Nuclear magnetic resonance characterization of peptide models of collagen-folding diseases

Philosophical Transactions of the Royal Society B: Biological Sciences

Volumn 356, Issue 1406, 2001, Pages 159-168

  Buevich, A ^a   Baum, J ^a   Lindquist, S ^a   Kelly, J W ^a   Byers, P H ^a   Seckler, R ^a   Helenius, A ^a  

^a RUTGERS UNIVERSITY   (United States)

Author keywords

Collagen; Dynamics; Nuclear magnetic resonance; Osteogenesis imperfecta; Peptides; Triple helix

Indexed keywords

EID: 0035961347     PISSN: 09628436     EISSN: None     Source Type: Journal    
DOI: 10.1098/rstb.2000.0761     Document Type: Conference Paper

References (47)

1. Sequence dependence of the folding of collagen-like peptides - Single amino acids affect the rate of triple-helix nucleation
2. The influence of peptidyl-prolyl cis-trans isomerase on the in vitro folding of type III collagen
3. The role of cis-trans isomerization of peptide bonds in the coil triple helix conversion of collagen
4. Folding mechanism of the triple helix in type-III collagen and type-II pN-collagen. Role of disulfide bridges and peptide bond isomerization
5. Real-time NMR investigations of triple helix folding and collagen folding diseases
6. Folding of peptide models of collagen and misfolding in disease
7. Destabilization of osteogenesis imperfecta collagen-like model peptides correlates with the identity of the residue replacing glycine
8. Crystal and molecular structure of a collagen-like peptide at 1.9 Å resolution
9. Subtle structural alterations in the chains of type I procollagen produce osteogenesis imperfecta type II
10. Conformational energy estimates for statistically coiling polypeptide chains
11. The collagen triple-helix structure
12. The triple-helix motif in proteins
13. Conformationally distinct domains in the amino-terminal segment of type III procollagen and its rapid helix-coil transition
14. Site-specific NMR monitoring of cis-trans isomerization in the folding of the proline-rich collagen triple helix
15. The C-propeptide domain of procollagen can be replaced with a transmembrane domain without affecting trimer formation or collagen triple helix folding during biosynthesis
16. Osteogenesis imperfecta
17. From Levinthal to pathways to funnels
18. Kinetics studies of protein folding using NMR spectroscopy
19. Protein folding: A perspective from theory and experiment
20. Insight into protein folding from NMR
21. Equilibrium NMR studies of unfolded and partially folded proteins
22. Folding and unfolding of collagen triple helices
23. The zipper-like folding of collagen triple-helices and the effects of mutations that disrupt the zipper
24. Perspectives on synthesis and applications of triple-helical collagen model peptides
25. Collagen mimetics
26. Formation and stabilization of the collagen-fold
27. Substrate specificities of the peptidyl prolyl cis-trans isomerase activities of cyclophilin and FK-506 binding protein: Evidence for the existence of a family of distinct enzymes
28. Transthyretin quaternary and tertiary structural changes facilitate misassembly into amyloid
29. Connective tissue and its hereditable disorders, molecular, genetic and medical aspects
30. Mutations in fibrillar collagens (types I, II, II, and IX), fibril-associated collagen (type IX), and network-forming collagen (type X) cause a spectrum of diseases of bone, cartilage, and blood vessels
31. Structural neurology: Are seeds at the root of neuronal degeneration?
32. Direct NMR measurement of the folding kinetics of a trimeric peptide
33. NMR shows asymmetric loss of triple helix in peptides modeling a collagen mutation in brittle bone disease
34. Nuclear magnetic resonance and circular dichroism studies of a triple-helical peptide with a glycine substitution
35. Characterization of collagen-like peptides containing interruptions in the repeating Gly-X-Y sequence
36. Molecular recognition in procollagen chain assembly
37. Pathways of protein folding
38. NMR and X-ray studies of collagen model peptides
39. Stability and mobility of the collagen structure
40. Collagens: Molecular biology, diseases, and potentials for therapy
41. Delayed triple helix formation of mutant collagen from patients with osteogenesis imperfecta
42. The molecular structure of collagen
43. Methods for exploring early events in protein folding
44. Conformational energies and configurational statistics of copolypeptides containing L-proline
45. Amino acid sequence environment modulates the disruption by osteogenesis imperfecta glycine substitutions in collagen-like peptides