Mark James E. (ed.). Physical Properties of Polymers Handbook

Подождите немного. Документ загружается.

TABLE 8.5. Temperature dependence of the partial molar heat capacities (J K

1

mol

1

) of the peptide unit and of the side chains

of amino acid residues for the temperature range 5–125 8C [18].

Temperature (8C)

5 25 50 75 100 125

–CHCONH– 3.7 15.2 26.2 29.8 33.7 33.7

--- R

Ala 175.7 166.7 156.2 144.7 134.6 124.1

Arg 204.6 273.4 305.8 315.1 318.7 318.5

Asn 72.9 88.8 109.8 125.2 140.5 154.2

Asp 72.8 89 106.2 124.5 140.7 154.3

Cys 225.4 237.6 250.8 260.7 268.2 276.1

Gln 168 180.2 193.4 203.3 210.8 218.7

Glu 168.3 179 192 203.7 211.4 217.8

Gly 82.3 78 71.7 66.4 59.7 53.9

His 205.7 179.6 177.2 179.6 187.1 196.8

Ile 406.8 402.3 397.1 390.8 386 380.8

Leu 385.9 381.7 377.8 372.9 369.4 365.5

Lys 215.1 249.8 266.9 274.4 278.1 274.4

Met 197.1 175.9 158.1 150.3 148.1 143.9

Phe 395.7 383 370.3 358.4 348.3 339.6

Pro 214.6 177.7 152.3 142.8 135.6 130.1

Ser 75.6 81.2 85.7 91.4 97.3 102.1

Thr 194.2 184.5 182.2 186.5 199 216.2

Trp 471.2 458.5 445.8 433.9 423.8 415.1

Tyr 310.6 301.7 295.2 294.5 300.1 304

Val 324.6 314.4 305 294.7 285.7 269.6

TABLE 8.6. Temperature dependence of the partial molar volumes (cm

mol

1

) of the peptide unit and of the side chains of

amino acid residues for the temperature range 5–125 8C [11].

Temperature (8C)

5 25 50 75 100 125

–CHCONH– 28.3 28.0 28.6 28.9 29.0 29.4

--- R

Ala 24.8 27.2 30.1 33.1 36.3 39.4

Arg 81.2 85.7 88.4 90.4 92.1 93.5

Asn 44.1 45.7 47.8 49.3 50.8 52.4

Asp 39.0 41.5 44.5 47.3 49.9 52.6

Cys 40.5 40.5 40.5 40.5 40.5 40.5

Gln 58.4 61.0 63.2 66.0 68.5 69.7

Glu 54.9 57.5 60.7 63.6 66.3 69.3

Gly 10.9 10.3 9.6 9.2 8.9 8.5

His 65.1 64.0 63.1 62.4 61.8 61.1

Ile 64.5 66.1 67.7 69.8 71.8 74.0

Leu 75.0 77.6 80.2 82.9 86.5 89.4

Lys 72.4 73.5 75.8 78.5 81.3 84.8

Met 73.3 72.1 70.2 69.0 67.9 66.7

Phe 82.0 86.3 92.0 97.9 102.6 107.9

Pro 36.0 35.8 34.1 33.7 33.5 33.2

Ser 27.1 27.8 28.8 29.7 30.7 32.0

Thr 44.2 44.7 45.9 47.6 50.9 54.6

Trp 110.9 110.9 110.9 110.9 110.9 110.9

Tyr 88.2 90.0 92.2 94.1 95.9 97.8

Val 60.7 63.0 65.7 68.5 71.7 74.5

THERMODYNAMIC PROPERTIES OF PROTEINS / 137

TABLE 8.7. Thermodynamics characteristics of the proteins (partial molar heat capacity of the native, C

(kJ K

1

mol

1

and unfolded state, C

(kJ K

1

mol

1

), and the heat capacity, D

(kJ K

1

mol

1

), enthalpy, D

H(kJ mol

1

), entropy,

S(J K

1

mol

1

), and Gibbs energy changes upon unfolding, D

G(kJ  mol

1

))*.

