메뉴 건너뛰기




Volumn 138, Issue 3, 2008, Pages 115-119

Solvent-free crystallizations of amino acids: The effects of the hydrophilicity/hydrophobicity of side-chains

Author keywords

Amino acids; Crystallization; Hydrophilicity hydrophobicity; Polymorphism; Solvent free; Sublimation

Indexed keywords

ALANINE; AMINO ACID DERIVATIVE; ISOLEUCINE; LEUCINE; METHIONINE; PHENYLALANINE; PROLINE; SOLVENT; THREONINE; TRYPTOPHAN; TYROSINE; VALINE;

EID: 55549117101     PISSN: 03014622     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.bpc.2008.09.011     Document Type: Article
Times cited : (15)

References (37)
  • 1
    • 84897765658 scopus 로고    scopus 로고
    • Crystalline amino acids - a link between chemistry, materials science and biology
    • Boeyens J.C.A., and Ogilvie J.F. (Eds)
    • Boldyreva E. Crystalline amino acids - a link between chemistry, materials science and biology. In: Boeyens J.C.A., and Ogilvie J.F. (Eds). Models, Mysteries and Magic of Molecules (2008)
    • (2008) Models, Mysteries and Magic of Molecules
    • Boldyreva, E.1
  • 2
    • 0005401737 scopus 로고
    • Optical second-harmonic generation in crystalline amino acids
    • Rieckhoff K.E., and Peticolas W.L. Optical second-harmonic generation in crystalline amino acids. Science 147 (1965) 610-611
    • (1965) Science , vol.147 , pp. 610-611
    • Rieckhoff, K.E.1    Peticolas, W.L.2
  • 3
    • 0036499568 scopus 로고    scopus 로고
    • Growth of nonlinear optical gamma-glycine crystals
    • Bhat M.N., and Dharmaprakash S.M. Growth of nonlinear optical gamma-glycine crystals. J. Cryst. Growth 236 (2002) 376-380
    • (2002) J. Cryst. Growth , vol.236 , pp. 376-380
    • Bhat, M.N.1    Dharmaprakash, S.M.2
  • 4
    • 27844520861 scopus 로고    scopus 로고
    • Pyroelectric properties of some compounds based on protein amino acids
    • Yarmarkin V.K., Shulman S.G., Pankova G.A., and Lemanov V.V. Pyroelectric properties of some compounds based on protein amino acids. Phys. Solid State 47 (2005) 2135-2137
    • (2005) Phys. Solid State , vol.47 , pp. 2135-2137
    • Yarmarkin, V.K.1    Shulman, S.G.2    Pankova, G.A.3    Lemanov, V.V.4
  • 5
    • 41449100252 scopus 로고    scopus 로고
    • Amino acid network and its scoring application in protein-protein docking
    • Chang S., Jiao X., Li C., Gong X., Chen W., and Wang C. Amino acid network and its scoring application in protein-protein docking. Biophys. Chem. 134 (2008) 111-118
    • (2008) Biophys. Chem. , vol.134 , pp. 111-118
    • Chang, S.1    Jiao, X.2    Li, C.3    Gong, X.4    Chen, W.5    Wang, C.6
  • 6
    • 0018525374 scopus 로고
    • Hydrogen-bonds in crystal-structures of amino-acids, peptides and related molecules
    • Vinogradov S.N. Hydrogen-bonds in crystal-structures of amino-acids, peptides and related molecules. Int. J. Pept. Protein Res. 14 (1979) 281-289
    • (1979) Int. J. Pept. Protein Res. , vol.14 , pp. 281-289
    • Vinogradov, S.N.1
  • 7
    • 0000809197 scopus 로고
    • Hydrogen-bond distances and angles in the structures of amino acids and peptides
    • Görbitz C.H. Hydrogen-bond distances and angles in the structures of amino acids and peptides. Acta Crystallogr. B45 (1989) 390-395
    • (1989) Acta Crystallogr. , vol.B45 , pp. 390-395
    • Görbitz, C.H.1
  • 8
    • 0032539604 scopus 로고    scopus 로고
