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Volumn 425, Issue 18, 2013, Pages 3522-3535

The role of aromatic-aromatic interactions in strand-strand stabilization of β-sheets

Author keywords

Dynamics; Folding; Hydrogen bond; Stacking; barrel

Indexed keywords

CELLULAR RETINOIC ACID BINDING PROTEIN 1; HYDROGEN; LIPID BINDING PROTEIN; PHENYLALANINE; RETINOIC ACID BINDING PROTEIN; UNCLASSIFIED DRUG;

EID: 84883305785     PISSN: 00222836     EISSN: 10898638     Source Type: Journal    
DOI: 10.1016/j.jmb.2013.06.030     Document Type: Article
Times cited : (25)

References (60)
  • 1
    • 0036897848 scopus 로고    scopus 로고
    • Aromatic interactions in model systems
    • Waters ML. Aromatic interactions in model systems. Curr Opin Chem Biol 2002;6:736-41.
    • (2002) Curr Opin Chem Biol , vol.6 , pp. 736-741
    • Waters, M.L.1
  • 2
    • 34848842845 scopus 로고    scopus 로고
    • Geometry of nonbonded interactions involving planar groups in proteins
    • Chakrabarti P, Bhattacharyya R. Geometry of nonbonded interactions involving planar groups in proteins. Prog Biophys Mol Biol 2007;95:83-137.
    • (2007) Prog Biophys Mol Biol , vol.95 , pp. 83-137
    • Chakrabarti, P.1    Bhattacharyya, R.2
  • 3
    • 47249128045 scopus 로고    scopus 로고
    • A reexamination of the propensities of amino acids towards a particular secondary structure: Classification of amino acids based on their chemical structure
    • Malkov SN, Zivkovic MV, Beljanski MV, Hall MB, Zaric SD. A reexamination of the propensities of amino acids towards a particular secondary structure: classification of amino acids based on their chemical structure. J Mol Model 2008;14: 769-75.
    • (2008) J Mol Model , vol.14 , pp. 769-775
    • Malkov, S.N.1    Zivkovic, M.V.2    Beljanski, M.V.3    Hall, M.B.4    Zaric, S.D.5
  • 4
    • 0036721382 scopus 로고    scopus 로고
    • Aromatic side-chain interactions in proteins. I. Main structural features
    • Thomas A, Meurisse R, Charloteaux B, Brasseur R. Aromatic side-chain interactions in proteins. I. Main structural features. Proteins 2002;48:628-34.
    • (2002) Proteins , vol.48 , pp. 628-634
    • Thomas, A.1    Meurisse, R.2    Charloteaux, B.3    Brasseur, R.4
  • 5
    • 0036841958 scopus 로고    scopus 로고
    • Protein aggregation in disease: A role for folding intermediates forming specific multimeric interactions
    • Horwich A. Protein aggregation in disease: a role for folding intermediates forming specific multimeric interactions. J Clin Invest 2002;110:1221-32.
    • (2002) J Clin Invest , vol.110 , pp. 1221-1232
    • Horwich, A.1
  • 6
    • 28244437028 scopus 로고    scopus 로고
    • The Yin and Yang of protein folding
    • Jahn TR, Radford SE. The Yin and Yang of protein folding. FEBS J 2005;272:5962-70.
    • (2005) FEBS J , vol.272 , pp. 5962-5970
    • Jahn, T.R.1    Radford, S.E.2
  • 7
    • 0032502839 scopus 로고    scopus 로고
    • Contact order, transition state placement and the refolding rates of single domain proteins
    • Plaxco KW, Simons KT, Baker D. Contact order, transition state placement and the refolding rates of single domain proteins. J Mol Biol 1998;277:985-94.
    • (1998) J Mol Biol , vol.277 , pp. 985-994
    • Plaxco, K.W.1    Simons, K.T.2    Baker, D.3
  • 8
    • 35648931551 scopus 로고    scopus 로고
    • On the role of structural class of a protein with two-state folding kinetics in determining correlations between its size, topology, and folding rate
    • Istomin AY, Jacobs DJ, Livesay DR. On the role of structural class of a protein with two-state folding kinetics in determining correlations between its size, topology, and folding rate. Protein Sci 2007;16:2564-9.
