메뉴 건너뛰기




Volumn 107, Issue 40, 2010, Pages 17101-17106

Hydration dynamics at fluorinated protein surfaces

Author keywords

Fluorine; Noncanonical amino acids; Protein engineering; Solvation dynamics; Ultrafast hydration

Indexed keywords

2 AMINO 4 METHYLHEXANOIC ACID; 5,5,5 TRIFLUOROLEUCINE; FLUORINE DERIVATIVE; HEXANOIC ACID DERIVATIVE; UNCLASSIFIED DRUG; WATER;

EID: 78049299552     PISSN: 00278424     EISSN: 10916490     Source Type: Journal    
DOI: 10.1073/pnas.1011569107     Document Type: Article
Times cited : (65)

References (56)
  • 3
    • 33749019097 scopus 로고    scopus 로고
    • Innovation: A chemical toolkit for proteins - An expanded genetic code
    • Xie JM, Schultz PG (2006) Innovation: a chemical toolkit for proteins - an expanded genetic code. Nat Rev Mol Cell Biol 7:775-782.
    • (2006) Nat Rev Mol Cell Biol , vol.7 , pp. 775-782
    • Xie, J.M.1    Schultz, P.G.2
  • 4
    • 0033912062 scopus 로고    scopus 로고
    • Towards the nonstick egg: Designing fluorous proteins
    • Marsh ENG (2000) Towards the nonstick egg: designing fluorous proteins. Chem Biol 7:R153-R157.
    • (2000) Chem Biol , vol.7
    • Marsh, E.N.G.1
  • 5
    • 33751408183 scopus 로고    scopus 로고
    • Bioorthogonal noncovalent chemistry: Fluorous phases in chemical biology
    • Yoder NC, Yuksel D, Dafik L, Kumar K (2006) Bioorthogonal noncovalent chemistry: fluorous phases in chemical biology. Curr Opin Chem Biol 10:576-583.
    • (2006) Curr Opin Chem Biol , vol.10 , pp. 576-583
    • Yoder, N.C.1    Yuksel, D.2    Dafik, L.3    Kumar, K.4
  • 6
    • 0034817253 scopus 로고    scopus 로고
    • A coiled coil with a fluorous core
    • Bilgicer B, Fichera A, Kumar K (2001) A coiled coil with a fluorous core. J Am Chem Soc 123:4393-4399.
    • (2001) J Am Chem Soc , vol.123 , pp. 4393-4399
    • Bilgicer, B.1    Fichera, A.2    Kumar, K.3
  • 7
    • 33746320232 scopus 로고    scopus 로고
    • Fluorine in a native protein environment-how the spatial demand and polarity of fluoroalkyl groups affect protein folding
    • Jackel C, Salwiczek M, Koksch B (2006) Fluorine in a native protein environment-how the spatial demand and polarity of fluoroalkyl groups affect protein folding. Angewandte Chemie International Edition 45:4198-4203.
    • (2006) Angewandte Chemie International Edition , vol.45 , pp. 4198-4203
    • Jackel, C.1    Salwiczek, M.2    Koksch, B.3
  • 8
    • 11144320703 scopus 로고    scopus 로고
    • Fluorous effect in proteins: De novo design and characterization of a four-alpha-helix bundle protein containing hexafluoroleucine
    • Lee KH, Lee HY, Slutsky MM, Anderson JT, Marsh ENG (2004) Fluorous effect in proteins: de novo design and characterization of a four-alpha-helix bundle protein containing hexafluoroleucine. Biochemistry 43:16277-16284.
    • (2004) Biochemistry , vol.43 , pp. 16277-16284
    • Lee, K.H.1    Lee, H.Y.2    Slutsky, M.M.3    Anderson, J.T.4    Marsh, E.N.G.5
  • 9
    • 59649103752 scopus 로고    scopus 로고
    • Biosynthesis and stability of coiled-coil peptides containing (2S,4R)-5,5,5-Trifluoroleucine and (2S,4S)-5,5,5-Trifluoroleucine
    • Montclare JK, Son S, Clark GA, Kumar K, Tirrell DA (2009) Biosynthesis and stability of coiled-coil peptides containing (2S,4R)-5,5,5-Trifluoroleucine and (2S,4S)-5,5,5-Trifluoroleucine. ChemBioChem 10:84-86.
