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Rational Design of Protein Stability: Effect of (2S,4R)-4-Fluoroproline on the Stability and Folding Pathway of Ubiquitin

By Maria D. Crespo and Marina Rubini
Topics: Research Article
Publisher: Public Library of Science
OAI identifier: oai:pubmedcentral.nih.gov:3095602
Provided by: PubMed Central

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  1. (2004). A (4R)- or a (4S)-fluoroproline residue in position Xaa of the (Xaa-Yaa-Gly) collagen repeat severely affects triple-helix formation.
  2. (1999). A hyperstable collagen mimic.
  3. (2005). A stereoelectronic effect on turn formation due to proline substitution in elastin-mimetic polypeptides.
  4. (1998). Anion binding to the ubiquitin molecule.
  5. (2009). Biosynthesis and stability of coiled-coil peptides containing (2S,4R)-5,5,5-trifluoroleucine and (2S,4S)-5,5,5-trifluoroleucine.
  6. (2003). Characterization of collagen model peptides containing 4-fluoroproline; (4(S)-fluoroproline-pro-gly)10 forms a triple helix, but (4(R)-fluoroproline-pro-gly)10 does not.
  7. (2005). Cistrans isomerization at a proline opens the pore of a neurotransmitter-gated ion channel.
  8. (1998). Code for collagen’s stability deciphered.
  9. (2002). Collagen stability: insights from NMR spectroscopic and hybrid density functional computational investigations of the effect of electronegative substituents on prolyl ring conformations.
  10. (2009). Collagen structure and stability.
  11. (2001). Conformational stability of collagen relies on a stereoelectronic effect.
  12. (2004). Context-dependent effects of proline residues on the stability and folding pathway of ubiquitin.
  13. (2004). Cotranslational incorporation of a structurally diverse series of proline analogues in an Escherichia coli expression system.
  14. (2005). Different effects of 4-hydroxyproline and 4-fluoroproline on the stability of collagen triple helix.
  15. (1992). Early hydrogen-bonding events in the folding reaction of ubiquitin.
  16. (2003). Effect of 3-hydroxyproline residues on collagen stability.
  17. (1996). Evidence for a three-state model of protein folding from kinetic analysis of ubiquitin variants with altered core residues.
  18. (2003). Evidence for sequential barriers and obligatory intermediates in apparent two-state protein folding.
  19. (2001). Fluorinated Coiled-Coil Proteins Prepared In Vivo Display Enhanced Thermal and Chemical Stability.
  20. (2006). Fluoroproline flip-flop: regiochemical reversal of a stereoelectronic effect on peptide and protein structures.
  21. (2001). Fluoroprolines as Tools for Protein Design and Engineering Angew Chem.
  22. (1993). Folding and stability of a tryptophan-containing mutant of ubiquitin.
  23. (2003). Incorporation of trifluoroisoleucine into proteins in vivo.
  24. (2002). Insights on the conformational stability of collagen.
  25. (2004). Is an intermediate state populated on the folding pathway of ubiquitin?
  26. (1975). Isolation of a polypeptide that has lymphocyte-differentiating properties and is probably represented universally in living cells.
  27. Michnick SW (2007) Multiple tryptophan probes reveal that ubiquitin folds via a late misfolded intermediate.
  28. (2009). Modulating collagen triple-helix stability with 4-chloro, 4-fluoro, and 4-methylprolines.
  29. (2006). Modulating protein structure with fluorous amino acids: increased stability and native-like structure conferred on a 4-helix bundle protein by hexafluoroleucine.
  30. (2005). Peptidyl prolyl cis/trans-isomerases: comparative reactivities of cyclophilins, FK506-binding proteins, and parvulins with fluorinated oligopeptide and protein substrates.
  31. (2006). Population of on-pathway intermediates in the folding of ubiquitin.
  32. (2005). Protein folding handbook.
  33. (1993). Protein folding in the absence of the solvent ordering contribution to the hydrophobic interaction.
  34. (2006). Single proline residues can dictate the oxidative folding pathways of cysteine-rich peptides.
  35. (2006). Stabilization of bzip peptides through incorporation of fluorinated aliphatic residues.
  36. (2001). Stabilization of coiled-coil peptide domains by introduction of trifluoroleucine.
  37. (2010). Stereoelectronic and steric effects in side chains preorganize a protein main chain.
  38. (2003). Stereoelectronic effects on collagen stability: the dichotomy of 4-fluoroproline diastereomers.
  39. (1987). Structure of ubiquitin refined at 1.8 A resolution.
  40. (1996). Structure of very early protein folding intermediates: new insights through a variant of hydrogen exchange labelling.
  41. (2010). Synthetic biology of protein folding.
  42. (2008). Synthetic biology of proteins: tuning GFPs folding and stability with fluoroproline.
  43. (1993). The HPV-16 E6 and E6-AP complex functions as a ubiquitin-protein ligase in the ubiquitination of p53.
  44. (2000). The importance of being proline: the interaction of proline-rich motifs in signaling proteins with their cognate domains.
  45. (2003). The role of cystine knots in collagen folding and stability, part II. Conformational properties of (ProHyp-Gly)n model trimers with N- and C-terminal collagen type III cystine knots.
  46. (1998). The ubiquitin-protein ligase E6-associated protein (E6-AP) serves as its own substrate.
  47. (1999). Thermal versus guanidine-induced unfolding of ubiquitin. An analysis in terms of the contributions from charge-charge interactions to protein stability.
  48. (1994). Thermodynamics of ubiquitin unfolding.
  49. (2000). Towards the nonstick egg: designing fluorous proteins.
  50. (2006). Ubiquitin: a small protein folding paradigm.