Protein

Temperature (8C)

5 25 50 75 100 125

ROP

7.9 9.0 10.4 11.7 13.1 14.4

11.9 12.9 13.9 14.2 14.5 14.6

7.9 7.9 7.0 5.0 2.9 0.4

H 107 265 451 580 601 700

SH3 domain

9.7 10.6 11.7 12.8 13.9 15.0

14.7 15.4 16 16.4 16.6 16.6

5.0 4.8 4.3 3.6 2.7 1.6

H  32 52 146 222 274 296

S  166 126 428 653 797 856

G 14.1 14.5 7.8  5.2  23.3  44.7

BPTI

8.7 9.5 10.5 11.4 12.4 13.4

11.5 12.5 13.1 13.5 13.7 13.7

2.8 3.0 2.6 2.1 1.3 0.3

H 72 130 200 259 303 323

S 87 288 514 690 809 864

G 47.8 44.2 34.0 18.9 1.2  20.9

CI2

12.4 13.3 14.5 15.6 16.7 17.8

15.8 16.9 17.8 18.0 18.2 18.0

3.4 3.6 3.3 2.4 1.5 0.2

H 66 135 221 292 341 362

S 119 360 636 850 986 1041

G 32.9 27.7 15.6  3.8  26.8  52.3

Eglin-c

11.9 12.9 14.1 15.4 16.6 17.9

16.1 16.8 17.6 17.9 18.2 18.1

4.2 3.9 3.5 2.5 1.6 0.2

H 33 115 208 283 335 358

S  22 262 561 786 929 989

G 39.1 36.9 26.8 9.5  11.5  35.6

Protein G

8.1 8.9 9.9 10.9 11.9 12.9

11.7 12.5 13.2 13.5 13.9 13.9

3.6 3.6 3.3 2.6 2.0 1.0

H  4 67 153 227 283 320

S  103 145 422 643 801 897

G 24.6 23.8 16.7 3.2  15.8  37.0

Tendamistat

11.4 12.1 13.0 13.9 14.8 15.7

14.9 15.7 16.6 16.8 17.1 17.1

3.5 3.6 3.6 2.9 2.3 1.4

H  22 70 176 262 321 351

S  213 109 452 711 877 955

G 37.2 37.5 30.0 14.6  6.1  29.1

138 / CHAPTER 8

TABLE 8.7. Continued.

Protein

Temperature (8C)

5 25 50 75 100 125

Ubiquitin

11.2 12.6 14.3 16.0 17.7 19.4

17.0 18.3 19.4 19.8 20.2 20.2

5.8 5.7 5.1 3.8 2.5 0.8

H  88 27 162 273 351 393

S  444  44 393 727 959 1068

G 35.4 40.1 35.1 20.0  6.7  32.1

RNase T1

14.6 16.1 17.8 19.7 21.9 24.3

20.1 21.4 22.8 24.0 24.9 25.1

5.5 5.3 5.0 4.3 3.0 0.8

H 173 281 410 528 621 672

S 444 817 1233 1584 1845 1976

G 49.6 37.5 11.7  23.2  67.2  114.4

Met-J

37.8 40.2 43.2 46.2 49.2 52.2

45.8 49.2 52.1 53.2 54.3 54.3

8.0 9.0 8.9 7.0 5.1 2.1

H 92 270 498 692 832 902

Cytochrome c

15.8 17.5 19.7 21.9 24.0 26.2

22.7 24.3 25.8 26.3 26.8 26.8

6.9 6.8 6.1 4.4 2.8 0.6

H  53 89 268 421 532 593

S  319 174 752 1210 1520 1681

G 35.7 37.1 25.1  1.1  35.0  76.0

Barnase

16.5 18.5 21.0 23.5 26.0 28.5

23.6 25.4 26.9 27.4 28.0 28.1

7.1 6.9 5.9 3.9 2.0 0.1

H 167 307 467 590 664 690

S 379 866 1384 1752 1959 2029

G 61.6 48.9 20.0  19.7  66.7  117.5

RNase A

19.5 20.8 22.5 24.2 25.8 27.5

24.1 26.0 27.8 28.5 29.3 29.5

4.6 5.2 5.3 4.3 3.5 2.0

H 220 294 405 512 603 664

S 641 896 1254 1574 1826 1989

G 41.8 27.0  0.0  35.8  78.1  127.6

Lysozyme

18.2 20.0 22.2 24.4 26.7 28.9

26.7 29.1 31.1 31.8 32.4 32.5

8.5 9.1 8.9 7.4 5.7 3.6

H 111 242 408 562 683 753

THERMODYNAMIC PROPERTIES OF PROTEINS / 139

TABLE 8.7. Continued.

