Minimal model systems for beta sheet secondary structure in proteins (Q77891983)

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9 December 2019

review article

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title

Minimal model systems for beta sheet secondary structure in proteins (English)

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https://www.ebi.ac.uk/europepmc/webservices/rest/search?query=EXT_ID:9914187%20AND%20SRC:MED&resulttype=core&format=json

9 December 2019

author name string

S H Gellman

series ordinal

1

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9 December 2019

publication date

1 December 1998

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Current Opinion in Chemical Biology

9 December 2019

published in

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https://www.ebi.ac.uk/europepmc/webservices/rest/search?query=EXT_ID:9914187%20AND%20SRC:MED&resulttype=core&format=json

9 December 2019

volume

2

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9 December 2019

issue

6

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9 December 2019

page(s)

717-725

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

9 December 2019

cites work

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7 January 2021

Beta-hairpin families in globular proteins

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7 January 2021

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

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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

1 reference

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7 January 2021

Tendamistat (12-26) fragment. NMR characterization of isolated beta-turn folding intermediates

1 reference

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7 January 2021

Dissecting the structure of a partially folded protein. Circular dichroism and nuclear magnetic resonance studies of peptides from ubiquitin

1 reference

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7 January 2021

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

1 reference

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7 January 2021

Native-like beta-hairpin structure in an isolated fragment from ferredoxin: NMR and CD studies of solvent effects on the N-terminal 20 residues

1 reference

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7 January 2021

Design and characterization of peptides with amphiphilic beta-strand structures

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7 January 2021

Conformation of β-hairpins in protein structures

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7 January 2021

Beta-hairpins in proteins revisited: lessons for de novo design

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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

A designed beta-hairpin peptide in crystals

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7 January 2021

Engineering of betabellin 14D: disulfide-induced folding of a beta-sheet protein

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7 January 2021

Design of a monomeric 23-residue polypeptide with defined tertiary structure

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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

Turn Residue Sequence Determines β-Hairpin Conformation in Designed Peptides

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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

Folding dynamics and mechanism of beta-hairpin formation

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7 January 2021

A statistical mechanical model for beta-hairpin kinetics.

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7 January 2021

Cross-strand side-chain interactions versus turn conformation in beta-hairpins

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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

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.

1 reference

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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

10.1016/S1367-5931(98)80109-9

Identifiers

DOI

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https://www.ebi.ac.uk/europepmc/webservices/rest/search?query=EXT_ID:9914187%20AND%20SRC:MED&resulttype=core&format=json

9 December 2019

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