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97. Gautieri A, Uzel S, Vesentini S, Redaelli A, Buehler MJ (2009) Molecular and mesoscale
mechanisms of osteogenesis imperfecta disease in collagen fibrils. Biophys J 97(3):857–865
98. Raman SS, Parthasarathi R, Subramanian V, Ramasami T (2008) Role of length-dependent
stability of collagen-like peptides. J Phys Chem B 112(5):1533–1539
99. Raman SS, Parthasarathi R, Subramanian V, Ramasami T (2006) Role of aspartic acid
in collagen structure and stability: a molecular dynamics investigation. J Phys Chem B
110(41):20678–20685
100. Punitha V, Raman SS, Parthasarathi R, Subramanian V, Rao JR, Nair BU, Ramasami T (2009)
Molecular dynamics investigations on the effect of D amino acid substitution in a triple-helix
structure and the stability of collagen. J Phys Chem B 113(26):8983–8992
101. Tang M, Gandhi NS, Burrage K, Gu Y (2019) Interaction of gold nanosurfaces/nanoparticles
with collagen-like peptides. Phys Chem Chem Phys 21(7):3701–3711
102. Gopalakrishnan R, Singam EA, Sundar JV, Subramanian V (2015) Interaction of collagen
like peptides with gold nanosurfaces: a molecular dynamics investigation. Phys Chem Chem
Phys 17(7):5172–5186
103. Buehler MJ (2006) Atomistic and continuum modeling of mechanical properties of collagen:
elasticity, fracture, and self-assembly. J Mater Res 21(8):1947–1961
104. Buehler MJ (2006) Nature designs tough collagen: explaining the nanostructure of collagen
fibrils. Proc Natl Acad Sci 103(33):12285–12290
105. Gautieri A, Russo A, Vesentini S, Redaelli A, Buehler MJ (2010) Coarse-grained model
of collagen molecules using an extended MARTINI force field. J Chem Theory Comput
6(4):1210–1218
106. Condon JE, Jayaraman A (2018) Development of a coarse-grained model of collagen-like
peptide (CLP) for studies of CLP triple helix melting. J Phys Chem B 122(6):1929–1939
107. Walker KT, Nan R, Wright DW, Gor J, Bishop AC, Makhatadze GI, Brodsky B, Perkins SJ
(2017) Non-linearity of the collagen triple helix in solution and implications for collagen
function. Biochem J BCJ20170217
108. Berisio R, Vitagliano L, Mazzarella L, Zagari A (2000) Crystal structure of a collagenlike polypeptide with repeating sequence Pro–Hyp–Gly at 1.4 Å resolution: implications for
collagen hydration. Biopolymers 56(1):8–13
109. Paul DR (2012) Polymer blends, vol 1. Elsevier, Amsterdam
110. Coleman MM, Painter PC, Graf JF (1985) Specific interactions and the miscibility of polymer
blends, 1st edn. CRC Press, Boca Raton
111. Crosby AJ, Lee JY (2007) Polymer nanocomposites: the “nano” effect on mechanical
properties. Polym Rev 47(2):217–229
112. Krishnamoorti R, Vaia RA (2007) Polymer nanocomposites. J Polym Sci Part B Polym Phys
45(24):3252–3256
113. Kumar SK, Krishnamoorti R (2010) Nanocomposites: structure, phase behavior, and
properties. Ann Rev Chem Biomol Eng 1:37–58
114. Hall LM, Jayaraman A, Schweizer KS (2010) Molecular theories of polymer nanocomposites.
Curr Opin Solid State Mater Sci 14(2):38–48
115. Chevigny C, Dalmas F, Di Cola E, Gigmes D, Bertin D, Boué FO, Jestin J (2010)
Polymer-grafted-nanoparticles nanocomposites: dispersion, grafted chain conformation, and
rheological behavior. Macromolecules 44(1):122–133
116. Kumar SK, Jouault N, Benicewicz B, Neely T (2013) Nanocomposites with polymer grafted
nanoparticles. Macromolecules 46(9):3199–3214
117. Koning C, Van Duin M, Pagnoulle C, Jerome R (1998) Strategies for compatibilization of
polymer blends. Prog Polym Sci 23(4):707–757
118. Coleman MM, Serman CJ, Bhagwagar DE, Painter PC (1990) A practical guide to polymer
miscibility. Polymer 31(7):1187–1203
119. Gelles R, Frank CW (1983) Effect of molecular weight on polymer blend phase separation
kinetics. Macromolecules 16(9):1448–1456
120. Hariharan A, Kumar SK, Russell TP (1993) Free surfaces of polymer blends. II. Effects of
molecular weight and applications to asymmetric polymer blends. J Chem Phys 99(5):4041–
