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Volumn 112, Issue 30, 2015, Pages 9270-9275

How osmolytes influence hydrophobic polymer conformations: A unified view from experiment and theory

Author keywords

Free energy; Preferential binding; Single molecule force spectroscopy; TMAO; Urea

Indexed keywords

POLYSTYRENE; TRIMETHYLAMINE OXIDE; UREA; METHYLAMINE; POLYMER; POLYSTYRENE DERIVATIVE; PROTEIN; PROTEIN BINDING; SOLVENT; TRIMETHYLOXAMINE; WATER;

EID: 84938118055     PISSN: 00278424     EISSN: 10916490     Source Type: Journal    
DOI: 10.1073/pnas.1511780112     Document Type: Article
Times cited : (102)

References (61)
  • 1
    • 0020336190 scopus 로고
    • Living with water stress: Evolution of osmolyte systems
    • Yancey PH, Clark ME, Hand SC, Bowlus RD, Somero GN (1982) Living with water stress: Evolution of osmolyte systems. Science 217(4566):1214-1222.
    • (1982) Science , vol.217 , Issue.4566 , pp. 1214-1222
    • Yancey, P.H.1    Clark, M.E.2    Hand, S.C.3    Bowlus, R.D.4    Somero, G.N.5
  • 2
    • 67650040559 scopus 로고
    • Linked functions and reciprocal effects in hemoglobin: A second look
    • Wyman J, Jr (1964) Linked functions and reciprocal effects in hemoglobin: A second look. Adv Protein Chem 19:223-286.
    • (1964) Adv Protein Chem , vol.19 , pp. 223-286
    • Wyman, J.1
  • 3
    • 0014674115 scopus 로고
    • Extension of the theory of linked functions to incorporate the effects of protein hydration
    • Tanford C (1969) Extension of the theory of linked functions to incorporate the effects of protein hydration. J Mol Biol 39(3):539-544.
    • (1969) J Mol Biol , vol.39 , Issue.3 , pp. 539-544
    • Tanford, C.1
  • 4
    • 0037162456 scopus 로고    scopus 로고
    • Protein-solvent preferential interactions, protein hydration, and the modulation of biochemical reactions by solvent components
    • Timasheff SN (2002) Protein-solvent preferential interactions, protein hydration, and the modulation of biochemical reactions by solvent components. Proc Natl Acad Sci USA 99(15):9721-9726.
    • (2002) Proc Natl Acad Sci USA , vol.99 , Issue.15 , pp. 9721-9726
    • Timasheff, S.N.1
  • 5
    • 0034635965 scopus 로고    scopus 로고
    • Osmotic stress, crowding, preferential hydration, and binding: A comparison of perspectives
    • Parsegian VA, Rand RP, Rau DC (2000) Osmotic stress, crowding, preferential hydration, and binding: A comparison of perspectives. Proc Natl Acad Sci USA 97(8):3987-3992.
    • (2000) Proc Natl Acad Sci USA , vol.97 , Issue.8 , pp. 3987-3992
    • Parsegian, V.A.1    Rand, R.P.2    Rau, D.C.3
  • 6
    • 46449109015 scopus 로고    scopus 로고
    • Structure and energetics of the hydrogen-bonded backbone in protein folding
    • Bolen DW, Rose GD (2008) Structure and energetics of the hydrogen-bonded backbone in protein folding. Annu Rev Biochem 77:339-362.
    • (2008) Annu Rev Biochem , vol.77 , pp. 339-362
    • Bolen, D.W.1    Rose, G.D.2
  • 7
    • 0034681955 scopus 로고    scopus 로고
    • Vapor pressure osmometry studies of osmolyte-protein interactions: Implications for the action of osmoprotectants in vivo and for the interpretation of "osmotic stress" experiments in vitro
    • Courtenay ES, Capp MW, Anderson CF, Record MT, Jr (2000) Vapor pressure osmometry studies of osmolyte-protein interactions: Implications for the action of osmoprotectants in vivo and for the interpretation of "osmotic stress" experiments in vitro. Biochemistry 39(15):4455-4471.