    • The pressure dependence of hydrophobic interactions is consistent with the observed pressure denaturation of proteins
    • Hummer G., Garde S., Garcia A.E., Paulaitis M.E., and Pratt L.R. The pressure dependence of hydrophobic interactions is consistent with the observed pressure denaturation of proteins. Proc. Natl. Acad. Sci. U. S. A. 95 (1998) 1552-1555
    • (1998) Proc. Natl. Acad. Sci. U. S. A. , vol.95 , pp. 1552-1555
    • Hummer, G.1    Garde, S.2    Garcia, A.E.3    Paulaitis, M.E.4    Pratt, L.R.5
  • 9
    • 2342517463 scopus 로고    scopus 로고
    • Crystal structures of hydrophobic amino acids: interaction energies of hydrogen-bonded layers revealed by ab initio calculations
    • Dalhus B., and Gorbitz C.H. Crystal structures of hydrophobic amino acids: interaction energies of hydrogen-bonded layers revealed by ab initio calculations. J. Mol. Struct., Theochem 675 (2004) 47-52
    • (2004) J. Mol. Struct., Theochem , vol.675 , pp. 47-52
    • Dalhus, B.1    Gorbitz, C.H.2
  • 12
    • 33745360913 scopus 로고    scopus 로고
    • Unique crystal morphologies of glycine grown from octanoic acid-in-water emulsions
    • Nicholson C.E., Cooper S.J., and Jamieson M.J. Unique crystal morphologies of glycine grown from octanoic acid-in-water emulsions. J. Am. Chem. Soc. 128 (2006) 7718-7719
    • (2006) J. Am. Chem. Soc. , vol.128 , pp. 7718-7719
    • Nicholson, C.E.1    Cooper, S.J.2    Jamieson, M.J.3
  • 13
    • 33745685955 scopus 로고    scopus 로고
    • Abundant polymorphism in a system with multiple hydrogen-bonding opportunities: oxalyl dihydrazide
    • Ahn S.Y., Guo F., Kariuki B.M., and Harris K.D.M. Abundant polymorphism in a system with multiple hydrogen-bonding opportunities: oxalyl dihydrazide. J. Am. Chem. Soc. 128 (2006) 8441-8452
    • (2006) J. Am. Chem. Soc. , vol.128 , pp. 8441-8452
    • Ahn, S.Y.1    Guo, F.2    Kariuki, B.M.3    Harris, K.D.M.4
  • 14
    • 33947462481 scopus 로고
    • On the sublimation of amino acids and peptides
    • Gross D., and Grodsky G. On the sublimation of amino acids and peptides. J. Am. Chem. Soc. 77 (1955) 1678-1680
    • (1955) J. Am. Chem. Soc. , vol.77 , pp. 1678-1680
    • Gross, D.1    Grodsky, G.2
  • 15
    • 0001754796 scopus 로고
    • Structure and conformation of orthorhombic l-cysteine
    • Kerr K.A., and Ashmore J.P. Structure and conformation of orthorhombic l-cysteine. Acta Crystallogr. B29 (1973) 2124-2127
    • (1973) Acta Crystallogr. , vol.B29 , pp. 2124-2127
    • Kerr, K.A.1    Ashmore, J.P.2
  • 16
    • 0030195852 scopus 로고    scopus 로고
    • l-cysteine, monoclinic form, redetermination at 120 K
    • Gorbitz C.H., and Dalhus B. l-cysteine, monoclinic form, redetermination at 120 K. Acta Crystallogr. C52 (1996) 1756-1759
    • (1996) Acta Crystallogr. , vol.C52 , pp. 1756-1759
    • Gorbitz, C.H.1    Dalhus, B.2
  • 17
    • 35848956318 scopus 로고    scopus 로고
    • Crystallization of metastable beta glycine from gas phase via the sublimation of alpha or gamma form in vacuum
    • Liu Z., Zhong L., Ying P., Feng Z., and Li C. Crystallization of metastable beta glycine from gas phase via the sublimation of alpha or gamma form in vacuum. Biophys. Chem. 132 (2008) 18-22
    • (2008) Biophys. Chem. , vol.132 , pp. 18-22
    • Liu, Z.1    Zhong, L.2    Ying, P.3    Feng, Z.4    Li, C.5
  • 18
    • 0014677262 scopus 로고