    • (2007) Protein Sci , vol.16 , pp. 2564-2569
    • Istomin, A.Y.1    Jacobs, D.J.2    Livesay, D.R.3
  • 9
    • 3142782241 scopus 로고    scopus 로고
    • Quantifying the roughness on the free energy landscape: Entropic bottlenecks and protein folding rates
    • Chavez LL, Onuchic JN, Clementi C. Quantifying the roughness on the free energy landscape: entropic bottlenecks and protein folding rates. J Am Chem Soc 2004;126:8426-32.
    • (2004) J Am Chem Soc , vol.126 , pp. 8426-8432
    • Chavez, L.L.1    Onuchic, J.N.2    Clementi, C.3
  • 11
    • 0037077578 scopus 로고    scopus 로고
    • Selective aromatic interactions in β-hairpin peptides
    • Tatko CD, Waters ML. Selective aromatic interactions in β-hairpin peptides. J Am Chem Soc 2002;124:9372-3.
    • (2002) J Am Chem Soc , vol.124 , pp. 9372-9373
    • Tatko, C.D.1    Waters, M.L.2
  • 12
    • 31944446531 scopus 로고    scopus 로고
    • NMR analysis of aromatic interactions in designed peptide β-hairpins
    • Mahalakshmi R, Raghothama S, Balaram P. NMR analysis of aromatic interactions in designed peptide β-hairpins. J Am Chem Soc 2006;128:1125-38.
    • (2006) J Am Chem Soc , vol.128 , pp. 1125-1138
    • Mahalakshmi, R.1    Raghothama, S.2    Balaram, P.3
  • 13
    • 84871029355 scopus 로고    scopus 로고
    • NMR analysis of cross strand aromatic interactions in an 8 residue hairpin and a 14 residue three stranded β-sheet peptide
    • Sonti R, Rai R, Ragothama S, Balaram P. NMR analysis of cross strand aromatic interactions in an 8 residue hairpin and a 14 residue three stranded β-sheet peptide. J Phys Chem B 2012;116:14207-15.
    • (2012) J Phys Chem B , vol.116 , pp. 14207-14215
    • Sonti, R.1    Rai, R.2    Ragothama, S.3    Balaram, P.4
  • 14
    • 22244463276 scopus 로고    scopus 로고
    • The absence of favorable aromatic interactions between β-sheet peptides
    • Chung DM, Dou Y, Baldi P, Nowick JS. The absence of favorable aromatic interactions between β-sheet peptides. J Am Chem Soc 2005;127:9998-9.
    • (2005) J Am Chem Soc , vol.127 , pp. 9998-9999
    • Chung, D.M.1    Dou, Y.2    Baldi, P.3    Nowick, J.S.4
  • 15
    • 0022419375 scopus 로고
    • Aromatic-aromatic interaction: A mechanism of protein structure stabilization
    • Burley SK, Petsko GA. Aromatic-aromatic interaction: a mechanism of protein structure stabilization. Science 1985;229:23-8.
    • (1985) Science , vol.229 , pp. 23-28
    • Burley, S.K.1    Petsko, G.A.2
  • 16
    • 0033773555 scopus 로고    scopus 로고
    • Role of a solvent-exposed aromatic cluster in the folding of Escherichia coli CspA
    • Rodriguez HM, Vu DM, Gregoret LM. Role of a solvent-exposed aromatic cluster in the folding of Escherichia coli CspA. Protein Sci 2000;9:1993-2000.
    • (2000) Protein Sci , vol.9 , pp. 1993-2000
    • Rodriguez, H.M.1    Vu, D.M.2    Gregoret, L.M.3
  • 17
    • 4344660409 scopus 로고    scopus 로고
    • Buried hydrophobic side-chains essential for the folding of the parallel β-helix domains of the P22 tailspike
    • Betts S, Haase-Pettingell C, Cook K, King J. Buried hydrophobic side-chains essential for the folding of the parallel β-helix domains of the P22 tailspike. Protein Sci 2004;13:2291-303.