    • (2000) Biochemistry , vol.39 , Issue.15 , pp. 4455-4471
    • Courtenay, E.S.1    Capp, M.W.2    Anderson, C.F.3    Record, M.T.4
  • 8
    • 33749365298 scopus 로고    scopus 로고
    • A molecular mechanism for osmolyte-induced protein stability
    • Street TO, Bolen DW, Rose GD (2006) A molecular mechanism for osmolyte-induced protein stability. Proc Natl Acad Sci USA 103(38):13997-14002.
    • (2006) Proc Natl Acad Sci USA , vol.103 , Issue.38 , pp. 13997-14002
    • Street, T.O.1    Bolen, D.W.2    Rose, G.D.3
  • 9
    • 0030762556 scopus 로고    scopus 로고
    • A naturally occurring protective system in urea-rich cells: Mechanism of osmolyte protection of proteins against urea denaturation
    • Wang A, Bolen DW (1997) A naturally occurring protective system in urea-rich cells: Mechanism of osmolyte protection of proteins against urea denaturation. Biochemistry 36(30):9101-9108.
    • (1997) Biochemistry , vol.36 , Issue.30 , pp. 9101-9108
    • Wang, A.1    Bolen, D.W.2
  • 11
    • 0028150954 scopus 로고
    • Why do some organisms use a urea-methylamine mixture as osmolyte? Thermodynamic compensation of urea and trimethylamine N-oxide interactions with protein
    • Lin TY, Timasheff SN (1994) Why do some organisms use a urea-methylamine mixture as osmolyte? Thermodynamic compensation of urea and trimethylamine N-oxide interactions with protein. Biochemistry 33(42):12695-12701.
    • (1994) Biochemistry , vol.33 , Issue.42 , pp. 12695-12701
    • Lin, T.Y.1    Timasheff, S.N.2
  • 13
    • 0028862864 scopus 로고
    • The peptide backbone plays a dominant role in protein stabilization by naturally occurring osmolytes
    • Liu Y, Bolen DW (1995) The peptide backbone plays a dominant role in protein stabilization by naturally occurring osmolytes. Biochemistry 34(39):12884-12891.
    • (1995) Biochemistry , vol.34 , Issue.39 , pp. 12884-12891
    • Liu, Y.1    Bolen, D.W.2
  • 14
    • 80052319202 scopus 로고    scopus 로고
    • Osmolyte effects on protein stability and solubility: A balancing act between backbone and side-chains
    • Auton M, Rösgen J, Sinev M, Holthauzen LMF, Bolen DW (2011) Osmolyte effects on protein stability and solubility: A balancing act between backbone and side-chains. Biophys Chem 159(1):90-99.
    • (2011) Biophys Chem , vol.159 , Issue.1 , pp. 90-99
    • Auton, M.1    Rösgen, J.2    Sinev, M.3    Holthauzen, L.M.F.4    Bolen, D.W.5
  • 15
    • 33746882148 scopus 로고    scopus 로고
    • Metrics that differentiate the origins of osmolyte effects on protein stability: A test of the surface tension proposal
    • Auton M, Ferreon ACM, Bolen DW (2006) Metrics that differentiate the origins of osmolyte effects on protein stability: A test of the surface tension proposal. J Mol Biol 361(5):983-992.
    • (2006) J Mol Biol , vol.361 , Issue.5 , pp. 983-992
    • Auton, M.1    Ferreon, A.C.M.2    Bolen, D.W.3
  • 16
    • 77649101458 scopus 로고    scopus 로고
    • Unfolding of hydrophobic polymers in guanidinium chloride solutions
    • Godawat R, Jamadagni SN, Garde S (2010) Unfolding of hydrophobic polymers in guanidinium chloride solutions. J Phys Chem B 114(6):2246-2254.
    • (2010) J Phys Chem B , vol.114 , Issue.6 , pp. 2246-2254
    • Godawat, R.1    Jamadagni, S.N.2    Garde, S.3
  • 17
    • 84879521356 scopus 로고    scopus 로고
    • Trimethylamine N-oxide (TMAO) and tertbutyl alcohol (TBA) at hydrophobic interfaces: Insights from molecular dynamics simulations
    • Fiore A, Venkateshwaran V, Garde S (2013) Trimethylamine N-oxide (TMAO) and tertbutyl alcohol (TBA) at hydrophobic interfaces: Insights from molecular dynamics simulations. Langmuir 29(25):8017-8024.
