(Q58622073)

English

Structural analysis of peptides encompassing all α-helices of three α/β parallel proteins: Che-Y, flavodoxin and P21-Ras: Implications for α-Helix stability and the folding of α/β parallel proteins

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scholarly article

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Structural analysis of peptides encompassing all α-helices of three α/β parallel proteins: Che-Y, flavodoxin and P21-Ras: Implications for α-Helix stability and the folding of α/β parallel proteins (English)

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protein folding

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author name string

Victor Muñoz

1

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Luis Serrano

2

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M. Angeles Jiménez

3

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Manuel Rico

4

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language of work or name

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publication date

April 1995

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Journal of Molecular Biology

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247

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648-669

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4

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Circular dichroism and optical rotatory dispersion of proteins and polypeptides.

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Two‐dimensional spectroscopy. Application to nuclear magnetic resonance

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Magnesium binding to the bacterial chemotaxis protein CheY results in large conformational changes involving its functional surface

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The homologous angiogenin and ribonuclease N-terminal fragments fold into very similar helices when isolated

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A short linear peptide that folds into a native stable beta-hairpin in aqueous solution

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NMR solution structure of the isolated N-terminal fragment of protein-G B1 domain. Evidence of trifluoroethanol induced native-like beta-hairpin formation

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Identification of protein folds: matching hydrophobicity patterns of sequence sets with solvent accessibility patterns of known structures

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Side chain-backbone hydrogen bonding contributes to helix stability in peptides derived from an alpha-helical region of carboxypeptidase A.

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1H- and 15N-NMR assignment and solution structure of the chemotactic Escherichia coli Che Y protein

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Aromatic side-chain contribution to far-ultraviolet circular dichroism of helical peptides and its effect on measurement of helix propensities

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Determination of the helix and beta form of proteins in aqueous solution by circular dichroism.

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Defining solution conformations of small linear peptides

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Folding of peptide fragments comprising the complete sequence of proteins. Models for initiation of protein folding. I. Myohemerythrin

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Folding of peptide fragments comprising the complete sequence of proteins

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Improved efficiency of protein structure calculations from NMR data using the program DIANA with redundant dihedral angle constraints.

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Helix stop signals in proteins and peptides: the capping box

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Peptide group chemical shift computation

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Helical peptides with three pairs of Asp-Arg and Glu-Arg residues in different orientations and spacings

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Effect of a single aspartate on helix stability at different positions in a neutral alanine-based peptide

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Periodic properties of proton conformational shifts in isolated protein helices. An experimental study

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CD and 1H-NMR studies on the conformational properties of peptide fragments from the C-terminal domain of thermolysin.

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Dictionary of protein secondary structure: pattern recognition of hydrogen-bonded and geometrical features

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Protein-folding dynamics

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Local conformations of peptides representing the entire sequence of bovine pancreatic trypsin inhibitor and their roles in folding

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A helix stop signal in the isolated S-peptide of ribonuclease A

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A two-dimensional nuclear Overhauser enhancement (2D NOE) experiment for the elucidation of complete proton-proton cross-relaxation networks in biological macromolecules

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Peptide alpha-helicity in aqueous trifluoroethanol: correlations with predicted alpha-helicity and the secondary structure of the corresponding regions of bovine growth hormone

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Theoretical study of the contribution of aromatic side chains to the circular dichroism of basic bovine pancreatic trypsin inhibitor

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Application of phase sensitive two-dimensional correlated spectroscopy (COSY) for measurements of 1H-1H spin-spin coupling constants in proteins

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The folding of an enzyme. IV. Structure of an intermediate in the refolding of barnase analysed by a protein engineering procedure

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Effect of amino acid ion pairs on peptide helicity

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Elucidating the folding problem of helical peptides using empirical parameters.

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Elucidating the folding problem of helical peptides using empirical parameters. II. Helix macrodipole effects and rational modification of the helical content of natural peptides.

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Elucidating the folding problem of helical peptides using empirical parameters. III. Temperature and pH dependence.

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Persistence of the alpha-helix stop signal in the S-peptide in trifluoroethanol solutions

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Helix-stabilizing Interaction Between Tyrosine and Leucine or Valine when the Spacing is i,i + 4

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Refined crystal structure of the triphosphate conformation of H-ras p21 at 1.35 A resolution: implications for the mechanism of GTP hydrolysis

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Conformational properties of the isolated 1–23 fragment of human hemoglobin α-chain

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Helix signals in proteins

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Amino acid preferences for specific locations at the ends of alpha helices

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Low-temperature 1H-NMR evidence of the folding of isolated ribonuclease S-peptide

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Conformational behavior of Escherichia coli OmpA signal peptides in membrane mimetic environments

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An N-terminal fragment of barnase has residual helical structure similar to that in a refolding intermediate

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The energetics of ion-pair and hydrogen-bonding interactions in a helical peptide

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Helix propagation in trifluoroethanol solutions

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Comparisons between the three-dimensional structures of the chemotactic protein CheY and the normal Gly 12-p21 protein.

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10.1016/S0022-2836(05)80145-7

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