Equilibrium thermal transitions of collagen model peptides

Protein Science

Volumn 13, Issue 4, 2004, Pages 893-902

  Persikov, Anton V ^a   Xu, Yujia ^a,b   Brodsky, Barbara ^a  

^a RUTGERS ROBERT WOOD JOHNSON MEDICAL SCHOOL   (United States)

^b CITY UNIVERSITY OF NEW YORK   (United States)

Author keywords

Collagen; Equilibrium; Peptide; Relaxation; Thermodynamics; Triple helix; Two state model

Indexed keywords

COLLAGEN; MONOMER; PEPTIDE DERIVATIVE;

ARTICLE; CONCENTRATION (PARAMETERS); ISOMERIZATION; KINETICS; MODEL; PHASE TRANSITION; PRIORITY JOURNAL; PROTEIN FOLDING; PROTEIN FUNCTION; PROTEIN STRUCTURE; PROTEIN SYNTHESIS; STRUCTURE ANALYSIS; TEMPERATURE DEPENDENCE; THERMAL ANALYSIS; THERMODYNAMICS; TRIPLE HELIX;

CALORIMETRY, DIFFERENTIAL SCANNING; CIRCULAR DICHROISM; COLLAGEN; HEAT; KINETICS; MODELS, CHEMICAL; PEPTIDES; PROTEIN DENATURATION; PROTEIN FOLDING; THERMODYNAMICS;

EID: 1842559515     PISSN: 09618368     EISSN: None     Source Type: Journal    
DOI: 10.1110/ps.03501704     Document Type: Article

References (43)

