The design of linear peptides that fold as monomeric beta-sheet structures. (Q30322862)

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11 December 2019

review article

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title

The design of linear peptides that fold as monomeric beta-sheet structures (English)

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11 December 2019

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11 December 2019

E Lacroix

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11 December 2019

M Lopez de la Paz

series ordinal

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11 December 2019

L Serrano

series ordinal

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11 December 2019

publication date

1 August 1999

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Current Opinion in Structural Biology

11 December 2019

published in

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11 December 2019

volume

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11 December 2019

issue

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11 December 2019

page(s)

487-493

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α-Helix formation by peptides of defined sequence

11 December 2019

cites work

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Helix design, prediction and stability

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Elucidating the folding problem of alpha-helices: local motifs, long-range electrostatics, ionic-strength dependence and prediction of NMR parameters.

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7 January 2021

Deciphering rules of helix stability in peptides

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7 January 2021

Analysis of the effect of local interactions on protein stability.

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Stabilization of proteins by rational design of alpha-helix stability using helix/coil transition theory.

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7 January 2021

The de novo design of protein structures

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A designed metal-binding protein with a novel fold

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NMR structure of a de novo designed, peptide 33mer with two distinct, compact beta-sheet folds

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7 January 2021

Protein structure. Born to be beta

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7 January 2021

Guidelines for protein design: the energetics of beta sheet side chain interactions

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Electrostatic Interactions across a β-Sheet†

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Aromatic rescue of glycine in beta sheets

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7 January 2021

Formation and stability of beta-hairpin structures in polypeptides

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7 January 2021

Beta-hairpin and beta-sheet formation in designed linear peptides.

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7 January 2021

An analysis of side chain interactions and pair correlations within antiparallel beta-sheets: the differences between backbone hydrogen-bonded and non-hydrogen-bonded residue pairs.

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7 January 2021

Determinants of strand register in antiparallel beta-sheets of proteins

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7 January 2021

A revised set of potentials for beta-turn formation in proteins

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7 January 2021

Minimal model systems for beta sheet secondary structure in proteins

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7 January 2021

Thermodynamic beta-sheet propensities measured using a zinc-finger host peptide.

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7 January 2021

Measurement of the β-sheet-forming propensities of amino acids

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7 January 2021

Context is a major determinant of β-sheet propensity

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7 January 2021

A thermodynamic scale for the beta-sheet forming tendencies of the amino acids.

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7 January 2021

Role of beta-turn residues in beta-hairpin formation and stability in designed peptides.

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7 January 2021

Modulation of intrinsic phi,psi propensities of amino acids by neighbouring residues in the coil regions of protein structures: NMR analysis and dissection of a beta-hairpin peptide.

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7 January 2021

Origin of β-Hairpin Stability in Solution: Structural and Thermodynamic Analysis of the Folding of a Model Peptide Supports Hydrophobic Stabilization in Water

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7 January 2021

De novo design and structural analysis of a model beta-hairpin peptide system

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7 January 2021

Interactions Responsible for the pH Dependence of the beta-Hairpin Conformational Population Formed by a Designed Linear Peptide

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7 January 2021

Rate of beta-structure formation in polypeptides

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7 January 2021

Cooperative Interaction between the Three Strands of a Designed Antiparallel β-Sheet

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7 January 2021

Design of a 20-amino acid, three-stranded beta-sheet protein

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7 January 2021

Comparison between the phi distribution of the amino acids in the protein database and NMR data indicates that amino acids have various phi propensities in the random coil conformation

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7 January 2021

Analysis of main chain torsion angles in proteins: prediction of NMR coupling constants for native and random coil conformations

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7 January 2021

NMR analysis of main-chain conformational preferences in an unfolded fibronectin-binding protein

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7 January 2021

Denaturant m values and heat capacity changes: relation to changes in accessible surface areas of protein unfolding

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7 January 2021

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

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7 January 2021

A short linear peptide derived from the N-terminal sequence of ubiquitin folds into a water-stable non-native β-hairpin

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7 January 2021

Folding dynamics and mechanism of β-hairpin formation

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7 January 2021

De novo protein design: towards fully automated sequence selection

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7 January 2021

10.1016/S0959-440X(99)80069-4

Identifiers

DOI

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11 December 2019

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