    • (2013) Langmuir , vol.29 , Issue.25 , pp. 8017-8024
    • Fiore, A.1    Venkateshwaran, V.2    Garde, S.3
  • 18
    • 0036234983 scopus 로고    scopus 로고
    • Size and temperature dependence of hydrocarbon solubility in concentrated aqueous solutions of urea and guanidine hydrochloride
    • Graziano G (2002) Size and temperature dependence of hydrocarbon solubility in concentrated aqueous solutions of urea and guanidine hydrochloride. Can J Chem 80(4):388-400.
    • (2002) Can J Chem , vol.80 , Issue.4 , pp. 388-400
    • Graziano, G.1
  • 19
    • 80855139861 scopus 로고    scopus 로고
    • Entropic stabilization of proteins by TMAO
    • Cho SS, Reddy G, Straub JE, Thirumalai D (2011) Entropic stabilization of proteins by TMAO. J Phys Chem B 115(45):13401-13407.
    • (2011) J Phys Chem B , vol.115 , Issue.45 , pp. 13401-13407
    • Cho, S.S.1    Reddy, G.2    Straub, J.E.3    Thirumalai, D.4
  • 20
    • 34547534081 scopus 로고    scopus 로고
    • The influence of urea and trimethylamine-N-oxide on hydrophobic interactions
    • Paul S, Patey GN (2007) The influence of urea and trimethylamine-N-oxide on hydrophobic interactions. J Phys Chem B 111(28):7932-7933.
    • (2007) J Phys Chem B , vol.111 , Issue.28 , pp. 7932-7933
    • Paul, S.1    Patey, G.N.2
  • 21
    • 63149153986 scopus 로고    scopus 로고
    • Urea's action on hydrophobic interactions
    • Zangi R, Zhou R, Berne BJ (2009) Urea's action on hydrophobic interactions. J Am Chem Soc 131(4):1535-1541.
    • (2009) J Am Chem Soc , vol.131 , Issue.4 , pp. 1535-1541
    • Zangi, R.1    Zhou, R.2    Berne, B.J.3
  • 22
    • 23244459863 scopus 로고    scopus 로고
    • Osmolyte trimethylamine-N-oxide does not affect the strength of hydrophobic interactions: Origin of osmolyte compatibility
    • Athawale MV, Dordick JS, Garde S (2005) Osmolyte trimethylamine-N-oxide does not affect the strength of hydrophobic interactions: Origin of osmolyte compatibility. Biophys J 89(2):858-866.
    • (2005) Biophys J , vol.89 , Issue.2 , pp. 858-866
    • Athawale, M.V.1    Dordick, J.S.2    Garde, S.3
  • 23
    • 84887153107 scopus 로고    scopus 로고
    • Effects of the osmolyte TMAO (Trimethylamine-N-oxide) on aqueous hydrophobic contact-pair interactions
    • Macdonald RD, Khajehpour M (2013) Effects of the osmolyte TMAO (Trimethylamine-N-oxide) on aqueous hydrophobic contact-pair interactions. Biophys Chem 184:101-107.
    • (2013) Biophys Chem , vol.184 , pp. 101-107
    • Macdonald, R.D.1    Khajehpour, M.2
  • 24
    • 84869798960 scopus 로고    scopus 로고
    • Single polymer studies of hydrophobic hydration
    • Li ITS, Walker GC (2012) Single polymer studies of hydrophobic hydration. Acc Chem Res 45(11):2011-2021.
    • (2012) Acc Chem Res , vol.45 , Issue.11 , pp. 2011-2021
    • Li, I.T.S.1    Walker, G.C.2
  • 25
    • 47149098205 scopus 로고    scopus 로고
    • Force spectroscopy of polymers: Studying on intramolecular and intermolecular interactions in single molecular level
    • Zhang X, Liu C, Wang Z (2008) Force spectroscopy of polymers: Studying on intramolecular and intermolecular interactions in single molecular level. Polymer (Guildf) 49(16):3353-3361.