    • On the unit-cell dimensions and space group of l-tyrosine and l-tryptophane
    • Khawas B., and Krishna Murti G.S.R. On the unit-cell dimensions and space group of l-tyrosine and l-tryptophane. Acta Crystallogr. B25 (1969) 1006-1009
    • (1969) Acta Crystallogr. , vol.B25 , pp. 1006-1009
    • Khawas, B.1    Krishna Murti, G.S.R.2
  • 19
    • 37049075067 scopus 로고
    • Analysis of organic polymorphs - a review
    • Threlfall T.L. Analysis of organic polymorphs - a review. Analyst 120 (1995) 2435-2460
    • (1995) Analyst , vol.120 , pp. 2435-2460
    • Threlfall, T.L.1
  • 22
    • 0034740079 scopus 로고    scopus 로고
    • Neutron scattering, infra red, Raman spectroscopy and ab initio study of l-threonine
    • Pawlukojc A., Leciejewicz J., Tomkinson J., and Parker S.F. Neutron scattering, infra red, Raman spectroscopy and ab initio study of l-threonine. Spectrochim. Acta A57 (2001) 2513-2523
    • (2001) Spectrochim. Acta , vol.A57 , pp. 2513-2523
    • Pawlukojc, A.1    Leciejewicz, J.2    Tomkinson, J.3    Parker, S.F.4
  • 23
    • 0001244187 scopus 로고    scopus 로고
    • Infrared spectral, structural, and conformational studies of zwitterionic l-tryptophan
    • Cao X.L., and Fischer G. Infrared spectral, structural, and conformational studies of zwitterionic l-tryptophan. J. Phys. Chem., A 103 (1999) 9995-10003
    • (1999) J. Phys. Chem., A , vol.103 , pp. 9995-10003
    • Cao, X.L.1    Fischer, G.2
  • 24
    • 0242569648 scopus 로고    scopus 로고
    • Low-temperature Fourier transform infrared spectra and hydrogen bonding in polycrystalline l-alanine
    • Rozenberg M., Shoham G., Reva I., and Fausto R. Low-temperature Fourier transform infrared spectra and hydrogen bonding in polycrystalline l-alanine. Spectrochim. Acta A59 (2003) 3253-3266
    • (2003) Spectrochim. Acta , vol.A59 , pp. 3253-3266
    • Rozenberg, M.1    Shoham, G.2    Reva, I.3    Fausto, R.4
  • 25
    • 0037265678 scopus 로고    scopus 로고
    • Crystallization in polymorphic systems: the solution-mediated transformation beta to alpha glycine
    • Ferrari E.S., Davey R.J., Cross W.I., Gillon A.L., and Towler C.S. Crystallization in polymorphic systems: the solution-mediated transformation beta to alpha glycine. Cryst. Growth Des. 3 (2003) 53-60
    • (2003) Cryst. Growth Des. , vol.3 , pp. 53-60
    • Ferrari, E.S.1    Davey, R.J.2    Cross, W.I.3    Gillon, A.L.4    Towler, C.S.5
  • 26
    • 84900041761 scopus 로고    scopus 로고
    • Is polymorphism caused by molecular conformation changes?
    • Boeyens J.C.A., and Ogilvie J.F. (Eds)
    • Bernal I. Is polymorphism caused by molecular conformation changes?. In: Boeyens J.C.A., and Ogilvie J.F. (Eds). Models, Mysteries, and Magic of Molecules (2008)
    • (2008) Models, Mysteries, and Magic of Molecules
    • Bernal, I.1
  • 27
    • 20744450085 scopus 로고    scopus 로고
    • A correlation between the proton stretching vibration red shift and the hydrogen bond length in polycrystalline amino acids and peptides
    • Rozenberg M., Shoham G., Reva I., and Fausto R. A correlation between the proton stretching vibration red shift and the hydrogen bond length in polycrystalline amino acids and peptides. Phys. Chem. Chem. Phys. 7 (2005) 2376-2383
    • (2005) Phys. Chem. Chem. Phys. , vol.7 , pp. 2376-2383