    • (2004) Protein Sci , vol.13 , pp. 2291-2303
    • Betts, S.1    Haase-Pettingell, C.2    Cook, K.3    King, J.4
  • 18
    • 79952151932 scopus 로고    scopus 로고
    • Contributions of aromatic pairs to the folding and stability of long-lived human ãD-crystallin
    • Kong F, King J. Contributions of aromatic pairs to the folding and stability of long-lived human ãD-crystallin. Protein Sci 2011;20:513-28.
    • (2011) Protein Sci , vol.20 , pp. 513-528
    • Kong, F.1    King, J.2
  • 19
    • 0036812339 scopus 로고    scopus 로고
    • Evolution of the family of intracellular lipid binding proteins in vertebrates
    • Schaap FG, van der Vusse GJ, Glatz JF. Evolution of the family of intracellular lipid binding proteins in vertebrates. Mol Cell Biochem 2002;239:69-77.
    • (2002) Mol Cell Biochem , vol.239 , pp. 69-77
    • Schaap, F.G.1    Van Der Vusse, G.J.2    Glatz, J.F.3
  • 20
    • 0030716169 scopus 로고    scopus 로고
    • Cavity formation before stable hydrogen bonding in the folding of a β-clam protein
    • Clark PL, Liu ZP, Rizo J, Gierasch LM. Cavity formation before stable hydrogen bonding in the folding of a β-clam protein. Nat Struct Biol 1997;4:883-6.
    • (1997) Nat Struct Biol , vol.4 , pp. 883-886
    • Clark, P.L.1    Liu, Z.P.2    Rizo, J.3    Gierasch, L.M.4
  • 21
    • 0031784567 scopus 로고    scopus 로고
    • Probing the folding pathway of a β-clam protein with single-tryptophan constructs
    • Clark PL, Weston BF, Gierasch LM. Probing the folding pathway of a β-clam protein with single-tryptophan constructs. Folding Des 1998;3:401-12.
    • (1998) Folding des , vol.3 , pp. 401-412
    • Clark, P.L.1    Weston, B.F.2    Gierasch, L.M.3
  • 22
    • 0347089152 scopus 로고    scopus 로고
    • Sequence and structural analysis of cellular retinoic acid-binding proteins reveals a network of conserved hydrophobic interactions
    • Gunasekaran K, Hagler AT, Gierasch LM. Sequence and structural analysis of cellular retinoic acid-binding proteins reveals a network of conserved hydrophobic interactions. Proteins 2004;54:179-94.
    • (2004) Proteins , vol.54 , pp. 179-194
    • Gunasekaran, K.1    Hagler, A.T.2    Gierasch, L.M.3
  • 23
    • 0034622583 scopus 로고    scopus 로고
    • Dynamics of cellular retinoic acid binding protein i on multiple time scales with implications for ligand binding
    • Krishnan VV, Sukumar M, Gierasch LM, Cosman M. Dynamics of cellular retinoic acid binding protein I on multiple time scales with implications for ligand binding. Biochemistry 2000;39:9119-29.
    • (2000) Biochemistry , vol.39 , pp. 9119-9129
    • Krishnan, V.V.1    Sukumar, M.2    Gierasch, L.M.3    Cosman, M.4
  • 24
    • 0031036243 scopus 로고    scopus 로고
    • Discrete backbone disorder in the nuclear magnetic resonance structure of apo intestinal fatty acid-binding protein: Implications for the mechanism of ligand entry
    • Hodsdon ME, Cistola DP. Discrete backbone disorder in the nuclear magnetic resonance structure of apo intestinal fatty acid-binding protein: implications for the mechanism of ligand entry. Biochemistry 1997;36:1450-60.