    • (2008) Polymer (Guildf) , vol.49 , Issue.16 , pp. 3353-3361
    • Zhang, X.1    Liu, C.2    Wang, Z.3
  • 26
    • 0034665438 scopus 로고    scopus 로고
    • Force spectroscopy of molecular systems-Single molecule spectroscopy of polymers and biomolecules
    • Janshoff A, Neitzert M, Oberdörfer Y, Fuchs H (2000) Force spectroscopy of molecular systems-Single molecule spectroscopy of polymers and biomolecules. Angew Chem Int Ed Engl 39(18):3212-3237.
    • (2000) Angew Chem Int Ed Engl , vol.39 , Issue.18 , pp. 3212-3237
    • Janshoff, A.1    Neitzert, M.2    Oberdörfer, Y.3    Fuchs, H.4
  • 27
    • 84871581078 scopus 로고    scopus 로고
    • Single-molecule adhesion of a stimuli-responsive oligo (ethylene glycol) copolymer to gold
    • Nash MA, Gaub HE (2012) Single-molecule adhesion of a stimuli-responsive oligo (ethylene glycol) copolymer to gold. ACS Nano 6(12):10735-10742.
    • (2012) ACS Nano , vol.6 , Issue.12 , pp. 10735-10742
    • Nash, M.A.1    Gaub, H.E.2
  • 28
    • 42949162627 scopus 로고    scopus 로고
    • Peptide adsorption on a hydrophobic surface results from an interplay of solvation, surface, and intrapeptide forces
    • Horinek D, et al. (2008) Peptide adsorption on a hydrophobic surface results from an interplay of solvation, surface, and intrapeptide forces. Proc Natl Acad Sci USA 105(8):2842-2847.
    • (2008) Proc Natl Acad Sci USA , vol.105 , Issue.8 , pp. 2842-2847
    • Horinek, D.1
  • 29
    • 84859047273 scopus 로고    scopus 로고
    • The effect of temperature on single-polypeptide adsorption
    • Kienle S, Liese S, Schwierz N, Netz RR, Hugel T (2012) The effect of temperature on single-polypeptide adsorption. ChemPhysChem 13(4):982-989.
    • (2012) ChemPhysChem , vol.13 , Issue.4 , pp. 982-989
    • Kienle, S.1    Liese, S.2    Schwierz, N.3    Netz, R.R.4    Hugel, T.5
  • 30
    • 34249940831 scopus 로고    scopus 로고
    • Signatures of hydrophobic collapse in extended proteins captured with force spectroscopy
    • Walther KA, et al. (2007) Signatures of hydrophobic collapse in extended proteins captured with force spectroscopy. Proc Natl Acad Sci USA 104(19):7916-7921.
    • (2007) Proc Natl Acad Sci USA , vol.104 , Issue.19 , pp. 7916-7921
    • Walther, K.A.1
  • 31
    • 84865514087 scopus 로고    scopus 로고
    • Single molecule force spectroscopy reveals critical roles of hydrophobic core packing in determining the mechanical stability of protein GB1
    • Bu T, Wang HCE, Li H (2012) Single molecule force spectroscopy reveals critical roles of hydrophobic core packing in determining the mechanical stability of protein GB1. Langmuir 28(33):12319-12325.
    • (2012) Langmuir , vol.28 , Issue.33 , pp. 12319-12325
    • Bu, T.1    Wang, H.C.E.2    Li, H.3
  • 32
    • 36348998132 scopus 로고    scopus 로고
    • How do chemical denaturants affect the mechanical folding and unfolding of proteins?
    • Cao Y, Li H (2008) How do chemical denaturants affect the mechanical folding and unfolding of proteins? J Mol Biol 375(1):316-324.
    • (2008) J Mol Biol , vol.375 , Issue.1 , pp. 316-324
    • Cao, Y.1    Li, H.2
  • 33
    • 0034250769 scopus 로고    scopus 로고
    • Atomic force microscopic study of stretching a single polymer chain in a polymer brush
    • Yamamoto S, Tsujii Y, Fukuda T (2000) Atomic force microscopic study of stretching a single polymer chain in a polymer brush. Macromolecules 33(16):5995-5998.
