Helix design, prediction and stability

Current Opinion in Biotechnology

Volumn 6, Issue 4, 1995, Pages 382-386

  Muñoz, Victor ^a   Serrano, Luis ^a  

^a EUROPEAN MOLECULAR BIOLOGY LABORATORY   (Germany)

Author keywords

[No Author keywords available]

Indexed keywords

POLYPEPTIDE;

GENETIC ENGINEERING; PRIORITY JOURNAL; PROTEIN SECONDARY STRUCTURE; PROTEIN STABILITY; SHORT SURVEY; THERMODYNAMICS;

AMINO ACID SEQUENCE; MODELS, MOLECULAR; MOLECULAR SEQUENCE DATA; PROTEIN CONFORMATION; PROTEIN ENGINEERING; PROTEIN STRUCTURE, SECONDARY; PROTEINS;

EID: 0029155035     PISSN: 09581669     EISSN: None     Source Type: Journal    
DOI: 10.1016/0958-1669(95)80066-2     Document Type: Article

References (59)

1. Calorimetric determination of the enthalpy change for the α-helix to coil transition of an alanine peptide in water
2. A thermodynamic scale for the helix-forming tendencies of the commonly occurring amino acids
3. Relative helix-forming tendencies of nonpolar amino acids
4. Positional independence and additivity of amino acid replacements on helix stability in monomeric peptides
5. Effect of central-residue replacements on the helical stability of a monomeric peptide
6. Local effect of glycine substitution in a model helical peptide
7. Large differences in the helix propensities of alanine and glycine
8. Straight-chain non-polar amino acids are good helix-formers in water
9. Residue helix parameters obtained from dichroic analysis of peptides of defined sequence
10. A single-stranded amphipatic α-helix in aqueous solution: design, structural characterisation, and its application for determining α-helical propensities of amino acids
11. Helix propensities of the amino-acids measured in alanine-based peptides without helix-stabilizing side chain interactions
12. Effect of alanine versus glycine in α-helices on protein stability
13. α-Helix stability in proteins. I. Empirical correlations concerning substitution of side chains at the N- and C-caps and the replacement of alanine by glicine or serine at solvent-exposed surfaces
14. α-helix stability in proteins. II. Factors that influence stability at an internal position
15. Structural basis of amino acid α-helix propensity
16. Intrinsic secondary structure propensities of the amino acids, using statistical φ-ψ matrices: Comparison with experimental scales
17. Position-dependent stabilizing effects in .alpha.-helices: N-terminal capping in synthetic model peptides
18. Capping interactions in isolated α-helices: position-dependent substitution effects and structure of a serine-capped peptide helix
19. Helix N-cap propensities in peptides parallel those found in proteins
20. Stabilization of α-helical structures in short peptides via end capping
21. Determination of the free energies of N-capping in α-helices by modification of the Lifson—Roig helix-coil theory to include N- and C-capping
22. Capping and α-helix stability
23. Dissection of helix capping in T4 Lysozyme by structural and thermodynamical analysis of six amino acids substitutions at Thr59
24. Mutational analysis of the N-capping box of the α-helix of chymotrypsin inhibitor 2
25. Effect of end group blockage on the properties of a class A amphipathic helical peptide
26. The contribution of residue ion pairs to the helical stability of a model peptide
27. Helical peptides with three pairs of Asp-Arg and Glu-Arg residues in different orientations and spacings
28. The role of interhelical ionic interactions in controlling protein folding and stability
29. The energetics of ion-pair and hydrogen-bonding interactions in a helical peptide
30. Helix-stabilizing Interaction Between Tyrosine and Leucine or Valine when the Spacing is i,i + 4
31. Side-chain interactions between sulfur-containing amino acids and phenylalanine in alpha-helices.
32. The (i, i+4) Phe-His interaction studied in an alanine-based α-helix
33. Tests for helix-stabilizing interactions between various nonpolar side chains in alanine-based peptides
34. Analysis of the interaction between charged side chains and the α-helix dipole using designed thermostable mutants of phage T4 lysozyme
35. s, and protein stability
36. Electrostatic screening of charge and dipole interactions with the helix backbone
37. Effect of a single aspartate on helix stability at different positions in a neutral alanine-base peptide
38. Charged histidine effects of α-helix stability at all positions in the helix by interacting with the backbone charges
39. Design of helix ends
40. Helix stop signals in proteins and peptides: the capping box
41. Sequence determinants of the capping box, a stabilizing motif at the N-termini of α-helices
42. Rules for α-helix termination by glycine
43. α-Helix capping in synthetic model peptides by reciprocal side chain—main chain interactions: evidence for an N-terminal ‘capping box’
44. Helix stop and start signals in peptides and proteins. The capping box does not necessarily prevent helix elongation.
45. The hydrophobic-staple motif and a role for loop-residues in α-helix stability and protein folding
46. Theory of the Phase Transition between Helix and Random Coil in Polypeptide Chains
47. On the theory of helix-coil transitions in biopolymers
48. Physical reasons for secondary structure stability: α-helices in short peptides
49. The helix-coil transition in heterogeneous peptides with specific side-chain interactions: theory and comparison with CD spectral data
50. Effect of sequence-specific interactions on the stability of helical conformations in polypeptides
51. The energetics of ion-pair and hydrogen-bonding interactions in a helical peptide
52. Elucidating the folding problem of helical peptides using empirical parameters
53. Elucidating the Folding Problem of Helical Peptides using Empirical Parameters. II†. Helix Macrodipole Effects and Rational Modification of the Helical Content of Natural Peptides
54. Aromatic side-chain contribution to far-ultraviolet circular dichroism of helical peptides and its effect on measurement of helix propensities
55. Elucidating the Folding Problem of Helical Peptides using Empirical Parameters. III>Temperature and pH Dependence
56. A neutral, water-soluble, .alpha.-helical peptide: the effect of ionic strength on the helix-coil equilibrium
57. Stabilization of myoglobin by multiple alanine substitutions in helical positions
58. Alanine scanning mutagenesis of the α-helix 115–123 of phage T4 lysozyme: effects on structure, stability and the binding of solvent
59. Peptide conformation and protein folding