramanian, V.3    Ramasami, T.4
  • 82
    • 33749682240 scopus 로고    scopus 로고
    • ··O and CḦO H-bonds to the stability of β-sheets in proteins
    • ··O and CH··O H-bonds to the stability of β-sheets in proteins. J. Phys. Chem. B, 2006, 110, 18670-18679.
    • (2006) J. Phys. Chem. B , vol.110 , pp. 18670-18679
    • Scheiner, S.1
  • 83
    • 84961978617 scopus 로고    scopus 로고
    • ··O hydrogen bonds between polypeptide chain segments
    • ··O hydrogen bonds between polypeptide chain segments. J. Phys. Chem. B, 2005, 109, 16132-16141.
    • (2005) J. Phys. Chem. B , vol.109 , pp. 16132-16141
    • Scheiner, S.1
  • 85
    • 35148868285 scopus 로고    scopus 로고
    • The strength with which a peptide group can form a hydrogen bond varies with the internal conformation of the polypeptide chain
    • Scheiner, S. The strength with which a peptide group can form a hydrogen bond varies with the internal conformation of the polypeptide chain. J. Phys. Chem. B, 2007, 111, 11312-11317.
    • (2007) J. Phys. Chem. B , vol.111 , pp. 11312-11317
    • Scheiner, S.1
  • 86
    • 63849298906 scopus 로고    scopus 로고
    • Remarkable blue shifts of C-H and N-H stretching frequencies in the interaction of monosubstituted formaldehyde and thioformaldehyde with nitrosyl hydride
    • Trung, N. T.; Hue, T. T.; Nguyen, M. T. Remarkable blue shifts of C-H and N-H stretching frequencies in the interaction of monosubstituted formalde-hyde and thioformaldehyde with nitrosyl hydride. J. Phys. Chem. A, 2009, 113, 3245-3253.
    • (2009) J. Phys. Chem. A , vol.113 , pp. 3245-3253
    • Trung, N.T.1    Hue, T.T.2    Nguyen, M.T.3
  • 87
    • 61449177030 scopus 로고    scopus 로고
    • ···π interactions for benzene dimer: How to amend MP2 calculations to reproduce the experimental results
    • ···π interactions for benzene dimer: How to amend MP2 calculations to reproduce the experimental results. J. Chem. Phys., 2009, 130, 081101.
    • (2009) J. Chem. Phys. , vol.130 , pp. 081101
    • Dinadayalane, T.C.1    Leszczynski, J.2
  • 90
    • 44449160482 scopus 로고    scopus 로고
    • Blue shifts of the C-H stretching vibrations in hydrogen-bonded and protonated trimethylamine Effect of hyperconjugation on bond properties
    • Chandra, A. K.; Parveen, S.; Das, S.; Zeegers-Huyskens, T. Blue shifts of the C-H stretching vibrations in hydrogen-bonded and protonated trimethy-lamine. Effect of hyperconjugation on bond properties. J. Comput. Chem., 2008, 29, 1490-1496.
    • (2008) J. Comput. Chem. , vol.29 , pp. 1490-1496
    • Chandra, A.K.1    Parveen, S.2    Das, S.3    Zeegers-Huyskens, T.4
  • 92
    • 34548559273 scopus 로고    scopus 로고
    • Blue-shifted A-H stretching modes and cooperative hydrogen bonding 1. Complexes of substituted formaldehyde with cyclic hydrogen fluoride and water clusters
    • Karpfen, A.; Kryachko, E. S. Blue-shifted A-H stretching modes and cooperative hydrogen bonding. 1. Complexes of substituted formaldehyde with cyclic hydrogen fluoride and water clusters. J. Phys. Chem. A, 2007, 111, 8177-8187.
    • (2007) J. Phys. Chem. A , vol.111 , pp. 8177-8187
    • Karpfen, A.1    Kryachko, E.S.2
  • 93
    • 33749504880 scopus 로고    scopus 로고
    • Theoretical force-field model for blue-shifted hydrogen bonds with fluoromethanes
    • Kryachko, E. S.; Karpfen, A. Theoretical force-field model for blue-shifted hydrogen bonds with fluoromethanes. Chem. Phys., 2006, 329, 313-328.
    • (2006) Chem. Phys. , vol.329 , pp. 313-328
    • Kryachko, E.S.1    Karpfen, A.2
  • 95
    • 34247355541 scopus 로고    scopus 로고
    • Chemical origin of blueand redshifted hydrogen bonds: Intramolecular hyperconjugation and its coupling with intermolecular hyperconjugation
    • Li, A. Y. Chemical origin of blue-and redshifted hydrogen bonds: Intramolecular hyperconjugation and its coupling with intermolecular hyperconjugation. J. Chem. Phys., 2007, 126, 154102.