    • (2000) Macromolecules , vol.33 , Issue.16 , pp. 5995-5998
    • Yamamoto, S.1    Tsujii, Y.2    Fukuda, T.3
  • 34
    • 34548172927 scopus 로고    scopus 로고
    • Force-induced globule-coil transition in single polystyrene chains in water
    • Gunari N, Balazs AC, Walker GC (2007) Force-induced globule-coil transition in single polystyrene chains in water. J Am Chem Soc 129(33):10046-10047.
    • (2007) J Am Chem Soc , vol.129 , Issue.33 , pp. 10046-10047
    • Gunari, N.1    Balazs, A.C.2    Walker, G.C.3
  • 35
    • 77952076441 scopus 로고    scopus 로고
    • Interfacial free energy governs single polystyrene chain collapse in water and aqueous solutions
    • Li ITS, Walker GC (2010) Interfacial free energy governs single polystyrene chain collapse in water and aqueous solutions. J Am Chem Soc 132(18):6530-6540.
    • (2010) J Am Chem Soc , vol.132 , Issue.18 , pp. 6530-6540
    • Li, I.T.S.1    Walker, G.C.2
  • 36
    • 80053634226 scopus 로고    scopus 로고
    • Signature of hydrophobic hydration in a single polymer
    • Li ITS, Walker GC (2011) Signature of hydrophobic hydration in a single polymer. Proc Natl Acad Sci USA 108(40):16527-16532.
    • (2011) Proc Natl Acad Sci USA , vol.108 , Issue.40 , pp. 16527-16532
    • Li, I.T.S.1    Walker, G.C.2
  • 37
    • 84880797580 scopus 로고    scopus 로고
    • When does trimethylamine N-oxide fold a polymer chain and urea unfold it?
    • Mondal J, Stirnemann G, Berne BJ (2013) When does trimethylamine N-oxide fold a polymer chain and urea unfold it? J Phys Chem B 117(29):8723-8732.
    • (2013) J Phys Chem B , vol.117 , Issue.29 , pp. 8723-8732
    • Mondal, J.1    Stirnemann, G.2    Berne, B.J.3
  • 38
    • 84903757486 scopus 로고    scopus 로고
    • Direct osmolyte-macromolecule interactions confer entropic stability to folded states
    • Rodríguez-Ropero F, Van Der Vegt NFA (2014) Direct osmolyte-macromolecule interactions confer entropic stability to folded states. J Phys Chem B 118(26):7327-7334.
    • (2014) J Phys Chem B , vol.118 , Issue.26 , pp. 7327-7334
    • Rodríguez-Ropero, F.1    Van Der Vegt, N.F.A.2
  • 39
    • 84863763684 scopus 로고    scopus 로고
    • Destruction of hydrogen bonds of poly (N-isopropylacrylamide) aqueous solution by trimethylamine N-oxide
    • Reddy PM, Taha M, Venkatesu P, Kumar A, Lee MJ (2012) Destruction of hydrogen bonds of poly (N-isopropylacrylamide) aqueous solution by trimethylamine N-oxide. J Chem Phys 136(23):234904.
    • (2012) J Chem Phys , vol.136 , Issue.23 , pp. 234904
    • Reddy, P.M.1    Taha, M.2    Venkatesu, P.3    Kumar, A.4    Lee, M.J.5
  • 40
    • 0026218825 scopus 로고
    • Stretching polymer brushes in poor solvents
    • Halperin A, Zhulina E (1991) Stretching polymer brushes in poor solvents. Macromolecules 24(19):5393-5397.
    • (1991) Macromolecules , vol.24 , Issue.19 , pp. 5393-5397
    • Halperin, A.1    Zhulina, E.2
  • 41
    • 51349115045 scopus 로고    scopus 로고
    • Dissecting entropic coiling and poor solvent effects in protein collapse
    • Gräter F, Heider P, Zangi R, Berne BJ (2008) Dissecting entropic coiling and poor solvent effects in protein collapse. J Am Chem Soc 130(35):11578-11579.