Protein

Temperature (8C)

5 25 50 75 100 125

S 164 618 1153 1615 1954 2138

G 65.4 57.8 35.6  0.0  45.8  97.9

Interleukin 1b

26.4 28.1 30.1 32.2 34.3 36.4

33.3 35.6 37.6 38.4 39.2 39.2

6.9 7.5 7.5 6.2 4.9 2.8

H 7 151 330 501 640 736

S  99 401 1006 1516 1903 2155

G 34.5 31.5 5.1  26.6  69.8  121.7

Myoglobin

21.8 24.2 27.3 30.3 33.4 36.5

35.6 37.6 39.5 40.0 40.5 40.3

14.4 14.0 12.8 10.3 7.7 4.4

H  231 6 291 555 774 920

S  919  116 805 1595 2207 2588

G 24.5 40.6 31.0  0.1  49.2  110.0

T4-Lyz

25.2 28.1 31.8 35.5 39.1 42.8

36.2 39.1 41.5 42.2 43.1 43.0

11.0 11.0 9.7 6.7 4.0 0.2

H 20 240 499 671 805 856

S  190 576 1413 1928 2302 2439

G 72.8 68.4 42.6 0.1  53.6  114.7

Papain

28.1 32.0 36.8 41.7 46.5 51.4

45.0 48.0 50.5 51.3 52.1 51.9

16.9 16.0 13.7 9.6 5.6 0.5

H  166 164 535 826 1015 1091

S  911 236 1438 2312 2840 3042

Chymotrypsin

34.3 37.7 42.0 46.3 50.6 54.8

49.2 51.8 54.3 55.1 56.0 55.8

14.9 14.1 12.3 8.8 5.4 1.0

H  21 268 598 862 1039 1119

S  260 746 1813 2602 3099 3312

G 51.3 45.7 12.4  43.5  116.9  199.2

Pepsinogen

44.2 51.7 61.1 70.4 79.8 89.2

78.4 82.3 86.3 87.7 89.6 89.7

34.2 30.6 25.2 17.3 9.8 0.5

H  577 72 770 1301 1639 1767

S  2279  19 2242 3739 4687 5030

ROP[36];

SH3[37];

BPTI[5];

CI-2[38];

Eglin-c[39];

protein G[40];

Tendamistat[41];

Ubiquitin[42];

RNase T1[43];

Met-

J[44];

Cytochrome c, RNase A, Lysozyme, Myoglobin[45,46];

Barnase[47];

Interleukin-1b[48];

T4-Lyz[49];

Papain,

Chymotrypsin, Pepsinogen[50].

*Reported entropies and Gibbs energies are for the conditions of maximal stability [17]. The entropies and Gibbs energy of

unfolding for rop and met-J are not available since the unfolding represents a bimolecular two-state process.

140 / CHAPTER 8

TABLE 8.8. Normalized values of the heat capacities (D

hyd

in J K

1

mol

1

2

), enthalpies (D

hyd

in J mol

1

2

entropies (D

hyd

in 10

3

1

mol

1

2

), and Gibbs energies (D

hyd

in J K

1

mol

1

2

) of hydration of various surfaces [17].

Temperature (8C)

5 25 50 75 100 125

Nonpolar surfaces

Aliphatic D

hyd

2.24 2.14 2.03 1.91 1.80 1.66

hyd

 166  122  70  21 26 69

hyd

 730  578  409  263  134  22

hyd

37 50 62 71 75 77

Aromatic D

hyd

1.65 1.55 1.41 1.29 1.19 1.09

hyd

 180  148  111  77  46  18

hyd

 430  319  199  98  12 62

hyd

 61  53  47  43  42  43

Polar surfaces of:

Arg D

hyd

 0.38  0.20  0.12  0.04 0.01 0.08

hyd

 821  827  831  833  834  833

hyd

 458  478  492  497  498  495

hyd

 694  685  672  660  647  635

Asn D

hyd

 1.27  1.01  0.67  0.41  0.16 0.09

hyd

 871  894  915  928  936  936

hyd

 575  654  723  763  783  785

hyd

 711  699  681  663  643  623

Asp D

hyd

 1.72  1.40  1.07  0.71  0.40  0.11

hyd

 684  715  746  768  782  788

hyd

 360  469  569  636  675  691

hyd

 584  575  562  547  530  513

Cys D

hyd

1.80 2.01 2.23 2.42 2.54 2.70

hyd

 309  271  218  160  98  32

hyd

 535  402  232  59 113 283

hyd

 160  151  143  139  140  145

Gln D

hyd

 0.38  0.22  0.06 0.07 0.17 0.30

hyd

 697  703  706  706  703  697

hyd

 571  591  604  603  594  579

hyd

 538  527  511  497  481  467

Glu D

hyd

 0.71  0.55  0.35  0.17  0.05 0.09

hyd

 549  562  573  580  583  582

hyd

 392  436  473  492  500  498

hyd

 440  432  420  409  396  383

THERMODYNAMIC PROPERTIES OF PROTEINS / 141

TABLE 8.8. Continued.

Temperature (8C)

5 25 50 75 100 125

His D

hyd

 1.96  2.43  2.38  2.26  2.07  1.82

hyd

 1,084  1,128  1,188  1,247  1,301  1,349

hyd

 542  693  888  1060  1211  1337

hyd

 933  922  901  878  848  816

Lys D

hyd

 1.31  1.53  1.59  1.36  1.15  0.94

hyd

 685  714  753  789  821  847

hyd

 384  482  609  716  804  870

hyd

 578  570  556  540  519  498

Met D

hyd

 3.51  3.83  4.07  4.04  3.91  3.75

hyd

 399  473  572  672  774  869

hyd

 158  412  732  1031  1308  1555

hyd

 356  350  335  315  283  247

Ser D

hyd

 1.62  1.40  1.20  0.96  0.72  0.48

hyd

 1015  1045  1078  1104  1126  1140

hyd

 878  983  1089  1168  1227  1265

hyd

 771  752  726  698  667  636

Thr D

hyd

 1.09  1.29  1.22  0.89  0.29 0.55

hyd

 1262  1287  1318  1343  1359  1356

hyd

 971  1053  1156  1232  1274  1265

hyd

 992  972  944  916  881  850

Trp D

hyd

1.05 0.96 1.07 1.08 1.03 1.05

hyd

 1,181  1,161  1,135  1,110  1,084  1,055

hyd

 766  693  615  534  460  392

hyd

 968  954  936  924  912  899

Tyr D

hyd

 1.46  1.48  1.36  1.15  0.86  0.59

hyd

 824  854  889  921  946  963

hyd

 314  415  531  625  695  742

hyd

 735  730  717  703  686  667

CONH D

hyd

 2.08  1.81  1.56  1.53  1.49  1.55

hyd

 1662  1702  1745  1785  1823  1862

hyd

 890  1026  1162  1278  1383  1481

hyd

 1415  1396  1370  1340  1307  1272

142 / CHAPTER 8

REFERENCES

1. Zhang G, Lebedev BV, Wunderlich B, Zhang JY J. P.S.P. B-P. P.

1995; 33: 2449–2455.

2. Privalov PL, Khechinashvili NN J. Mol. Biol. 1974; 86: 665–684.

3. Privalov PL, Tiktopulo EI, Venyaminov SY, Griko YV, Makhatadze

GI, Khechinashvili NN. J. Mol. Biol. 1989; 205: 737.

4. Sturtevant JM. Ann. Rev. Phys. Chem. 1987; 38: 463–488.

5. Makhatadze GI, Kim KS, Woodward C, Privalov PL. Prot. Sci. 1993;

2: 2028.

6. Makhatadze GI. Heat capacities of amino acids, peptides and proteins.

Biophys. Chem. 1998; 71: 133–156.

7. Privalov PL, Makhatadze GI. J. Mol. Biol. 1990; 213: 385.

8. Privalov PL, Makhatadze GI. J. Mol. Biol. 1992; 224: 715–723.

9. Richardson JM, McMahon KW, MacDonald CC, Makhatadze GI.

Biochemistry 1999; 38: 12869–12875.

10. Richardson JM, Makhatadze GI. Temperature dependence of the

thermodynamics of helix-coil transition. J. Mol. Biol. 2004; 335:

1029–1037.

11. Makhatadze GI, Medvedkin VN, Privalov PL. Biopolymers 1990; 30:

1001–1010.