    • (1997) Biochemistry , vol.36 , pp. 1450-1460
    • Hodsdon, M.E.1    Cistola, D.P.2
  • 25
    • 44349108965 scopus 로고    scopus 로고
    • Conformational and dynamics changes induced by bile acids binding to chicken liver bile acid binding protein
    • Eberini I, Rocco AG, Ientile AR, Baptista AM, Gianazza E, Tomaselli S, et al. Conformational and dynamics changes induced by bile acids binding to chicken liver bile acid binding protein. Proteins 2008;71:1889-98.
    • (2008) Proteins , vol.71 , pp. 1889-1898
    • Eberini, I.1    Rocco, A.G.2    Ientile, A.R.3    Baptista, A.M.4    Gianazza, E.5    Tomaselli, S.6
  • 26
    • 0030933329 scopus 로고    scopus 로고
    • Modeling unfolded states of proteins and peptides. II. Backbone solvent accessibility
    • Creamer TP, Srinivasan R, Rose GD. Modeling unfolded states of proteins and peptides. II. Backbone solvent accessibility. Biochemistry 1997;36:2832-5.
    • (1997) Biochemistry , vol.36 , pp. 2832-2835
    • Creamer, T.P.1    Srinivasan, R.2    Rose, G.D.3
  • 27
    • 0038309560 scopus 로고    scopus 로고
    • Analysis of accessible surface of residues in proteins
    • Lins L, Thomas A, Brasseur R. Analysis of accessible surface of residues in proteins. Protein Sci 2003;12:1406-17.
    • (2003) Protein Sci , vol.12 , pp. 1406-1417
    • Lins, L.1    Thomas, A.2    Brasseur, R.3
  • 28
    • 42149084432 scopus 로고    scopus 로고
    • Assessing the solvent-dependent surface area of unfolded proteins using an ensemble model
    • Gong H, Rose GD. Assessing the solvent-dependent surface area of unfolded proteins using an ensemble model. Proc Natl Acad Sci USA 2008;105:3321-6.
    • (2008) Proc Natl Acad Sci USA , vol.105 , pp. 3321-3326
    • Gong, H.1    Rose, G.D.2
  • 30
    • 0026511656 scopus 로고
    • The folding of an enzyme. I. Theory of protein engineering analysis of stability and pathway of protein folding
    • Fersht AR, Matouschek A, Serrano L. The folding of an enzyme. I. Theory of protein engineering analysis of stability and pathway of protein folding. J Mol Biol 1992;224:771-82.
    • (1992) J Mol Biol , vol.224 , pp. 771-782
    • Fersht, A.R.1    Matouschek, A.2    Serrano, L.3
  • 31
    • 0028820703 scopus 로고
    • Denaturantmvalues and heat capacity changes: Relation to changes in accessible surface areas of protein unfolding
    • Myers JK, PaceCN, ScholtzJM.Denaturantmvalues and heat capacity changes: relation to changes in accessible surface areas of protein unfolding. Protein Sci 1995;4:2138-48.
    • (1995) Protein Sci , vol.4 , pp. 2138-2148
    • Myers, J.K.1    Pace, C.N.2    Scholtz, J.M.3
  • 32
    • 0027171034 scopus 로고
    • Application of physical organic chemistry to engineered mutants of proteins: Hammond postulate behavior in the transition state of protein folding
    • Matouschek A, Fersht AR. Application of physical organic chemistry to engineered mutants of proteins: Hammond postulate behavior in the transition state of protein folding. Proc Natl Acad Sci USA 1993;90:7814-8.
    • (1993) Proc Natl Acad Sci USA , vol.90 , pp. 7814-7818
    • Matouschek, A.1    Fersht, A.R.2
  • 34
    • 0029125852 scopus 로고
    • Crystal structure of cellular retinoic acid binding protein i shows increased access to the binding cavity due to formation of an intermolecular β-sheet
    • Thompson JR, Bratt JM, Banaszak LJ. Crystal structure of cellular retinoic acid binding protein I shows increased access to the binding cavity due to formation of an intermolecular β-sheet. J Mol Biol 1995;252:433-46.
