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 very sensitive to the relative orientation of the segments. We provide here evidence that the alignment of secondary structure dipoles is significant in determining the three-dimensional structure of globular proteins
The conformational analysis of a pair of two-linked peptide units in the anti-parallel arrangement i...
The conformational analysis of a pair of two-linked peptide units in the anti-parallel arrangement i...
AbstractA novel super-secondary structure common for many non-homological proteins is considered. Th...
As a result of the regular arrangement of peptide dipoles in secondary structure segments and the lo...
As a result of the regular arrangement of peptide dipoles in secondary structure segments and the lo...
Electrostatic interactions between the peptide dipoles in α-helices and in parallel β-strands have b...
ABSTRACT: We present a generic solvated coarse-grained protein model that can be used to characteriz...
Proteins fold into unique three-dimensional structures by specific, orientation-dependent interactio...
SummaryAligned α helix peptide dipoles sum to a “macroscopic” dipole parallel to the helix axis that...
The tertiary structure and folding of proteins are interpreted in terms of the amino acid sequence. ...
194-202TIM proteins of ⍺/β barrel fold from ⍺/β class as given in SCOP database were taken for dipol...
Stabilization centers (SCs) were shown to play an important role in preventing decay of three-dimens...
The ground state electronic energy represents a complicated function of the nuclear coordinates. Eve...
AbstractWe demonstrate that an external constant electric field is able to modify the secondary stru...
The conformational analysis of a pair of two-linked peptide units in the anti-parallel arrangement i...
The conformational analysis of a pair of two-linked peptide units in the anti-parallel arrangement i...
The conformational analysis of a pair of two-linked peptide units in the anti-parallel arrangement i...
AbstractA novel super-secondary structure common for many non-homological proteins is considered. Th...
As a result of the regular arrangement of peptide dipoles in secondary structure segments and the lo...
As a result of the regular arrangement of peptide dipoles in secondary structure segments and the lo...
Electrostatic interactions between the peptide dipoles in α-helices and in parallel β-strands have b...
ABSTRACT: We present a generic solvated coarse-grained protein model that can be used to characteriz...
Proteins fold into unique three-dimensional structures by specific, orientation-dependent interactio...
SummaryAligned α helix peptide dipoles sum to a “macroscopic” dipole parallel to the helix axis that...
The tertiary structure and folding of proteins are interpreted in terms of the amino acid sequence. ...
194-202TIM proteins of ⍺/β barrel fold from ⍺/β class as given in SCOP database were taken for dipol...
Stabilization centers (SCs) were shown to play an important role in preventing decay of three-dimens...
The ground state electronic energy represents a complicated function of the nuclear coordinates. Eve...
AbstractWe demonstrate that an external constant electric field is able to modify the secondary stru...
The conformational analysis of a pair of two-linked peptide units in the anti-parallel arrangement i...
The conformational analysis of a pair of two-linked peptide units in the anti-parallel arrangement i...
The conformational analysis of a pair of two-linked peptide units in the anti-parallel arrangement i...
AbstractA novel super-secondary structure common for many non-homological proteins is considered. Th...