    • (2009) ChemBioChem , vol.10 , pp. 84-86
    • Montclare, J.K.1    Son, S.2    Clark, G.A.3    Kumar, K.4    Tirrell, D.A.5
  • 10
    • 33747179843 scopus 로고    scopus 로고
    • Stabilization of bzip peptides through incorporation of fluorinated aliphatic residues
    • Son S, Tanrikulu IC, Tirrell DA (2006) Stabilization of bzip peptides through incorporation of fluorinated aliphatic residues. ChemBioChem 7:1251-1257.
    • (2006) ChemBioChem , vol.7 , pp. 1251-1257
    • Son, S.1    Tanrikulu, I.C.2    Tirrell, D.A.3
  • 11
    • 0035901630 scopus 로고    scopus 로고
    • Fluorinated coiled-coil proteins prepared in vivo display enhanced thermal and chemical stability
    • Tang Y, et al. (2001) Fluorinated coiled-coil proteins prepared in vivo display enhanced thermal and chemical stability. Angewandte Chemie International Edition 40:1494-1496.
    • (2001) Angewandte Chemie International Edition , vol.40 , pp. 1494-1496
    • Tang, Y.1
  • 12
    • 0035823858 scopus 로고    scopus 로고
    • Biosynthesis of a highly stable coiled-coil protein containing hexafluoroleucine in an engineered bacterial host
    • Tang Y, Tirrell DA (2001) Biosynthesis of a highly stable coiled-coil protein containing hexafluoroleucine in an engineered bacterial host. J Am Chem Soc 123:11089-11090.
    • (2001) J Am Chem Soc , vol.123 , pp. 11089-11090
    • Tang, Y.1    Tirrell, D.A.2
  • 14
    • 0038276996 scopus 로고    scopus 로고
    • Incorporation of trifluoroisoleucine into proteins in vivo
    • Wang P, Tang Y, Tirrell DA (2003) Incorporation of trifluoroisoleucine into proteins in vivo. J Am Chem Soc 125:6900-6906.
    • (2003) J Am Chem Soc , vol.125 , pp. 6900-6906
    • Wang, P.1    Tang, Y.2    Tirrell, D.A.3
  • 15
    • 35348855019 scopus 로고    scopus 로고
    • Evolution of a fluorinated green fluorescent protein
    • Yoo TH, Link AJ, Tirrell DA (2007) Evolution of a fluorinated green fluorescent protein. Proc Natl Acad Sci USA 104:13887-13890.
    • (2007) Proc Natl Acad Sci USA , vol.104 , pp. 13887-13890
    • Yoo, T.H.1    Link, A.J.2    Tirrell, D.A.3
  • 16
    • 34447572857 scopus 로고    scopus 로고
    • High-throughput screening for Methionyl-tRNA synthetases that enable residue-specific incorporation of noncanonical amino acids into recombinant proteins in bacterial cells.
    • Yoo TH, Tirrell DA (2007) High-throughput screening for Methionyl-tRNA synthetases that enable residue-specific incorporation of noncanonical amino acids into recombinant proteins in bacterial cells. . Angewandte Chemie International Edition 46:5340-5343.
    • (2007) Angewandte Chemie International Edition , vol.46 , pp. 5340-5343
    • Yoo, T.H.1    Tirrell, D.A.2
  • 17
    • 4544316921 scopus 로고    scopus 로고
    • The polar hydrophobicity of fluorinated compounds
    • Biffinger JC, Kim HW, DiMagno SG (2004) The polar hydrophobicity of fluorinated compounds. ChemBioChem 5:622-627.
    • (2004) ChemBioChem , vol.5 , pp. 622-627
    • Biffinger, J.C.1    Kim, H.W.2    DiMagno, S.G.3
  • 18
    • 0028998264 scopus 로고
    • Increasing binding constants of ligands to carbonic-anhydrase by using greasy tails
    • Gao JM, Qiao S, Whitesides GM (1995) Increasing binding constants of ligands to carbonic-anhydrase by using greasy tails. J Med Chem 38:2292-2301.
