(Q30403861)

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Stabilization of protein structure by interaction of alpha-helix dipole with a charged side chain

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Europe PubMed Central

PubMed publication ID

21 June 2017

Stabilization of protein structure by interaction of alpha-helix dipole with a charged side chain (English)

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Europe PubMed Central

PubMed publication ID

21 June 2017

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Fersht AR

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21 June 2017

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Sali D

1

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21 June 2017

Bycroft M

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21 June 2017

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1 October 1988

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21 June 2017

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21 June 2017

335

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21 June 2017

6192

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Europe PubMed Central

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21 June 2017

740-743

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Europe PubMed Central

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21 June 2017

Contribution of hydrophobic interactions to protein stability

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A reversible thermal transition of the extracellular ribonuclease of Bacillus amyloliquefaciens

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Tailoring the pH dependence of enzyme catalysis using protein engineering

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The alpha-helix dipole and the properties of proteins

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The role of the alpha-helix dipole in protein function and structure

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Calculation of the electric potential in the active site cleft due to alpha-helix dipoles

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The pKa values of two histidine residues in human haemoglobin, the Bohr effect, and the dipole moments of α-helices

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Conformation analysis of L-pyroglutamic acid N-methylamide by depolarized Rayleigh diffusion, vibration spectroscopy, and conformational energy calculation

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Nature of the charge distribution in proteins

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Nature of the charged-group effect on the stability of the C-peptide helix

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Protein engineering of cytochrome c by semisynthesis: substitutions at glutamic acid 66.

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Molecular structure of a new family of ribonucleases

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Probing histidine-substrate interactions in tyrosyl-tRNA synthetase using asparagine and glutamine replacements

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Identifiers

10.1038/335740A0

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Europe PubMed Central

PubMed publication ID

21 June 2017

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PubMed publication ID

1 reference

Europe PubMed Central

PubMed publication ID

21 June 2017

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