    • (2008) J Am Chem Soc , vol.130 , Issue.35 , pp. 11578-11579
    • Gräter, F.1    Heider, P.2    Zangi, R.3    Berne, B.J.4
  • 42
    • 84855833014 scopus 로고    scopus 로고
    • Conformational dynamics and internal friction in homopolymer globules: Equilibrium vs. Non-equilibrium simulations
    • Einert TR, Sing CE, Alexander-Katz A, Netz RR (2011) Conformational dynamics and internal friction in homopolymer globules: Equilibrium vs. non-equilibrium simulations. Eur Phys J E Soft Matter 34(12):1-16.
    • (2011) Eur Phys J E Soft Matter , vol.34 , Issue.12 , pp. 1-16
    • Einert, T.R.1    Sing, C.E.2    Alexander-Katz, A.3    Netz, R.R.4
  • 43
    • 84876266482 scopus 로고    scopus 로고
    • Collapse of a hydrophobic polymer in a mixture of denaturants
    • Das P, Xia Z, Zhou R (2013) Collapse of a hydrophobic polymer in a mixture of denaturants. Langmuir 29(15):4877-4882.
    • (2013) Langmuir , vol.29 , Issue.15 , pp. 4877-4882
    • Das, P.1    Xia, Z.2    Zhou, R.3
  • 44
    • 0020633006 scopus 로고
    • Dispersion and polar force components of surface tension of some polymer films
    • Saito M, Yabe A (1983) Dispersion and polar force components of surface tension of some polymer films. Text Res J 53(1):54-59.
    • (1983) Text Res J , vol.53 , Issue.1 , pp. 54-59
    • Saito, M.1    Yabe, A.2
  • 46
    • 84879392285 scopus 로고    scopus 로고
    • Expulsion of ions from hydrophobic hydration shells
    • Rankin BM, Ben-Amotz D (2013) Expulsion of ions from hydrophobic hydration shells. J Am Chem Soc 135(24):8818-8821.
    • (2013) J Am Chem Soc , vol.135 , Issue.24 , pp. 8818-8821
    • Rankin, B.M.1    Ben-Amotz, D.2
  • 47
    • 36449007442 scopus 로고
    • Calibration of atomic force microscope tips
    • Hutter JL, Bechhoefer J (1993) Calibration of atomic force microscope tips. Rev Sci Instrum 64(7):1868-1873.
    • (1993) Rev Sci Instrum , vol.64 , Issue.7 , pp. 1868-1873
    • Hutter, J.L.1    Bechhoefer, J.2
  • 48
    • 34249830163 scopus 로고    scopus 로고
    • Hofmeister salt effects on surface tension arise from partitioning of anions and cations between bulk water and the air-water interface
    • Pegram LM, Record MT, Jr (2007) Hofmeister salt effects on surface tension arise from partitioning of anions and cations between bulk water and the air-water interface. J Phys Chem B 111(19):5411-5417.
    • (2007) J Phys Chem B , vol.111 , Issue.19 , pp. 5411-5417
    • Pegram, L.M.1    Record, M.T.2
  • 49
    • 84865723813 scopus 로고    scopus 로고
    • 2 dihedral angles
    • 2 dihedral angles. J Chem Theory Comput 8(9):3257-3273.
    • (2012) J Chem Theory Comput , vol.8 , Issue.9 , pp. 3257-3273
    • Best, R.B.1
  • 50
    • 84859754499 scopus 로고    scopus 로고
    • Atomistic simulations of dilute polyelectrolyte solutions
    • Park S, Zhu X, Yethiraj A (2012) Atomistic simulations of dilute polyelectrolyte solutions. J Phys Chem B 116(14):4319-4327.
    • (2012) J Phys Chem B , vol.116 , Issue.14 , pp. 4319-4327
    • Park, S.1    Zhu, X.2    Yethiraj, A.3
  • 52
    • 0038717923 scopus 로고    scopus 로고
    • Binary phases of aliphatic N-oxides and water: Force field development and molecular dynamics simulation
    • Kast KM, Brickman J, Kast SM, Berry RS (2003) Binary phases of aliphatic N-oxides and water: Force field development and molecular dynamics simulation. J Phys Chem A 107(27):5342-5351.