    • (1995) J Med Chem , vol.38 , pp. 2292-2301
    • Gao, J.M.1    Qiao, S.2    Whitesides, G.M.3
  • 19
    • 27644457086 scopus 로고    scopus 로고
    • Fluorine in peptide design and protein engineering
    • Jackel C, Koksch B (2005) Fluorine in peptide design and protein engineering. Eur J Org Chem 2005:4483-4503.
    • (2005) Eur J Org Chem , vol.2005 , pp. 4483-4503
    • Jackel, C.1    Koksch, B.2
  • 20
    • 4544387720 scopus 로고    scopus 로고
    • Atropisomerism, biphenyls, and fluorine: A comparison of rotational barriers and twist angles
    • Leroux F (2004) Atropisomerism, biphenyls, and fluorine: a comparison of rotational barriers and twist angles. ChemBioChem 5:644-649.
    • (2004) ChemBioChem , vol.5 , pp. 644-649
    • Leroux, F.1
  • 21
    • 34848848499 scopus 로고    scopus 로고
    • Fluorine in pharmaceuticals: Looking beyond intuition
    • Muller K, Faeh C, Diederich F (2007) Fluorine in pharmaceuticals: looking beyond intuition. Science 317:1881-1886.
    • (2007) Science , vol.317 , pp. 1881-1886
    • Muller, K.1    Faeh, C.2    Diederich, F.3
  • 22
    • 4544278491 scopus 로고    scopus 로고
    • Organic fluorine: Odd man out
    • Dunitz JD (2004) Organic fluorine: odd man out. ChemBioChem 5:614-621.
    • (2004) ChemBioChem , vol.5 , pp. 614-621
    • Dunitz, J.D.1
  • 23
    • 0033531751 scopus 로고    scopus 로고
    • Oriented surface dipoles strongly influence interfacial wettabilities
    • Graupe M, Takenaga M, Koini T, Colorado R, Lee TR (1999) Oriented surface dipoles strongly influence interfacial wettabilities. J Am Chem Soc 121:3222-3223.
    • (1999) J Am Chem Soc , vol.121 , pp. 3222-3223
    • Graupe, M.1    Takenaga, M.2    Koini, T.3    Colorado, R.4    Lee, T.R.5
  • 24
    • 0037117502 scopus 로고    scopus 로고
    • Is the first hydration shell of lysozyme of higher density than bulk water?
    • Merzel F, Smith JC (2002) Is the first hydration shell of lysozyme of higher density than bulk water? Proc Natl Acad Sci USA 99:5378-5383.
    • (2002) Proc Natl Acad Sci USA , vol.99 , pp. 5378-5383
    • Merzel, F.1    Smith, J.C.2
  • 25
    • 2342527858 scopus 로고    scopus 로고
    • Dynamics of water in biological recognition
    • Pal SK, Zewail AH (2004) Dynamics of water in biological recognition. Chem Rev 104:2099-2123.
    • (2004) Chem Rev , vol.104 , pp. 2099-2123
    • Pal, S.K.1    Zewail, A.H.2
  • 26
    • 33745032291 scopus 로고    scopus 로고
    • Water mediation in protein folding and molecular recognition
    • Levy Y, Onuchic JN (2006) Water mediation in protein folding and molecular recognition. Annu Rev Biophys Biomol Struct 35:389-415.
    • (2006) Annu Rev Biophys Biomol Struct , vol.35 , pp. 389-415
    • Levy, Y.1    Onuchic, J.N.2
  • 27
    • 33748991142 scopus 로고    scopus 로고
    • Protein surface hydration mapped by site-specific mutations
    • Qiu WH, et al. (2006) Protein surface hydration mapped by site-specific mutations. Proc Natl Acad Sci USA 103:13979-13984.
    • (2006) Proc Natl Acad Sci USA , vol.103 , pp. 13979-13984
    • Qiu, W.H.1
  • 28
    • 33745470061 scopus 로고    scopus 로고
    • Ultrafast solvation dynamics of human serum albumin: Correlations with conformational transitions and site-selected recognition
    • Qiu WH, et al. (2006) Ultrafast solvation dynamics of human serum albumin: correlations with conformational transitions and site-selected recognition. J Phys Chem B 110:10540-10549.
