The α-helix dipole and the properties of proteins

@article{Hol1978TheD,
  title={The $\alpha$-helix dipole and the properties of proteins},
  author={Wim G. J. Hol and P. T. van Duijnen and H. J. C. Berendsen},
  journal={Nature},
  year={1978},
  volume={273},
  pages={443-446}
}
Phosphate moieties bind frequently at N-termini of helices in proteins. It is shown that this corresponds with an optimal interaction of the helix dipole and the charged phosphate. This favourable arrangement may have been discovered several times during evolution. In some enzymes, the helix dipole might be used in catalysis. 
Dipoles of the α-helix and β-sheet: their role in protein folding
As a result of the regular arrangement of peptide dipoles in secondary structure segments and the low effective dielectric constant in Hydrophobic cores, the electrostatic energy of a protein is veryExpand
The Role of Electrostatic Interactions in the Structure of Globular Proteins
The structure of a protein may be considered as a scaffolding that brings into the correct spatial arrangement a constellation of amino acid side chains to perform a given function. If the structureExpand
Enhanced protein thermostability from designed mutations that interact with α-helix dipoles
Two different genetically engineered amino-acid substitutions designed to interact with α-helix dipoles in T4 lysozyme are shown to increase the thermal stability of the protein. CrystallographicExpand
Tests of the helix dipole model for stabilization of α-helices
Charged groups play a critical role in the stability of the helix formed by the isolated C-peptide (residues 1–13 of ribonuclease A) in aqueous solution. One charged-group effect may arise fromExpand
PHOSPHORYLATION STABILIZES THE N-TERMINI OF ALPHA -HELICES
: The role of phosphorylation in stabilizing the N-termini of alpha-helices is examined using computer simulations of model peptides. The models comprise either a phosphorylated or unphosphorylatedExpand
Stabilization of protein structure by interaction of α-helix dipole with a charged side chain
The α-helix in proteins has a dipole moment resulting from the alignment of dipoles of the peptide bond which can perturb the pKas of ionizing groups. One of the two histidine residues (His18) inExpand
Electrostatic potentials of the alpha helix dipole and of elastase
Abstract Molecular graphics has been used to display the electrostatic potentials of the α-helix dipole and that of elastase calculated using atomic charges obtained by a new, simple method 1–3 .Expand
The three-dimensional structure of trp repressor
TLDR
The crystal structure of the Escherichia coli trp repressor has been solved to atomic resolution and the binding of L-tryptophan activates the aporepressor indirectly by fixing the orientation of the second helix of the helix–turn–helix motif. Expand
Macrodipole Moment of Polypeptides in β-Sheet and Its Prediction from Dipole Moments of Amino Acid Residues as Building Blocks: Alanine and Glycine in β-Strand
The macrodipole moment of a β-sheet depends on the number and length of β-strands, as well as whether it is parallel or antiparallel. Here, we propose the VSHBβ model, in which the dipole moments o...
Electrostatic interactions between α‐helix dipoles in crystals of an uncharged helical undecapeptide
The electrostatic interactions between α‐helix dipoles in the crystals of an uncharged helical undecapeptide have been studied in detail. The electrostatic interaction energy between one helix dipoleExpand
...
1
2
3
4
5
...

References

SHOWING 1-10 OF 37 REFERENCES
The peptide chain of tyrosyl tRNA synthetase: no evidence for a super-secondary structure of four alpha-helices.
TLDR
A detailed backbone model has been built for 274 residues of tyrosyl tRNA synthetase, based on an X-ray diffraction study, which gives no support to the idea that four antiparallel helices form a common structural unit in proteins. Expand
Structure of Subtilisin BPN′ at 2.5 Å Resolution
The single polypeptide chain is folded into three parts, with the active site at their conjunction. In the active enzyme, the side chain of His 64 is in a position consistent with the formation of aExpand
Chemical and biological evolution of a nucleotide-binding protein
Three-dimensional alignment of the common nucleotide binding structure in dehydrogenases, kinases and flavodoxins permits the recognition of homologous amino acids when sequence comparisons aloneExpand
The covalent and tertiary structure of bovine liver rhodanese
Bovine liver rhodanese is a single polypeptide of 293 amino acids in which the halves of the molecule assume analogous tertiary structures in the absence of substantial sequence homology. The sulphurExpand
Structure of chicken muscle triose phosphate isomerase determined crystallographically at 2.5Å resolution: using amino acid sequence data
Each subunit of triose phosphate isomerase is composed of alternate segments of polypeptide chain in the α- and β-conformations that are arranged to form an inner cylinder of parallel-pleated sheetExpand
Three-dimensional Structure of Tosyl-elastase
TLDR
Amino-acid sequence studies and crystallographic evidence are used to construct an atomic model of elastase, which is compared with the structure of α-chymotrypsin, which shows opposite polarity. Expand
Tertiary structural differences between microbial serine proteases and pancreatic serine enzymes
TLDR
The three major regions of difference show how this family of proteolytic enzymes has developed from the more primitive bacterial to the relatively sophisticated pancreatic enzymes. Expand
Topological comparison of adenyl kinase with other proteins
A COMBINATION of amino acid sequence analysis1 and X-ray analysis has yielded the atomic structure of the enzyme adenyl kinase2 (adenylate kinase, EC 2.7.4.3). No protein of which the structure isExpand
Structure of crystalline -chymotrypsin. V. The atomic structure of tosyl- -chymotrypsin at 2 A resolution.
Abstract Refined atomic co-ordinates for tosyl-α-chymotrypsin have been obtained by computational refinement of co-ordinates derived from a carefully built atomic model. The two independent views ofExpand
Anion binding sites in the active center of D-glyceraldehyde-3-phosphate dehydrogenase.
Crystals of lobster holo- d -glyceraldehyde-3-phosphate dehydrogenase, grown in ammonium sulfate, were dialyzed against sodium citrate buffer at pH 6·2. This procedure caused two sulfate ions in eachExpand
...
1
2
3
4
...