Polyproline II helical structure in protein unfolded states: Lysine peptides revisited

Protein Science

Volumn 11, Issue 4, 2002, Pages 980-985

  Rucker, Adam L ^a   Creamer, Trevor P ^a  

^a UNIVERSITY OF KENTUCKY   (United States)

Author keywords

Denatured; Disordered; Poly(lysine); Protein folding

Indexed keywords

LYSINE; PROLINE DERIVATIVE; SOLVENT;

ARTICLE; CIRCULAR DICHROISM; HYPOTHESIS; PH; PRIORITY JOURNAL; PROTEIN CONFORMATION; PROTEIN DENATURATION; PROTEIN FOLDING; PROTEIN INTERACTION; PROTEIN STRUCTURE;

CIRCULAR DICHROISM; HYDROGEN BONDING; LYSINE; PEPTIDES; PROTEIN CONFORMATION; PROTEIN FOLDING;

EID: 0036129072     PISSN: 09618368     EISSN: None     Source Type: Journal    
DOI: None     Document Type: Article

References (36)

1. Left-handed polyproline II helices commonly occur in globular proteins
2. Principles that govern the folding of protein chains
3. Non-specific helix-induction in charged homopolypeptides by alcohols
4. Circular dichroism of collagen and related polypeptides
5. Derivative spectroscopy applied to tyrosyl chromophores. Studies on ribonuclease, lima bean inhibitors, insulin, and pancreatic trypsin inhibitor
6. Helix propensities of the amino acids measured in alanine-based peptides without helix-stabilizing side-chain interactions
7. Left-handed polyproline II helix formation is (very) locally driven
8. Side-chain conformational entropy in protein unfolded states
9. Denatured states of proteins
10. Reassessment of the electronic circular dichroism criteria for random coil conformations of poly(L-lysine) and the implications for protein folding and denaturation studies
11. Reassessment of the random coil conformation: Vibrational CD study of proline oligopeptides and related polypeptides
12. Critical chain length for polyproline-II structure formation in H-Gly-(Pro)n-OH
13. Steric structure of L-proline oligopeptides. I. Infrared absorption spectra of the oligopeptides and poly-L-proline
14. Host-guest study of left-handed polyproline II helix formation
15. The circular dichroism spectrum and structure of unordered polypeptides and proteins
16. Modeling compact denatured states of proteins
17. Estimation of changes in side chain configurational entropy in binding and folding: General methods and application to helix formation
18. Formation of a hydrophobic cluster in denatured bovine pancreatic trypsin inhibitor
19. Side chain contributions to the stability of α-helical structure in peptides
20. Melting of the left-handed helical conformation of charged poly-L-lysine
21. Conformational properties of poly-L-proline in concentrated salt solutions
22. Pseudo-prolines: Induction of cis/trans-conformational interconversion by decreased transition state barriers
23. The Flory isolated-pair hypothesis is not valid for polypeptide chains: Implications for protein folding
24. Residue helix parameters obtained from dichroic analysis of peptides of defined sequence
25. The role of PII conformations in the calculation of peptide fractional helix content
26. Biphasic effects of alcohols on the phase transition of poly(L-lysine) between α-helix and β-sheet conformations
27. Persistence of native-like topology in a denatured protein in 8M urea
28. Molecular dynamics simulations of polypeptide conformations in water: A comparison of α, β, and poly(Pro)II conformations
29. A survey of left-handed polyproline II helices
30. Circular dichroism of poly-L-proline in an unordered conformation
31. New chain conformations of poly(glutamic acid) and polylysine
32. Effect of temperature on the circular dichroism spectra of polypeptides in the extended states
33. Systemin has the characteristics of a poly(L-proline) II type helix
34. The structure and function of proline-rich regions in proteins
35. Residual structure in unfolded proteins revealed by Raman optical activity
36. Circular dichroism and conformation of unordered polypeptides