    • Rozenberg, M.1    Shoham, G.2    Reva, I.3    Fausto, R.4
  • 28
    • 27944436074 scopus 로고    scopus 로고
    • Polymorphism and molecular conformations of non-protonated alpha-amino acids
    • Mukhopadhyay U., and Bernal I. Polymorphism and molecular conformations of non-protonated alpha-amino acids. Mendeleev Commun. 14 (2004) 270-276
    • (2004) Mendeleev Commun. , vol.14 , pp. 270-276
    • Mukhopadhyay, U.1    Bernal, I.2
  • 29
    • 24344447148 scopus 로고
    • Preliminary examination of the crystal structure of l-proline
    • Wright B.A., and Cole P.A. Preliminary examination of the crystal structure of l-proline. Acta Crystallogr. 2 (1949) 129-130
    • (1949) Acta Crystallogr. , vol.2 , pp. 129-130
    • Wright, B.A.1    Cole, P.A.2
  • 30
    • 0000206534 scopus 로고    scopus 로고
    • Crystal structures of hydrophobic amino acids. 1. redeterminations of l-methionine and l-valine at 120 K
    • Dalhus B., and Gorbitz C.H. Crystal structures of hydrophobic amino acids. 1. redeterminations of l-methionine and l-valine at 120 K. Acta Chem. Scand. 50 (1996) 544-548
    • (1996) Acta Chem. Scand. , vol.50 , pp. 544-548
    • Dalhus, B.1    Gorbitz, C.H.2
  • 31
    • 0037438461 scopus 로고    scopus 로고
    • The basis of the hydrophobic effect
    • Kyte J. The basis of the hydrophobic effect. Biophys. Chem. 100 (2003) 193-203
    • (2003) Biophys. Chem. , vol.100 , pp. 193-203
    • Kyte, J.1
  • 32
    • 4644236471 scopus 로고    scopus 로고
    • Hydrophobic collapse in multidomain protein folding
    • Zhou R.H., Huang X.H., Margulis C.J., and Berne B.J. Hydrophobic collapse in multidomain protein folding. Science 305 (2004) 1605-1609
    • (2004) Science , vol.305 , pp. 1605-1609
    • Zhou, R.H.1    Huang, X.H.2    Margulis, C.J.3    Berne, B.J.4
  • 33
    • 34547516861 scopus 로고    scopus 로고
    • Hydrophobic association of alpha-helices, steric dewetting, and enthalpic barriers to protein folding
    • MacCallum J.L., Moghaddam M.S., Chan H.S., and Tieleman D.P. Hydrophobic association of alpha-helices, steric dewetting, and enthalpic barriers to protein folding. Proc. Natl. Acad. Sci. U. S. A. 104 (2007) 6206-6210
    • (2007) Proc. Natl. Acad. Sci. U. S. A. , vol.104 , pp. 6206-6210
    • MacCallum, J.L.1    Moghaddam, M.S.2    Chan, H.S.3    Tieleman, D.P.4
  • 34
    • 22144475817 scopus 로고    scopus 로고
    • New polymorphs of ROY and new record for coexisting polymorphs of solved structures
    • Chen S., Guzei I.A., and Yu L. New polymorphs of ROY and new record for coexisting polymorphs of solved structures. J. Am. Chem. Soc. 127 (2005) 9881-9885
    • (2005) J. Am. Chem. Soc. , vol.127 , pp. 9881-9885
    • Chen, S.1    Guzei, I.A.2    Yu, L.3
  • 35
    • 0001759976 scopus 로고
    • The Ostwald step rule
    • Van Santen R.A. The Ostwald step rule. J. Phys. Chem. 88 (1984) 5768-5769
    • (1984) J. Phys. Chem. , vol.88 , pp. 5768-5769
    • Van Santen, R.A.1
  • 36
    • 22144496413 scopus 로고    scopus 로고
    • Does water play a structural role in the folding of small nucleic acids?
    • Sorin E.J., Rhee Y.M., and Pande V.S. Does water play a structural role in the folding of small nucleic acids?. Biophys. J. 88 (2005) 2516-2524
    • (2005) Biophys. J. , vol.88 , pp. 2516-2524
    • Sorin, E.J.1    Rhee, Y.M.2    Pande, V.S.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.