    • (2003) J Phys Chem A , vol.107 , Issue.27 , pp. 5342-5351
    • Kast, K.M.1    Brickman, J.2    Kast, S.M.3    Berry, R.S.4
  • 53
    • 0029912748 scopus 로고    scopus 로고
    • Development and testing of the opls all-atom force field on conformational energetics and properties of organic liquids
    • Jorgensen WL, Maxwell DS, Tirado-Rives J (1996) Development and testing of the opls all-atom force field on conformational energetics and properties of organic liquids. J Am Chem Soc 118(45):11225-11236.
    • (1996) J Am Chem Soc , vol.118 , Issue.45 , pp. 11225-11236
    • Jorgensen, W.L.1    Maxwell, D.S.2    Tirado-Rives, J.3
  • 54
    • 78651349736 scopus 로고    scopus 로고
    • Coarse-graining polymers with the martini force-field: Polystyrene as a benchmark case
    • Rossi G, Monticelli L, Puisto SR, Vattulainen I, Ala-Nissila T (2011) Coarse-graining polymers with the martini force-field: Polystyrene as a benchmark case. Soft Matter 7(2):698-708.
    • (2011) Soft Matter , vol.7 , Issue.2 , pp. 698-708
    • Rossi, G.1    Monticelli, L.2    Puisto, S.R.3    Vattulainen, I.4    Ala-Nissila, T.5
  • 55
  • 56
    • 46249092554 scopus 로고    scopus 로고
    • Gromacs 4: Algorithms for highly efficient, load-balanced, and scalable molecular simulation
    • Hess B, Kutzner C, Van Der Spoel D, Lindahl E (2008) Gromacs 4: Algorithms for highly efficient, load-balanced, and scalable molecular simulation. J Chem Theory Comput 4(3):435-447.
    • (2008) J Chem Theory Comput , vol.4 , Issue.3 , pp. 435-447
    • Hess, B.1    Kutzner, C.2    Van Der Spoel, D.3    Lindahl, E.4
  • 57
    • 69349100797 scopus 로고    scopus 로고
    • PLUMED: A portable plugin for free-energy calculations with molecular dynamics
    • Bonomi M, Branduardi D, Bussi G, Camilloni C, Parrinello M (2009) PLUMED: A portable plugin for free-energy calculations with molecular dynamics. Comput Phys Commun 180(10):1961-1972.
    • (2009) Comput Phys Commun , vol.180 , Issue.10 , pp. 1961-1972
    • Bonomi, M.1    Branduardi, D.2    Bussi, G.3    Camilloni, C.4    Parrinello, M.5
  • 58
    • 84986519238 scopus 로고
    • The weighted histogram analysis method for free-energy calculations on biomolecules. I. The method
    • Kumar S, Bouzida D, Swendsen RH, Kollman PA, Rosenberg JM (1992) The weighted histogram analysis method for free-energy calculations on biomolecules. I. The method. J Comput Chem 13(8):1011-1021.
    • (1992) J Comput Chem , vol.13 , Issue.8 , pp. 1011-1021
    • Kumar, S.1    Bouzida, D.2    Swendsen, R.H.3    Kollman, P.A.4    Rosenberg, J.M.5
  • 60
    • 70349099268 scopus 로고    scopus 로고
    • Molecular computations of preferential interaction coefficients of proteins
    • Shukla D, Shinde C, Trout BL (2009) Molecular computations of preferential interaction coefficients of proteins. J Phys Chem B 113(37):12546-12554.
    • (2009) J Phys Chem B , vol.113 , Issue.37 , pp. 12546-12554
    • Shukla, D.1    Shinde, C.2    Trout, B.L.3
  • 61
    • 84868097108 scopus 로고    scopus 로고
    • Molecular mechanism for the preferential exclusion of TMAO from protein surfaces
    • Canchi DR, Jayasimha P, Rau DC, Makhatadze GI, Garcia AE (2012) Molecular mechanism for the preferential exclusion of TMAO from protein surfaces. J Phys Chem B 116(40):12095-12104.
    • (2012) J Phys Chem B , vol.116 , Issue.40 , pp. 12095-12104
    • Canchi, D.R.1    Jayasimha, P.2    Rau, D.C.3    Makhatadze, G.I.4    Garcia, A.E.5


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