1. Anfinsen, C.B. 1973. Principles that govern the folding of protein chains. Science 181: 223-230.
2. Bächinger, H.P. and Engel, J. 2001. Thermodynamic vs. kinetic stability of collagen triple helices. Matrix Biol. 20: 267-269.
3. Bächinger, H.P., Bruckner, P., Timpl, R., and Engel, J. 1978. The role of cis-trans isomerization of peptide bonds in the coil leads to and comes from triple helix conversion of collagen. Eur. J. Biochem. 90: 605-613.
4. Bächinger, H.P., Bruckner, P., Timpl, R., Prockop, D.J., and Engel, J. 1980. Folding mechanism of the triple helix in type-III collagen and type-III pN-collagen. Role of disulfide bridges and peptide bond isomerization. Eur. J. Biochem. 106: 619-632.
5. Baum, J. and Brodsky, B. 1999. Folding of peptide models of collagen and misfolding in disease. Curr. Opin. Struct. Biol. 9: 122-128.
6. Beck, K. and Brodsky, B. 1998. Supercoiled protein motifs: The collagen triple-helix and the α-helical coiled coil. J. Struct. Biol. 122: 17-29.
7. Buevich, A.V., Dai, Q.H., Liu, X., Brodsky, B., and Baum, J. 2000. Site-specific NMR monitoring of cis-trans isomerization in the folding of the proline-rich collagen triple helix. Biochemistry 39: 4299-4308.
8. 10 does not. J. Am. Chem. Soc. 125: 9922-9923.
9. Dragan, A.I. and Privalov, P.L. 2002. Unfolding of a leucine zipper is not a simple two-state transition. J. Mol. Biol. 321: 891-908.
10. Dürr, E. and Bosshard, H.R. 2000. Folding of a three-stranded coiled coil. Protein Sci. 9: 1410-1415.
11. Engel, J. and Bächinger, H.P. 2000. Cooperative equilibrium transitions coupled with a slow annealing step explain the sharpness and hysteresis of collagen folding. Matrix Biol. 19: 235-244.
12. Engel, J. and Prockop, D.J. 1991. The zipper-like folding of collagen triple helices and the effects of mutations that disrupt the zipper. Annu. Rev. Biophys. Biophys. Chem. 20: 137-152.
13. n. Biopolymers 16: 601-622.
14. Feng, Y., Melacini, G., and Goodman, M. 1997. Collagen-based structures containing the peptoid residue N-isobutylglycine (Nleu): Synthesis and biophysical studies of Gly-Nleu-Pro sequences by circular dichroism and optical rotation. Biochemistry 36: 8716-8724.
15. Goodman, M., Bhumralkar, M., Jefferson, E.A., Kwak, J., and Locardi, E. 1998. Collagen mimetics. Biopolymers 47: 127-142.
16. Hodges, J.A. and Raines, R.T. 2003. Stereoelectronic effects on collagen stability: The dichotomy of 4-fluoroproline diastereomers. J. Am. Chem. Soc. 125: 9262-9263.
17. Jaenicke, R. and Lilie, H. 2000. Folding and association of oligomeric and multimeric proteins. Adv. Protein Chem. 53: 329-401.
18. Jenkins, C.L. and Raines, R.T. 2002. Insights on the conformational stability of collagen. Nat. Prod. Rep. 19: 49-59.
19. Kadler, K.E., Hojima, Y., and Prockop, D.J. 1988. Assembly of type I collagen fibrils de novo. Between 37 and 41 degrees C the process is limited by micro-unfolding of monomers. J. Biol. Chem. 263: 10517-10523.
20. Kielty, C.M. and Grant, M.E. 2002. The collagen family: Structure, assembly, and organization in the extracellular matrix. In Connective tissue and its heritable disorders (eds. P.M. Royce and B. Steinmann), pp. 159-222. Wiley, New York.
21. Leikina, E., Mertts, M.V., Kuznetsova, N., and Leikin, S. 2002. Type I collagen is thermally unstable at body temperature. Proc. Natl. Acad. Sci. 99: 1314-1318.
22. 10 and a designed collagen triple-helical peptide. Biochemistry 32: 7377-7387.
23. Liu, X., Kim, S., Dai, Q.H., Brodsky, B., and Baum, J. 1998. Nuclear magnetic resonance shows asymmetric loss of triple helix in peptides modeling a collagen mutation in brittle bone disease. Biochemistry 37: 15528-15533.
24. Malkar, N.B., Lauer-Fields, J.L., Borgia, J.A., and Fields, G.B. 2002. Modulation of triple-helical stability and subsequent melanoma cellular responses by single-site substitution of fluoroproline derivatives. Biochemistry 41: 6054-6064.
25. McLaughlin, S.H. and Bulleid, N.J. 1998. Molecular recognition in procollagen chain assembly. Matrix Biol. 16: 369-377.
26. Miles, CA, 1993. Kinetics of collagen denaturation in mammalian lens capsules studied by differential scanning calorimetry. Int. J. Biol. Macromol. 15: 265-271.
27. Miles, C.A., Burjanadze, T.V., and Bailey A.J. 1995. The kinetics of the thermal denaturation of collagen in unrestrained rat tail tendon determined by differential scanning calorimetry. J. Mol. Biol. 245: 437-446.
28. Persikov, A.V. and Brodsky, B. 2002. Unstable molecules form stable tissues. Proc. Natl. Acad. Sci. 99: 1101-1103.
29. Persikov, A.V., Ramshaw, J.A.M., Kirkpatrick, A., and Brodsky, B. 2000. Amino acid propensities for the collagen triple-helix. Biochemistry 39: 14960-14967.
30. Persikov, A.V., Ramshaw, J.A.M., Kirkpatrick, A., and Brodsky, B. 2002. Peptide investigations of pairwise interactions in the collagen triple-helix. J. Mol. Biol. 316: 385-394.
31. -. 2003. Triple-helix propensity of hydroxyproline and fluoroproline: Comparison of host-guest and repeating tripeptide collagen models. J. Am. Chem. Soc. 125: 11500-11501.
32. Piez, K.A. and Sherman, M.R. 1970. Equilibrium and kinetic studies of the helix-coil transition in a I-CB2, a small peptide from collagen. Biochemistry 9: 4134-4140.
33. Potekhin, S.A. and Kovrigin, E.L. 1998. Folding under inequilibrium conditions as a possible reason for partial irreversibility of heat-denatured proteins: Computer simulation study. Biophys. Chem. 73: 241-248.
34. Privalov, P.L. 1982. Stability of proteins. Proteins which do not present a single cooperative system. Adv. Protein Chem. 35: 1-104.
35. Rigby, B.J. 1971. The thermal stability of collagen: Its significance in biology and physiology. Adv. Chem. Phys. 21: 537-555.
36. Ryhanen, L., Zaragoza, E.J., and Uitto, J. 1983. Conformational stability of type I collagen triple helix: Evidence for temporary and local relaxation of the protein conformation using a proteolytic probe. Arch. Biochem. Biophys. 223: 562-571.
37. Sanchez-Ruiz, J.M. 1992. Theoretical analysis of Lumry-Eyring models in differential scanning calorimetry. Biophys. J. 61: 921-935.
38. -. 1995. Differential Scanning Calorimetry of proteins. In Subcellular biochemistry, Vol 24. Proteins: Structure, Function, and Engineering (eds. B.B. Biswas and S. Roy), pp. 133-176. Plenum Press, New York.
39. Saygin, O., Heidemann, E., and Klump, H. 1978. The triple helix-coil transition of cyanogen-bromide peptides of the α1-chain of the calf-skin collagen. Biopolymers 17: 511-522.
40. Shah, N.K., Sharma, M., Kirkpatrick, A., Ramshaw, J.A.M., and Brodsky, B. 1997. Gly-Gly-containing triplets of low stability adjacent to a type III collagen epitope. Biochemistry 36: 5878-5883.
41. Weidner, H. 1975. Relaxation kinetics of the triple-stranded helix-coil transition at short chain length. A model including the staggering of chains. Biopolymers 14: 763-780.
42. Weidner, H., Engel, J., and Fietzek, P.P. 1974. Mechanism of the triple helix-Coil transition of short peptides with collagen-like sequence. In Peptides, polypeptides, andproteins (eds. E.R. Blout et al.), pp. 419-435. Wiley, New York.
43. Xu, Y., Hyde, T., Wang, X., Bhate, M., Brodsky, B., and Baurn, J. 2003. NMR and CD spectroscopy show that imino acid restriction of the unfolded state leads to efficient folding. Biochemistry 42: 8696-8703.