    • (2007) J. Chem. Phys. , vol.126 , pp. 154102
    • Li, A.Y.1
  • 96
    • 34247533707 scopus 로고    scopus 로고
    • Red-, blue-, or no-shift hydrogen bonds: A unified explanation
    • Joseph, J.; Jemmis, E. D. Red-, blue-, or no-shift hydrogen bonds: A unified explanation. J. Am. Chem. Soc., 2007, 129, 4620-4632.
    • (2007) J. Am. Chem. Soc. , vol.129 , pp. 4620-4632
    • Joseph, J.1    Jemmis, E.D.2
  • 98
    • 27944462143 scopus 로고    scopus 로고
    • ...HNC complexes [Rg=He, Ne, Ar Kr]
    • ···HNC complexes [Rg=He, Ne, Ar, Kr]. Mol. Phys., 2005, 103, 2763-2768.
    • (2005) Mol. Phys. , vol.103 , pp. 2763-2768
    • McDowell, S.A.C.1
  • 99
    • 22444431944 scopus 로고    scopus 로고
    • Ab initio studies of electron acceptor-donor interactions with blueand red-shifted hydrogen bonds
    • Rodziewicz, P.; Rutkowski, K. S.; Melikova, S. M.; Koll, A. Ab initio studies of electron acceptor-donor interactions with blueand red-shifted hydrogen bonds. ChemPhysChem, 2005, 6, 1282-1292.
    • (2005) ChemPhysChem , vol.6 , pp. 1282-1292
    • Rodziewicz, P.1    Rutkowski, K.S.2    Melikova, S.M.3    Koll, A.4
  • 101
    • 17744368503 scopus 로고    scopus 로고
    • On differences between hydrogen bonding and improper blue-shifting hydrogen bonding
    • Zierkiewicz, W.; Jurecka, P.; Hobza, P. On differences between hydrogen bonding and improper blue-shifting hydrogen bonding. ChemPhysChem, 2005, 6, 609-617.
    • (2005) ChemPhysChem , vol.6 , pp. 609-617
    • Zierkiewicz, W.1    Jurecka, P.2    Hobza, P.3
  • 103
    • 3242888424 scopus 로고    scopus 로고
    • Blue-shifting or redshifting hydrogen bonding? Predictions for haloform complexes with dimethyl ether on the basis of perturbation
    • Herrebout, W. A.; Delanoye, S. N.; Veken, B. J. V. D. Blue-shifting or redshifting hydrogen bonding? Predictions for haloform complexes with dimethyl ether on the basis of perturbation. J. Phys. Chem. A, 2004, 108, 6059-6064.
    • (2004) J. Phys. Chem. A , vol.108 , pp. 6059-6064
    • Herrebout, W.A.1    Delanoye, S.N.2    Veken, B.J.V.D.3
  • 105
    • 2342448514 scopus 로고    scopus 로고
    • Study of proper and improper hydrogen bonding using Bader's atoms in molecules [AIM] theory and NBO analysis
    • Kolandaivel, P.; Nirmala, V. Study of proper and improper hydrogen bonding using Bader's atoms in molecules [AIM] theory and NBO analysis. J. Mol. Struct., 2004, 694, 33-38.
    • (2004) J. Mol. Struct. , vol.694 , pp. 33-38
    • Kolandaivel, P.1    Nirmala, V.2
  • 107
    • 33846462065 scopus 로고    scopus 로고
    • On the origin of red and blue shifts of X-H and C-H stretching vibrations in formic acid [formate ion] and proton donor complexes
    • Parreira, R. L. T.; Galembeck, S. E.; Hobza, P. On the origin of red and blue shifts of X-H and C-H stretching vibrations in formic acid [formate ion] and proton donor complexes. ChemPhysChem, 2007, 8, 87-92.
    • (2007) ChemPhysChem , vol.8 , pp. 87-92
    • Parreira, R.L.T.1    Galembeck, S.E.2    Hobza, P.3
  • 108
    • 57149129443 scopus 로고    scopus 로고
    • Spectroscopic and structural signature of the CH--O Hbond
    • Scheiner, S.; Kar, T. Spectroscopic and structural signature of the CH--O H-bond. J. Phys. Chem. A, 2008, 112, 11854-11860.
    • (2008) J. Phys. Chem. A , vol.112 , pp. 11854-11860
    • Scheiner, S.1    Kar, T.2
  • 110
    • 34547274725 scopus 로고    scopus 로고
    • α stretch mode in peptides 1. Isolated alanine peptide structures
    • α stretch mode in peptides. 1. Isolated alanine peptide structures. J. Phys. Chem. A, 2007, 111, 5300-5303.
    • (2007) J. Phys. Chem. A , vol.111 , pp. 5300-5303
    • Mirkin, N.G.1    Krimm, S.2
  • 112
    • 65249154887 scopus 로고    scopus 로고
    • α-D stretch vibration in deuterated peptides
    • α-D stretch vibration in deuterated peptides. J. Phys. Chem. B, 2009, 113, 1813-1816.