    • (1995) J Mol Biol , vol.252 , pp. 433-446
    • Thompson, J.R.1    Bratt, J.M.2    Banaszak, L.J.3
  • 35
    • 0028774713 scopus 로고
    • Crystal structures of cellular retinoic acid binding proteins i and II in complex with all-trans-retinoic acid and a synthetic retinoid
    • Kleywegt GJ, Bergfors T, Senn H, Le Motte P, Gsell B, Shudo K, et al. Crystal structures of cellular retinoic acid binding proteins I and II in complex with all-trans-retinoic acid and a synthetic retinoid. Structure 1994;2:1241-58.
    • (1994) Structure , vol.2 , pp. 1241-1258
    • Kleywegt, G.J.1    Bergfors, T.2    Senn, H.3    Le Motte, P.4    Gsell, B.5    Shudo, K.6
  • 36
    • 14044269529 scopus 로고    scopus 로고
    • NMR studies of 4-19F-phenylalanine-labeled intestinal fatty acid binding protein: Evidence for conformational heterogeneity in the native state
    • Li H, Frieden C. NMR studies of 4-19F-phenylalanine-labeled intestinal fatty acid binding protein: evidence for conformational heterogeneity in the native state. Biochemistry 2005;44:2369-77.
    • (2005) Biochemistry , vol.44 , pp. 2369-2377
    • Li, H.1    Frieden, C.2
  • 37
    • 77952688100 scopus 로고    scopus 로고
    • New insights on the protein-ligand interaction differences between the two primary cellular retinol carriers
    • Franzoni L, Cavazzini D, Rossi GL, Lucke C. New insights on the protein-ligand interaction differences between the two primary cellular retinol carriers. J Lipid Res 2010;51:1332-43.
    • (2010) J Lipid Res , vol.51 , pp. 1332-1343
    • Franzoni, L.1    Cavazzini, D.2    Rossi, G.L.3    Lucke, C.4
  • 38
    • 77954257799 scopus 로고    scopus 로고
    • ConSurf 2010: Calculating evolutionary conservation in sequence and structure of proteins and nucleic acids
    • Ashkenazy H, Erez E, Martz E, Pupko T, Ben-Tal N. ConSurf 2010: calculating evolutionary conservation in sequence and structure of proteins and nucleic acids. Nucleic Acids Res 2010;38:W529-33.
    • (2010) Nucleic Acids Res , vol.38
    • Ashkenazy, H.1    Erez, E.2    Martz, E.3    Pupko, T.4    Ben-Tal, N.5
  • 39
    • 75549084424 scopus 로고    scopus 로고
    • PDBselect 1992-2009 and PDBfilterselect
    • Griep S, Hobohm U. PDBselect 1992-2009 and PDBfilterselect. Nucleic Acids Res 2009;38:D318-9.
    • (2009) Nucleic Acids Res , vol.38
    • Griep, S.1    Hobohm, U.2
  • 40
    • 79251560304 scopus 로고    scopus 로고
    • Residual interactions in unfolded bile acid-binding protein by 19FNMR
    • Basehore HK, Ropson IJ.Residual interactions in unfolded bile acid-binding protein by 19FNMR. ProteinSci 2011;20:327-35.
    • (2011) ProteinSci , vol.20 , pp. 327-335
    • Basehore, H.K.1    Ropson, I.J.2
  • 41
    • 34547545562 scopus 로고    scopus 로고
    • Observation of sequential steps in the folding of intestinal fatty acid binding protein using a slow folding mutant and 19F NMR
    • Li H, Frieden C. Observation of sequential steps in the folding of intestinal fatty acid binding protein using a slow folding mutant and 19F NMR. Proc Natl Acad Sci USA 2007;104: 11993-8.
    • (2007) Proc Natl Acad Sci USA , vol.104 , pp. 11993-11998
    • Li, H.1    Frieden, C.2
  • 42
    • 0039165184 scopus 로고    scopus 로고
    • A comparative study of the backbone dynamics of two closely related lipid binding proteins: Bovine heart fatty acid binding protein and porcine ileal lipid binding protein
    • Lucke C, Fushman D, Ludwig C, Hamilton JA, Sacchettini JC, Ruterjans H. A comparative study of the backbone dynamics of two closely related lipid binding proteins: bovine heart fatty acid binding protein and porcine ileal lipid binding protein. Mol Cell Biochem 1999;192:109-21.
