Structural characterization of a mutant peptide derived from ubiquitin: Implications for protein folding - Wikidata - awgldk - TriplyDB

Structural characterization of a mutant peptide derived from ubiquitin: Implications for protein folding

Structural characterization of a mutant peptide derived from ubiquitin: Implications for protein folding

http://www.wikidata.org/entity/Q27629222

about

Structure-function-folding relationship in a WW domain Tryptophan zippers: Stable, monomeric -hairpins Turn stability in β-hairpin peptides: Investigation of peptides containing 3:5 type I G1 bulge turns Folding of small proteins using constrained molecular dynamics Measuring the refolding of beta-sheets with different turn sequences on a nanosecond time scale.Yeast display evolution of a kinetically efficient 13-amino acid substrate for lipoic acid ligase.The role of the unfolded state in hairpin stability.Local structural preferences and dynamics restrictions in the urea-denatured state of SUMO-1: NMR characterization.Convergent evolution in structural elements of proteins investigated using cross profile analysis.Multiple Simulated Annealing-Molecular Dynamics (MSA-MD) for Conformational Space Search of Peptide and Miniprotein.Effects of turn residues in directing the formation of the beta-sheet and in the stability of the beta-sheet.Determining α-helical and β-sheet secondary structures via pulsed electron spin resonance spectroscopy.Determining the Secondary Structure of Membrane Proteins and Peptides Via Electron Spin Echo Envelope Modulation (ESEEM) Spectroscopy Mechanism of formation of the C-terminal beta-hairpin of the B3 domain of the immunoglobulin binding protein G from Streptococcus. II. Interplay of local backbone conformational dynamics and long-range hydrophobic interactions in hairpin formation.Expected and unexpected results from combined beta-hairpin design elements.

P2860

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P2860

Structural characterization of a mutant peptide derived from ubiquitin: Implications for protein folding

http://www.wikidata.org/entity/Q27629222

description

2000 nî lūn-bûn

@nan

2000 թուականի Նոյեմբերին հրատարակուած գիտական յօդուած

@hyw

2000 թվականի նոյեմբերին հրատարակված գիտական հոդված

@hy

2000年の論文

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2000年論文

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2000年論文

@zh-hant

2000年論文

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2000年論文

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2000年論文

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2000年论文

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name

Structural characterization of ...... plications for protein folding

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Structural characterization of ...... plications for protein folding

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Structural characterization of ...... plications for protein folding

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Structural characterization of ...... plications for protein folding

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Structural characterization of ...... plications for protein folding

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Structural characterization of ...... plications for protein folding

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Structural characterization of ...... plications for protein folding

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Structural characterization of ...... plications for protein folding

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P1433

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P2860

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P1433

Protein Science

P1476

Structural characterization of ...... plications for protein folding

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P2093

A Raine

http://www.w3.org/2001/XMLSchema#string

D H Williams

http://www.w3.org/2001/XMLSchema#string

P A Evans

http://www.w3.org/2001/XMLSchema#string

P Y Chen

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R Zerella

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P2860

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

Gradient-tailored excitation for single-quantum NMR spectroscopy of aqueous solutions

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

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

Dissecting the stability of a beta-hairpin peptide that folds in water: NMR and molecular dynamics analysis of the beta-turn and beta-strand contributions to folding.

Influence of non-bonded parameters on the quality of NMR structures: a new force field for NMR structure calculation.

Characterization of a partially denatured state of a protein by two-dimensional NMR: reduction of the hydrophobic interactions in ubiquitin.

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.

The turn sequence directs beta-strand alignment in designed beta-hairpins.

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

P304

2142-50

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scholarly article

P356

10.1110/PS.9.11.2142

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11

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P478

9

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2000-11-01T00:00:00Z

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P5875

12177604

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P698

11152124

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P921

protein folding

P932

2144502

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