    • (2009) J. Phys. Chem. B , vol.113 , pp. 1813-1816
    • Wang, J.1
  • 113
    • 14844357750 scopus 로고    scopus 로고
    • ··O hydrogen bonds with implications for protein folding
    • ··O hydrogen bonds with implications for protein folding. J. Phys. Chem. B, 2005, 109, 3681-3689.
    • (2005) J. Phys. Chem. B , vol.109 , pp. 3681-3689
    • Scheiner, S.1    Kar, T.2
  • 114
    • 0343791148 scopus 로고
    • Electric moments of molecules in liquids
    • Onsager, L. Electric moments of molecules in liquids. J. Am. Chem. Soc., 1936, 58, 1486-1493.
    • (1936) J. Am. Chem. Soc. , vol.58 , pp. 1486-1493
    • Onsager, L.1
  • 115
    • 0347377133 scopus 로고
    • Hartree-Fock second derivatives and electric field properties in a solvent reaction field: Theory and application
    • Wong, M. W.; Wiberg, K. B.; Frisch, M. Hartree-Fock second derivatives and electric field properties in a solvent reaction field: Theory and application. J. Chem. Phys., 1991, 95, 8991-8998.
    • (1991) J. Chem. Phys. , vol.95 , pp. 8991-8998
    • Wong, M.W.1    Wiberg, K.B.2    Frisch, M.3
  • 116
    • 84961979198 scopus 로고    scopus 로고
    • Continuum solvation models: A new approach to the problem of solute's charge distribution and cavity boundaries
    • Mennucci, B.; Tomasi, J. Continuum solvation models: A new approach to the problem of solute's charge distribution and cavity boundaries. J. Chem. Phys., 1997, 106, 5151-5198.
    • (1997) J. Chem. Phys. , vol.106 , pp. 5151-5198
    • Mennucci, B.1    Tomasi, J.2
  • 117
    • 0031209054 scopus 로고    scopus 로고
    • A new integral equation formalism for the polarizable continuum model: Theoretical background and applications to isotropic and anisotropic dielectrics
    • Cancès, E.; Menucci, B.; Tomasi, J. A new integral equation formalism for the polarizable continuum model: Theoretical background and applications to isotropic and anisotropic dielectrics. J. Chem. Phys., 1997, 107, 3032-3041.
    • (1997) J. Chem. Phys. , vol.107 , pp. 3032-3041
    • Cancès, E.1    Menucci, B.2    Tomasi, J.3
  • 118
    • 0032502372 scopus 로고    scopus 로고
    • Ab initio study of ionic solutions by a polarizable continuum dielectric model
    • Cossi, M.; Barone, V.; Mennucci, B.; Tomasi, J. Ab initio study of ionic solutions by a polarizable continuum dielectric model. Chem. Phys. Lett., 1998, 286, 253-260.
    • (1998) Chem. Phys. Lett. , vol.286 , pp. 253-260
    • Cossi, M.1    Barone, V.2    Mennucci, B.3    Tomasi, J.4
  • 119
    • 84961985847 scopus 로고    scopus 로고
    • Quantum calculation of molecular energies and energy gradients in solution by a conductor solvent model
    • Barone, V.; Cossi, M. Quantum calculation of molecular energies and energy gradients in solution by a conductor solvent model. J. Phys. Chem. A, 1998, 102, 1995-2001.
    • (1998) J. Phys. Chem. A , vol.102 , pp. 1995-2001
    • Barone, V.1    Cossi, M.2
  • 120
    • 1542356431 scopus 로고    scopus 로고
    • Solvent effects. 5. Influence of cavity shape, truncation of electrostatics, and electron correlation on ab initio reaction field calculations
    • Foresman, J. B.; Keith, T. A.; Wiberg, K. B.; Snoonian, J.; Frisch, M. J. Solvent effects. 5. Influence of cavity shape, truncation of electrostatics, and electron correlation on ab initio reaction field calculations. J. Phys. Chem., 1996, 100, 16098-16104.
    • (1996) J. Phys. Chem. , vol.100 , pp. 16098-16104
    • Foresman, J.B.1    Keith, T.A.2    Wiberg, K.B.3    Snoonian, J.4    Frisch, M.J.5
  • 121
    • 33644943244 scopus 로고    scopus 로고
    • Cooperativity of conventional and unconventional hydrogen bonds involving imidazole
    • Kar, T.; Scheiner, S. Cooperativity of conventional and unconventional hydrogen bonds involving imidazole. Int. J. Quantum Chem., 2006, 106, 843-851.
    • (2006) Int. J. Quantum Chem. , vol.106 , pp. 843-851
    • Kar, T.1    Scheiner, S.2
  • 122
    • 7544224411 scopus 로고    scopus 로고
    • ··O and OH··O hydrogen bonds
    • ··O and OH··O hydrogen bonds. J. Phys. Chem. A, 2004, 108, 9161-9168.
    • (2004) J. Phys. Chem. A , vol.108 , pp. 9161-9168
    • Kar, T.1    Scheiner, S.2


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