The factors controlling a-helix formation in water by peptides of defined sequence are beginning to be understood. The field is close to the point where the extent of helix formation can be predicted for peptides of any sequence. Our own approach to the problem, and the main results obtained by following this approach, are summarized below. The chief reason for studying a-helix formation by peptides is to understand precisely and in detail one part of the protein folding problem. Questions about peptide helix formation can be answered at a fundamental level, in terms of the physico-chemical mechanisms involved. Key~~~rrk: Helix-stabilizing interaction; Helix propensity; N-cap 1. Early studies of helices formed by protein fragments The study...
Much effort has been invested in seeking to understand the thermodynamic basis of helix stability in...
Recent analysis of alpha helices in protein crystal structures, available in literature, revealed hy...
alpha-Helix formation of a peptidyl sequence is stabilized by hydrophobic residues recurring at posi...
Helix formation; Salt bridge; Side-chain interaction Previous tudies have identified Lys 1, Glu 2, a...
One of the most common structural elements in proteins is the a-helix. The main goal of this study w...
Segments with the amino acid sequence EKAYLRT (glutamine-lysine-alanine-tyrosine-leucine-arginine-th...
It is generally accepted that protein folding proceeds via local folded intermediates which functio...
The molecular mechanism of helix nucleation in peptides and proteins is not yet understood and the q...
The molecular mechanism of helix nucleation in peptides and proteins is not yet understood and the q...
[[abstract]]Knowledge of the role of individual side chains in forming different secondary structure...
Previous studies have demonstrated that His 12 plays a major role in the pH-dependent stability of t...
Thesis (Ph. D.)--Massachusetts Institute of Technology, Dept. of Chemistry, 2009.This electronic ver...
we have discovered an acylated heptapeptide amide comprising six Ca-tetrasubstituted amino acids and...
Forming peptide hydrogen bonds was considered to be probably the most important driving force for pr...
ABSTRACT Interactions between the a-helix peptide dipoles and charged groups close to the ends of th...
Much effort has been invested in seeking to understand the thermodynamic basis of helix stability in...
Recent analysis of alpha helices in protein crystal structures, available in literature, revealed hy...
alpha-Helix formation of a peptidyl sequence is stabilized by hydrophobic residues recurring at posi...
Helix formation; Salt bridge; Side-chain interaction Previous tudies have identified Lys 1, Glu 2, a...
One of the most common structural elements in proteins is the a-helix. The main goal of this study w...
Segments with the amino acid sequence EKAYLRT (glutamine-lysine-alanine-tyrosine-leucine-arginine-th...
It is generally accepted that protein folding proceeds via local folded intermediates which functio...
The molecular mechanism of helix nucleation in peptides and proteins is not yet understood and the q...
The molecular mechanism of helix nucleation in peptides and proteins is not yet understood and the q...
[[abstract]]Knowledge of the role of individual side chains in forming different secondary structure...
Previous studies have demonstrated that His 12 plays a major role in the pH-dependent stability of t...
Thesis (Ph. D.)--Massachusetts Institute of Technology, Dept. of Chemistry, 2009.This electronic ver...
we have discovered an acylated heptapeptide amide comprising six Ca-tetrasubstituted amino acids and...
Forming peptide hydrogen bonds was considered to be probably the most important driving force for pr...
ABSTRACT Interactions between the a-helix peptide dipoles and charged groups close to the ends of th...
Much effort has been invested in seeking to understand the thermodynamic basis of helix stability in...
Recent analysis of alpha helices in protein crystal structures, available in literature, revealed hy...
alpha-Helix formation of a peptidyl sequence is stabilized by hydrophobic residues recurring at posi...