    • (1999) Mol Cell Biochem , vol.192 , pp. 109-121
    • Lucke, C.1    Fushman, D.2    Ludwig, C.3    Hamilton, J.A.4    Sacchettini, J.C.5    Ruterjans, H.6
  • 43
    • 35848964084 scopus 로고    scopus 로고
    • Structural and dynamic determinants of ligand binding in the ternary complex of chicken liver bile acid binding protein with two bile salts revealed by NMR
    • Eliseo T, Ragona L, CatalanoM, AssfalgM, PaciM, Zetta L, et al. Structural and dynamic determinants of ligand binding in the ternary complex of chicken liver bile acid binding protein with two bile salts revealed by NMR. Biochemistry 2007;46:12557-67.
    • (2007) Biochemistry , vol.46 , pp. 12557-12567
    • Eliseo, T.1    Ragona, L.2    Assfalgm, C.3    Pacim Zetta, L.4
  • 44
    • 0036216060 scopus 로고    scopus 로고
    • Aromatic-aromatic interactions in and around á-helices
    • Bhattacharyya R, Samanta U, Chakrabarti P. Aromatic-aromatic interactions in and around á-helices. Protein Eng 2002;15:91-100.
    • (2002) Protein Eng , vol.15 , pp. 91-100
    • Bhattacharyya, R.1    Samanta, U.2    Chakrabarti, P.3
  • 45
    • 0037151644 scopus 로고    scopus 로고
    • Contribution of aromatic interactions to á-helix stability
    • Butterfield SM, Patel PR, Waters ML. Contribution of aromatic interactions to á-helix stability. J Am Chem Soc 2002;124:9751-5.
    • (2002) J Am Chem Soc , vol.124 , pp. 9751-9755
    • Butterfield, S.M.1    Patel, P.R.2    Waters, M.L.3
  • 46
    • 0038631832 scopus 로고    scopus 로고
    • Aromatic-aromatic interactions in crystal structures of helical peptide scaffolds containing projecting phenylalanine residues
    • Aravinda S, Shamala N, Das C, Sriranjini A, Karle IL, Balaram P. Aromatic-aromatic interactions in crystal structures of helical peptide scaffolds containing projecting phenylalanine residues. J Am Chem Soc 2003;125: 5308-15.
    • (2003) J Am Chem Soc , vol.125 , pp. 5308-5315
    • Aravinda, S.1    Shamala, N.2    Das, C.3    Sriranjini, A.4    Karle, I.L.5    Balaram, P.6
  • 47
    • 34547857813 scopus 로고    scopus 로고
    • Aromatic and cation-pi interactions enhance helix-helix association in a membrane environment
    • Johnson RM, Hecht K, Deber CM. Aromatic and cation-pi interactions enhance helix-helix association in a membrane environment. Biochemistry 2007;46:9208-14.
    • (2007) Biochemistry , vol.46 , pp. 9208-9214
    • Johnson, R.M.1    Hecht, K.2    Deber, C.M.3
  • 49
    • 0034495733 scopus 로고    scopus 로고
    • Aromatic clusters: A determinant of thermal stability of thermophilic proteins
    • Kannan N, Vishveshwara S. Aromatic clusters: a determinant of thermal stability of thermophilic proteins. Protein Eng 2000;13:753-61.
    • (2000) Protein Eng , vol.13 , pp. 753-761
    • Kannan, N.1    Vishveshwara, S.2
  • 50
    • 82655179916 scopus 로고    scopus 로고
    • Aromatic residues link binding and function of intrinsically disordered proteins
    • Espinoza-Fonseca LM. Aromatic residues link binding and function of intrinsically disordered proteins. Mol Biosyst 2012;8:237-46.