    • (2006) J Phys Chem B , vol.110 , pp. 10540-10549
    • Qiu, W.H.1
  • 29
    • 0037204951 scopus 로고    scopus 로고
    • Probing protein electrostatics with a synthetic fluorescent amino acid
    • Cohen BE, et al. (2002) Probing protein electrostatics with a synthetic fluorescent amino acid. Science 296:1700-1703.
    • (2002) Science , vol.296 , pp. 1700-1703
    • Cohen, B.E.1
  • 30
    • 34848922762 scopus 로고    scopus 로고
    • Dehydration-driven solvent exposure of hydrophobic surfaces as a driving force in peptide folding
    • Daidone I, Ulmschneider MB, Di Nola A, Amadei A, Smith JC (2007) Dehydration-driven solvent exposure of hydrophobic surfaces as a driving force in peptide folding. Proc Natl Acad Sci USA 104:15230-15235.
    • (2007) Proc Natl Acad Sci USA , vol.104 , pp. 15230-15235
    • Daidone, I.1    Ulmschneider, M.B.2    Di Nola, A.3    Amadei, A.4    Smith, J.C.5
  • 31
    • 47249164324 scopus 로고    scopus 로고
    • Integration or segregation: How do molecules behave at oil/water interfaces?
    • Moore FG, Richmond GL (2008) Integration or segregation: how do molecules behave at oil/water interfaces? Acc Chem Res 41:739-748.
    • (2008) Acc Chem Res , vol.41 , pp. 739-748
    • Moore, F.G.1    Richmond, G.L.2
  • 32
    • 0015522150 scopus 로고
    • Determination of secondary structures of proteins by circular-dichroism and optical rotary dispersion
    • Chen YH, Yang JT, Martinez HM (1972) Determination of secondary structures of proteins by circular-dichroism and optical rotary dispersion. Biochemistry 11:4120-4131.
    • (1972) Biochemistry , vol.11 , pp. 4120-4131
    • Chen, Y.H.1    Yang, J.T.2    Martinez, H.M.3
  • 33
    • 44349189806 scopus 로고    scopus 로고
    • K2D2: Estimation of protein secondary structure from circular dichroism spectra
    • Perez-Iratxeta C, Andrade-Navarro MA (2008) K2D2: estimation of protein secondary structure from circular dichroism spectra. BMC Struct Biol 8:25-29.
    • (2008) BMC Struct Biol , vol.8 , pp. 25-29
    • Perez-Iratxeta, C.1    Andrade-Navarro, M.A.2
  • 35
    • 0035028745 scopus 로고    scopus 로고
    • Mechanisms of tryptophan fluorescence shifts in proteins
    • Vivian JT, Callis PR (2001) Mechanisms of tryptophan fluorescence shifts in proteins. Biophys J 80:2093-2109.
    • (2001) Biophys J , vol.80 , pp. 2093-2109
    • Vivian, J.T.1    Callis, P.R.2
  • 36
    • 0001966229 scopus 로고
    • ed JR Lakowicz (Plenum Press, New York)
    • Steiner RF (1991) Top. fluoresc. spectrosc, ed JR Lakowicz (Plenum Press, New York), Vol 2, pp 1-52.
    • (1991) Top. Fluoresc. Spectrosc , vol.2 , pp. 1-52
    • Steiner, R.F.1
  • 37
    • 66049120630 scopus 로고    scopus 로고
    • Ultrafast quenching of tryptophan fluorescence in proteins: Interresidue and intrahelical electron transfer
    • Qiu WH, et al. (2008) Ultrafast quenching of tryptophan fluorescence in proteins: interresidue and intrahelical electron transfer. Chem Phys 350:154-164.
    • (2008) Chem Phys , vol.350 , pp. 154-164
    • Qiu, W.H.1
  • 38
    • 24644444675 scopus 로고    scopus 로고
    • Analysis of tryptophan fluorescence lifetimes in a series of human serum albumin mutants with substitutions in subdomain 2A
    • Siemiarczuk A, Petersen CE, Ha CE, Yang JS, Bhagavan NV (2004) Analysis of tryptophan fluorescence lifetimes in a series of human serum albumin mutants with substitutions in subdomain 2A. Cell Biochem Biophys 40:115-122.