12. Durchschlag H. In: Hinz H-J, editor. ThermodynamicData for Biochem-

istry and Biotechnology. New York: Springer-Verlag; 1986. p 45–128.

13. Lee BK, Richards FM. J. Mol. Biol. 1971; 55: 379–400.

14. Miller S, Janin J, Lesk AM, Chothia C. J. Mol. Biol. 1987; 196:

641–656.

15. Wesson L, Eisenberg D. Protein Sci. 1992; 1: 227–235.

16. Oobatake M, Ooi T. Prog. Biophys. Mol. Biol. 1993; 59: 237–284.

17. Makhatadze GI, Privalov PL. Adv. Protein Chem. 1995; 47: 307.

18. Makhatadze GI, Privalov PL. J. Mol. Biol. 1990; 213: 375.

19. Izatt RM, Christensen JJ. In: Fasman GD, editor. The CRC Handbook

of Biochemistry and Molecular Biology, Physical and Chemical Data

Boca Raton, FL: CRC Press 1976. p 151–269.

20. Zamyatnin AA. Prog. Biophys. Mol. Biol. 1972; 24: 107–123.

21. Hutchens JO, Cole AG, Stout JW. J. Am. Chem. Soc. 1960; 82: 4813.

22. Cole AG, Hutchens JO, Stout JW. J. Phys. Chem. 1963; 67: 2245.

23. Hutchens JO, Cole AG, Robie RA, Stout JW. J. Biol. Chem. 1963; 238:

2407.

24. Hutchens JO, Cole AG, Stout JW. J. Biol. Chem. 1964; 239: 591.

25. Hutchens JO, Cole AG, Stout JW. J. Biol. Chem. 1969; 244: 33.

26. Hutchens JO, Cole AG, Stout JW. J. Phys. Chem. 1963; 67: 1128.

27. Cole AG, Hutchens JO, Stout JW. J. Phys. Chem. 1963; 67: 1852.

28. Hutchens JO, Cole AG, Stout JW. J. Biol. Chem. 1964; 239: 4194.

29. Roles KA, Wunderlich B. Biopolymers 1991; 31: 477.

30. Roles KA, Xenopoulos A, Wunderlich B. Biopolymers 1993; 33:

753.

31. Roles KA, Wunderlich B. J. Polym. Sci. Part B Polym. Phys. 1993; 31:

279.

32. Hutchens JO, Cole AG, Stout JW. J. Biol. Chem. 1969; 244: 26.

33. Mrevlishvili GM. In: Hinz H-J, editor Thermodynamic Data for

Biochemistry and Biotechnology. New York: Springer-Verlag; 1986

p 148.

34. Haly AR, Snaith JW. Biopolymers 1971;10:1681.

35. Haly AR, Snaith JW. Biopolymers 1968; 6:1355.

36. Steif C, Weber P, Hinz HJ, Flossdorf J, Cesareni G, Kikkinidis M,

Biochemistry 1993; 32: 3867–3876.

37. Viguera AR, Martinez JC, Filimonov VV, Mateo PL, Serrano L,

Biochemistry 1994; 33: 2142.

38. Jackson SE, Fersht AR, Biochemistry 1991; 30:10428–10435.

39. Bae SJ, Sturtevant JM, Biophys. Chem. 1995; 55: 247–252.

40. Alexander P, Fahnestock S, Lee T, Orban J, Bryan P, Biochemistry

1992; 31: 3597–3603.

41. Renner M, Hinz HJ, Scharf M, Engels JW, J. Mol. Biol. 1992; 223:769.

42. Wintrode PL, Makhatadze GI, Privalov PL, Proteins: Struct. Func.

Gen. 1994;18: 246.

43. Yu Y, Makhatadze GI, Pace N, Privalov PL, Biochemistry 1994; 33:

3312.

44. Johnson CM, Cooper A, Stockley PG, Biochemistry 1992; 31:

9717–9724.

45. Makhatadze GI, Privalov PL, J. Mol. Biol. 1993; 232: 639–659.

46. Privalov PL, Makhatadze GI, J. Mol. Biol. 1993; 232: 660–679.

47. Griko YV, Makhatadze GI, Privalov PL, Hartley RW, Protein Sci.

1994; 3: 669.

48. Makhatadze GI, Clore GM, Gronenborn AM, Privalov PL, Biochem-

istry 1994; 33: 9327.