4050
A. Jayaraman et al.
97. Gautieri A, Uzel S, Vesentini S, Redaelli A, Buehler MJ (2009) Molecular and mesoscale
mechanisms of osteogenesis imperfecta disease in collagen fibrils. Biophys J 97(3):857–865
98. Raman SS, Parthasarathi R, Subramanian V, Ramasami T (2008) Role of length-dependent
stability of collagen-like peptides. J Phys Chem B 112(5):1533–1539
99. Raman SS, Parthasarathi R, Subramanian V, Ramasami T (2006) Role of aspartic acid
in collagen structure and stability: a molecular dynamics investigation. J Phys Chem B
110(41):20678–20685
100. Punitha V, Raman SS, Parthasarathi R, Subramanian V, Rao JR, Nair BU, Ramasami T (2009)
Molecular dynamics investigations on the effect of D amino acid substitution in a triple-helix
structure and the stability of collagen. J Phys Chem B 113(26):8983–8992
101. Tang M, Gandhi NS, Burrage K, Gu Y (2019) Interaction of gold nanosurfaces/nanoparticles
with collagen-like peptides. Phys Chem Chem Phys 21(7):3701–3711
102. Gopalakrishnan R, Singam EA, Sundar JV, Subramanian V (2015) Interaction of collagen
like peptides with gold nanosurfaces: a molecular dynamics investigation. Phys Chem Chem
Phys 17(7):5172–5186
103. Buehler MJ (2006) Atomistic and continuum modeling of mechanical properties of collagen:
elasticity, fracture, and self-assembly. J Mater Res 21(8):1947–1961
104. Buehler MJ (2006) Nature designs tough collagen: explaining the nanostructure of collagen
fibrils. Proc Natl Acad Sci 103(33):12285–12290
105. Gautieri A, Russo A, Vesentini S, Redaelli A, Buehler MJ (2010) Coarse-grained model
of collagen molecules using an extended MARTINI force field. J Chem Theory Comput
6(4):1210–1218
106. Condon JE, Jayaraman A (2018) Development of a coarse-grained model of collagen-like
peptide (CLP) for studies of CLP triple helix melting. J Phys Chem B 122(6):1929–1939
107. Walker KT, Nan R, Wright DW, Gor J, Bishop AC, Makhatadze GI, Brodsky B, Perkins SJ
(2017) Non-linearity of the collagen triple helix in solution and implications for collagen
function. Biochem J BCJ20170217
108. Berisio R, Vitagliano L, Mazzarella L, Zagari A (2000) Crystal structure of a collagenlike polypeptide with repeating sequence Pro–Hyp–Gly at 1.4 Å resolution: implications for
collagen hydration. Biopolymers 56(1):8–13
109. Paul DR (2012) Polymer blends, vol 1. Elsevier, Amsterdam
110. Coleman MM, Painter PC, Graf JF (1985) Specific interactions and the miscibility of polymer
blends, 1st edn. CRC Press, Boca Raton
111. Crosby AJ, Lee JY (2007) Polymer nanocomposites: the “nano” effect on mechanical
properties. Polym Rev 47(2):217–229
112. Krishnamoorti R, Vaia RA (2007) Polymer nanocomposites. J Polym Sci Part B Polym Phys
45(24):3252–3256
113. Kumar SK, Krishnamoorti R (2010) Nanocomposites: structure, phase behavior, and
properties. Ann Rev Chem Biomol Eng 1:37–58
114. Hall LM, Jayaraman A, Schweizer KS (2010) Molecular theories of polymer nanocomposites.
Curr Opin Solid State Mater Sci 14(2):38–48
115. Chevigny C, Dalmas F, Di Cola E, Gigmes D, Bertin D, Boué FO, Jestin J (2010)
Polymer-grafted-nanoparticles nanocomposites: dispersion, grafted chain conformation, and
rheological behavior. Macromolecules 44(1):122–133
116. Kumar SK, Jouault N, Benicewicz B, Neely T (2013) Nanocomposites with polymer grafted
nanoparticles. Macromolecules 46(9):3199–3214
117. Koning C, Van Duin M, Pagnoulle C, Jerome R (1998) Strategies for compatibilization of
polymer blends. Prog Polym Sci 23(4):707–757
118. Coleman MM, Serman CJ, Bhagwagar DE, Painter PC (1990) A practical guide to polymer
miscibility. Polymer 31(7):1187–1203
119. Gelles R, Frank CW (1983) Effect of molecular weight on polymer blend phase separation
kinetics. Macromolecules 16(9):1448–1456
120. Hariharan A, Kumar SK, Russell TP (1993) Free surfaces of polymer blends. II. Effects of
molecular weight and applications to asymmetric polymer blends. J Chem Phys 99(5):4041–
4050