    • (2004) Cell Biochem Biophys , vol.40 , pp. 115-122
    • Siemiarczuk, A.1    Petersen, C.E.2    Ha, C.E.3    Yang, J.S.4    Bhagavan, N.V.5
  • 39
    • 69549114730 scopus 로고    scopus 로고
    • Quasi-static self-quenching of Trp-X and X-Trp dipeptides in water: Ultrafast fluorescence decay
    • Xu JH, Knutson JR (2009) Quasi-static self-quenching of Trp-X and X-Trp dipeptides in water: ultrafast fluorescence decay. J Phys Chem B 113:12084-12089.
    • (2009) J Phys Chem B , vol.113 , pp. 12084-12089
    • Xu, J.H.1    Knutson, J.R.2
  • 40
    • 1842525751 scopus 로고    scopus 로고
    • Femtosecond studies of tryptophan solvation: Correlation function and water dynamics at lipid surfaces
    • Lu WY, Kim J, Qiu WH, Zhong DP (2004) Femtosecond studies of tryptophan solvation: correlation function and water dynamics at lipid surfaces. Chem Phys Lett 388:120-126.
    • (2004) Chem Phys Lett , vol.388 , pp. 120-126
    • Lu, W.Y.1    Kim, J.2    Qiu, W.H.3    Zhong, D.P.4
  • 41
    • 33947425139 scopus 로고    scopus 로고
    • Hydration dynamics and time scales of coupled water-protein fluctuations
    • Li TP, Hassanali AAP, Kao YT, Zhong DP, Singer SJ (2007) Hydration dynamics and time scales of coupled water-protein fluctuations. J Am Chem Soc 129:3376-3382.
    • (2007) J Am Chem Soc , vol.129 , pp. 3376-3382
    • Li, T.P.1    Hassanali, A.A.P.2    Kao, Y.T.3    Zhong, D.P.4    Singer, S.J.5
  • 42
    • 68049087927 scopus 로고    scopus 로고
    • Protein hydration dynamics and molecular mechanism of coupled water-protein fluctuations
    • Zhang LY, Yang Y, Kao YT, Wang LJ, Zhong DP (2009) Protein hydration dynamics and molecular mechanism of coupled water-protein fluctuations. J Am Chem Soc 131:10677-10691.
    • (2009) J Am Chem Soc , vol.131 , pp. 10677-10691
    • Zhang, L.Y.1    Yang, Y.2    Kao, Y.T.3    Wang, L.J.4    Zhong, D.P.5
  • 43
    • 33847388020 scopus 로고    scopus 로고
    • Probing polar solvation dynamics in proteins: A molecular dynamics simulation analysis
    • Golosov AA, Karplus M (2007) Probing polar solvation dynamics in proteins: a molecular dynamics simulation analysis. J Phys Chem B 111:1482-1490.
    • (2007) J Phys Chem B , vol.111 , pp. 1482-1490
    • Golosov, A.A.1    Karplus, M.2
  • 44
    • 30744471668 scopus 로고    scopus 로고
    • Modulating protein structure with fluorous amino acids: Increased stability and native-like structure conferred on a 4-helix bundle protein by hexafluoroleucine
    • Lee HY, Lee KH, Al-Hashimi HM, Marsh ENG (2006) Modulating protein structure with fluorous amino acids: increased stability and native-like structure conferred on a 4-helix bundle protein by hexafluoroleucine. J Am Chem Soc 128:337-343.
    • (2006) J Am Chem Soc , vol.128 , pp. 337-343
    • Lee, H.Y.1    Lee, K.H.2    Al-Hashimi, H.M.3    Marsh, E.N.G.4
  • 45
    • 1542375172 scopus 로고    scopus 로고
    • Hydration dynamics near a model protein surface
    • Russo D, Hura G, Head-Gordon T (2004) Hydration dynamics near a model protein surface. Biophys J 86:1852-1862.
    • (2004) Biophys J , vol.86 , pp. 1852-1862
    • Russo, D.1    Hura, G.2    Head-Gordon, T.3
  • 47
    • 26944481188 scopus 로고    scopus 로고
    • Interfaces and the driving force of hydrophobic assembly
    • Chandler D (2005) Interfaces and the driving force of hydrophobic assembly. Nature 437:640-647.