49. Kitamura S, Sturtevant JM, Biochemistry 1989; 28: 3788–3792.

50. Privalov PL, Gill SJ, Adv. Protein Chem. 1988; 39:191–234.

THERMODYNAMIC PROPERTIES OF PROTEINS / 143

CHAPTER 9

Heat Capacities of Polymers

Jianye Wen

ALZA Corporation, 1900 Charleston Road, Mountain View, CA 94039

9.1 Introduction . . ............................................................. 145

References . . . ............................................................. 154

9.1 INTRODUCTION

The heat capacity of a substance can be defined as the

amount of heat required to change its temperature by one

degree. A more useful quantity is specific heat capacity,

which is the amount of heat required to change the tempera-

ture of one unit mass of a material by one degree. Heat

capacity is a fundamental property of any material. It is a

macroscopic parameter that can be linked to molecular

structure and vibrational motions at microscopic level [1].

Heat capacity under constant pressure (C

) is defined as

the heat quantity which is required to increase the tempera-

ture of the unit mass of a material by 1 K or 18C under

constant pressure. It is given by the following equation:

¼ DQ=mDT (unit: J=(g K) ), (9:1)

where DQ is the required heat quantity (in Joules), m is the

mass of the sample (in grams or kilograms), DT is the

temperature increase from T

to T

(in degrees Celsius or

Kelvins). The molar heat capacity under constant pressure is

defined as that heat quantity which is required to heat the

unit mole of a material through 1 K or 18C under constant

pressure (in J/(mol K)). The experimental heat capacities are

measured at constant pressure. However, in order to link

heat capacity with the vibrational spectrum, C

must first be

converted to the heat capacity at constant volume.

At constant volume, heat capacity can be defined as

follows;

¼ DQ=mDT (unit: J=(g K) ): (9:2)

The relationship between two heat capacities is

 C

¼ Va

T=K

(9:3)

where a is the thermal expansion coefficient and K

is the

isothermal bulk modulus.

Heat capacity is a fundamental property of any material.

It can be measured by adiabatic calorimetry (0–100 K),

differential scanning calorimetry (DSC) (above 100 K),

and some other techniques [2–4]. Theoretical interpretation

of heat capacity has been carried out by various researchers

through analysis based on the separation of the vibrational

spectrum into group and skeletal vibrations as well as

normal mode and their dispersion analysis [5–8]. The table

in this chapter contains the heat capacity data in the litera-

ture for selected polymers. The heat capacity for any

given polymer is a temperature-dependent quantity. Due

to the space limitations, the heat capacity values at selected

temperatures are listed in this table for the selected poly-

mers. Temperatures are chosen such that at least two

data points are included in both the glassy and rubbery

regions. A crude extrapolation could be used to compare

experimental data at other temperatures. The specific heat

increment at T

, DC

, is also given for the selected poly-

mers. Readers can find more detailed information about

from the original references. Since heat capacity also

depends on the state of the polymer, the state of the polymer

is specified by the following abbreviations whenever

possible:

a ¼ amorphous; c ¼ crystalline; s ¼ solid;

m ¼ melt; sc ¼ semicrystalline; g ¼ glassy:

The description of the theory of heat capacity and the

application of heat capacity measurements have been

given by Wunderlich and other researchers [2,3–17]. The

most comprehensive and updated heat capacity data are

collected in the ATHAS data bank (Advanced THermal

AnalysiS) which has been developed over the last 25 years

by Wunderlich (Chemistry Department, The University of

Tennessee), and coworkers.

145

TABLE 9.1. Heat capacities of selected polymers.

Polymer Abbreviations

Molecular

weight (g/mol) T

(K)

Temperature

(K) (kJ/(kg K)) (J/(mol K))

(J/(mol K)) Ref.