    • (2012) Mol Biosyst , vol.8 , pp. 237-246
    • Espinoza-Fonseca, L.M.1
  • 51
    • 0036135139 scopus 로고    scopus 로고
    • A possible role for pi-stacking in the self-assembly of amyloid fibrils
    • Gazit E. A possible role for pi-stacking in the self-assembly of amyloid fibrils. FASEB J 2002;16:77-83.
    • (2002) FASEB J , vol.16 , pp. 77-83
    • Gazit, E.1
  • 52
    • 33645510751 scopus 로고    scopus 로고
    • Assessing the role of aromatic residues in the amyloid aggregation of human muscle acylphosphatase
    • Bemporad F, Taddei N, Stefani M, Chiti F. Assessing the role of aromatic residues in the amyloid aggregation of human muscle acylphosphatase. Protein Sci 2006;15:862-70.
    • (2006) Protein Sci , vol.15 , pp. 862-870
    • Bemporad, F.1    Taddei, N.2    Stefani, M.3    Chiti, F.4
  • 53
    • 0032546782 scopus 로고    scopus 로고
    • Pi-Stacking interactions. Alive and well in proteins
    • McGaughey GB, Gagne M, Rappe AK. pi-Stacking interactions. Alive and well in proteins. J Biol Chem 1998;273: 15458-63.
    • (1998) J Biol Chem , vol.273 , pp. 15458-15463
    • McGaughey, G.B.1    Gagne, M.2    Rappe, A.K.3
  • 54
    • 0037100671 scopus 로고    scopus 로고
    • MAFFT: A novel method for rapid multiple sequence alignment based on fast Fourier transform
    • Katoh K, Misawa K, Kuma K, Miyata T. MAFFT: a novel method for rapid multiple sequence alignment based on fast Fourier transform. Nucleic Acids Res 2002;30:3059-66.
    • (2002) Nucleic Acids Res , vol.30 , pp. 3059-3066
    • Katoh, K.1    Misawa, K.2    Kuma, K.3    Miyata, T.4
  • 55
    • 84875592758 scopus 로고    scopus 로고
    • GROMACS 4.5: A high-throughput and highly parallel open source molecular simulation toolkit
    • Pronk S, Pall S, Schulz R, Larsson P, Bjelkmar P, Apostolov R, et al. GROMACS 4.5: a high-throughput and highly parallel open source molecular simulation toolkit. Bioinformatics 2013;29:845-54.
    • (2013) Bioinformatics , vol.29 , pp. 845-854
    • Pronk, S.1    Pall, S.2    Schulz, R.3    Larsson, P.4    Bjelkmar, P.5    Apostolov, R.6
  • 56
    • 0026724165 scopus 로고
    • Mutating the charged residues in the binding pocket of cellular retinoic acid-binding protein simultaneously reduces its binding affinity to retinoic acid and increases its thermostability
    • Zhang J, Liu ZP, Jones TA, Gierasch LM, Sambrook JF. Mutating the charged residues in the binding pocket of cellular retinoic acid-binding protein simultaneously reduces its binding affinity to retinoic acid and increases its thermostability. Proteins 1992;13:87-99.
    • (1992) Proteins , vol.13 , pp. 87-99
    • Zhang, J.1    Liu, Z.P.2    Jones, T.A.3    Gierasch, L.M.4    Sambrook, J.F.5
  • 59
    • 0017075905 scopus 로고
    • Binding affinities of retinol and related compounds to retinol binding proteins
    • Cogan U, Kopelman M, Mokady S, Shinitzky M. Binding affinities of retinol and related compounds to retinol binding proteins. Eur J Biochem 1976;65:71-8.
    • (1976) Eur J Biochem , vol.65 , pp. 71-78
    • Cogan, U.1    Kopelman, M.2    Mokady, S.3    Shinitzky, M.4
  • 60
    • 0022555885 scopus 로고
    • Determination and analysis of urea and guanidine hydrochloride denaturation curves
    • Pace CN. Determination and analysis of urea and guanidine hydrochloride denaturation curves. Methods Enzymol 1986;131:266-80.
    • (1986) Methods Enzymol , vol.131 , pp. 266-280
    • Pace, C.N.1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.