    • (2005) Nature , vol.437 , pp. 640-647
    • Chandler, D.1
  • 48
    • 0036667303 scopus 로고    scopus 로고
    • Molecular bonding and interactions at aqueous surfaces as probed by vibrational sum frequency spectroscopy
    • Richmond GL (2002) Molecular bonding and interactions at aqueous surfaces as probed by vibrational sum frequency spectroscopy. Chem Rev 102:2693-2724.
    • (2002) Chem Rev , vol.102 , pp. 2693-2724
    • Richmond, G.L.1
  • 49
    • 33646392509 scopus 로고    scopus 로고
    • Sum-frequency vibrational spectroscopy on water interfaces: Polar orientation of water molecules at interfaces
    • Shen YR, Ostroverkhov V (2006) Sum-frequency vibrational spectroscopy on water interfaces: polar orientation of water molecules at interfaces. Chem Rev 106:1140-1154.
    • (2006) Chem Rev , vol.106 , pp. 1140-1154
    • Shen, Y.R.1    Ostroverkhov, V.2
  • 50
    • 35448953685 scopus 로고    scopus 로고
    • Solvent coarse-graining and the string method applied to the hydrophobic collapse of a hydrated chain
    • Miller TF, Vanden-Eijnden E, Chandler D (2007) Solvent coarse-graining and the string method applied to the hydrophobic collapse of a hydrated chain. Proc Natl Acad Sci USA 104:14559-14564.
    • (2007) Proc Natl Acad Sci USA , vol.104 , pp. 14559-14564
    • Miller, T.F.1    Vanden-Eijnden, E.2    Chandler, D.3
  • 51
    • 0037076337 scopus 로고    scopus 로고
    • Drying-induced hydrophobic polymer collapse
    • ten Wolde PR, Chandler D (2002) Drying-induced hydrophobic polymer collapse. Proc Natl Acad Sci USA 99:6539-6543.
    • (2002) Proc Natl Acad Sci USA , vol.99 , pp. 6539-6543
    • Ten Wolde, P.R.1    Chandler, D.2
  • 52
    • 0035980398 scopus 로고    scopus 로고
    • Effect of solute size and solute-water attractive interactions on hydration water structure around hydrophobic solutes
    • Ashbaugh HS, Paulaitis ME (2001) Effect of solute size and solute-water attractive interactions on hydration water structure around hydrophobic solutes. J Am Chem Soc 123:10721-10728.
    • (2001) J Am Chem Soc , vol.123 , pp. 10721-10728
    • Ashbaugh, H.S.1    Paulaitis, M.E.2
  • 53
    • 0037187108 scopus 로고    scopus 로고
    • The hydrophobic effect and the influence of solutesolvent attractions
    • Huang DM, Chandler D (2002) The hydrophobic effect and the influence of solutesolvent attractions. J Phys Chem B 106:2047-2053.
    • (2002) J Phys Chem B , vol.106 , pp. 2047-2053
    • Huang, D.M.1    Chandler, D.2
  • 54
    • 84930069181 scopus 로고    scopus 로고
    • Water in contact with extended hydrophobic surfaces: Direct evidence of weak dewetting
    • Jensen TR, et al. (2003) Water in contact with extended hydrophobic surfaces: direct evidence of weak dewetting. Phys Rev Lett 90:086101.
    • (2003) Phys Rev Lett , vol.90 , pp. 086101
    • Jensen, T.R.1
  • 55
    • 77952370938 scopus 로고    scopus 로고
    • On the origin of the hydrophobic water gap: An X-ray reflectivity and MD simulation study
    • Mezger M, et al. (2010) On the origin of the hydrophobic water gap: an X-ray reflectivity and MD simulation study. J Am Chem Soc 132:6735-6741.
    • (2010) J Am Chem Soc , vol.132 , pp. 6735-6741
    • Mezger, M.1
  • 56
    • 77956355917 scopus 로고    scopus 로고
    • Molecular origins of fluorocarbon hydrophobicity
    • 10.1073/pnas.0915169107
    • Rossky PJ, Dalvi VH (2010) Molecular origins of fluorocarbon hydrophobicity. Proc Natl Acad Sci USA 10.1073/pnas.0915169107.
    • (2010) Proc Natl Acad Sci USA
    • Rossky, P.J.1    Dalvi, V.H.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.