1. Main-chain carbon polymers

Poly(acrylics)

Poly(iso-butyl acrylate) PiBA 128.17 249 220 1.2156 155.80 36.60 [18]

240 1.3365 171.30

300 1.8108 232.09

500 2.3388 299.77

Poly(n-butyl acrylate) PnBA 128.17 218 80 0.5598 71.75 45.40 [18]

180 1.0632 136.27

300 1.8201 233.28

440 2.1803 279.45

Poly(ethyl acrylate) PEA 100.12 249 90 0.5792 57.99 45.60 [18]

200 1.0301 103.13

300 1.7867 178.88

500 2.2189 222.16

Poly(methyl acrylate) PMA 86.09 279 100 0.6154 52.98 42.30 [18]

200 0.9816 84.51

300 1.765 151.99

500 2.143 184.49

Poly(dienes)

1,4-Poly(butadiene) PBD 54.09

cis- 171 50 0.3694 19.98 29.10 [19,20]

150 0.8967 48.50

300 1.960 106.00

350 2.214 114.90

trans- 180 50 0.3465 18.74 28.20 [19,20]

150 0.9057 48.99

300 NA NA

500 2.616 141.50

Poly(1-butene) PB 56.11 249 100 0.6733 37.78 23.06 [19]

200 1.2190 68.40

300 2.086 117.02

600 3.071 172.31

Poly(1-butenylene) PBUT 55.10

cis- 171 30 0.2140 11.79 28.91 [3,19,20]

130 0.7775 42.838

300 1.924 106.03

450 2.409 132.73

trans- 190 30 0.1761 9.704 26.48 [3,19,20]

130 0.7898 43.516

300 1.924 106.03

450 2.409 132.73

Poly(alkenes)

Poly(ethylene) PE 14.03 252 100 0.674 9.45 (c) 10.1 [21]

200 1.110 15.57

300 1.555 21.81 (s)

2.202 30.89 (m)

600 3.127 43.87

Poly(1-hexene) PHE 84.16 223 100 0.7020 59.08 (a) 25.1 [19]

200 1.3319 112.09

250 1.903 160.18 (a)

290 2.079 174.98 (a)

146 / CHAPTER 9

TABLE 9.1. Continued.

Polymer Abbreviations

Molecular

weight (g/mol) T

(K)

Temperature

(K) (kJ/(kg K)) (J/(mol K))

(J/(mol K)) Ref.

Poly(isobutene) PiB 56.11 200 50 0.2440 13.69 (a) 22.29 [19]

150 0.8660 48.59

300 1.962 110.09 (a)

380 2.311 129.66

Poly(2-methylbutadiene) PMBD 68.12

cis- 200 50 0.3573 24.34 30.87 (a) [19]

150 0.9025 61.48

300 1.911 130.20

360 2.216 144.80

Poly(4-methyl-1-pentene) P4MPE 84.16 303 80 0.5610 47.21 33.7 (a) [19]

180 1.090 91.75

250 1.4449 121.60

300 1.728 145.40

Poly(1-pentene) PPE 70.14 233 200 1.253 87.90 27.03 (a) [19]

220 1.338 93.82

300 2.058 144.34

470 2.770 194.32

Poly(propylene) PP 42.08 260 100 0.6238 26.25 (c) 17.37 [22]

200 1.132 47.63 (c)

300 1.622 68.24 (s)

2.099 88.34 (m)

600 3.178 133.73 (a)

Poly(methacrylics)

Poly(n-butyl methacrylate) PnBMA 142.20 293 80 0.5472 77.81 29.70 [18]

200 1.1557 164.34

300 1.8524 263.41

450 2.3673 336.63

Poly(i-butyl methacrylate) PiBMA 142.20 326 230 1.2229 173.90 39.00 [18]

300 1.5710 223.40

350 2.0190 287.10

400 2.1127 300.43

Poly(ethyl methacrylate) PEMA 114.15 338 80 0.5155 58.84 31.70 [18]

300 1.4666 167.42

350 1.9489 222.47

380 2.0462 233.57

Poly(hexyl methacrylate) PHMA 170.25 268 270 1.8264 310.77 — [18]

300 1.9091 324.83

420 2.2396 381.06

Poly(methacrylic acid) PMAA 86.09 — 100 0.5248 45.18 — [18]

200 0.9456 81.41

300 1.307 112.50

Poly(methacrylamide) PMAM 85.11 — 100 0.5904 50.25 — [18]

200 1.032 87.81

300 1.395 118.70

Poly(methyl methacrylate) PMMA 100.12 378 100 0.5742 57.49 33.5 [18]

300 1.3755 137.72

400 2.0766 207.91

550 2.4323 243.52

Poly(styrenes)

Poly(styrene) PS 104.15 373 100 0.4548 47.37 (g) 30.7 (a) [23]

300 1.2230 127.38

1.2730 132.58 [4]

HEAT CAPACITIES OF POLYMERS / 147