High helicity of peptide fragments corresponding to beta-strand regions of beta-lactoglobulin observed by 2D-NMR spectroscopy. (Q36851297)

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1 November 2019

title

High helicity of peptide fragments corresponding to beta-strand regions of beta-lactoglobulin observed by 2D-NMR spectroscopy (English)

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1 November 2019

2

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author name string

Kuroda Y

series ordinal

1

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Tanaka T

series ordinal

3

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Goto Y

series ordinal

4

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1 November 2019

publication date

1 January 1996

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1 November 2019

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1 November 2019

volume

1

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issue

4

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1 November 2019

page(s)

255-263

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Stabilization of helical structure in two 17-residue amphipathic analogues of the C-terminal peptide of cytochrome C.

1 November 2019

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Residual helical structure in the C-terminal fragment of cytochrome c

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A peptide corresponding to the N-terminal 13 residues of T4 lysozyme forms an alpha-helix

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A peptide model of a protein folding intermediate

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A noncovalent peptide complex as a model for an early folding intermediate of cytochrome c

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The nature of protein folding pathways: the classical versus the new view

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Structural characterization of a partly folded apomyoglobin intermediate

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Structural description of acid-denatured cytochrome c by hydrogen exchange and 2D NMR.

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Formation of a molten globule intermediate early in the kinetic folding pathway of apomyoglobin

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Structural characterization of folding intermediates in cytochrome c by H-exchange labelling and proton NMR.

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Conformation of peptide fragments of proteins in aqueous solution: implications for initiation of protein folding

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The structure of β-lactoglobulin and its similarity to plasma retinol-binding protein

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Rapid formation of secondary structure framework in protein folding studied by stopped-flow circular dichroism

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Trifluoroethanol-induced stabilization of the alpha-helical structure of beta-lactoglobulin: implication for non-hierarchical protein folding

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7 January 2021

Reversible effects of medium dielectric constant on structural transformation of beta-lactoglobulin and its retinol binding

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High helical propensity of the peptide fragments derived from beta-lactoglobulin, a predominantly beta-sheet protein

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7 January 2021

Predicting protein secondary structure based on amino acid sequence

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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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Helix-coil transition of the isolated amino terminus of ribonuclease

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Tests of the helix dipole model for stabilization of α-helices

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

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7 January 2021

Far-UV Circular Dichroism Reveals a Conformational Switch in a Peptide Fragment from the .beta.-Sheet of Hen Lysozyme

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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 of peptide fragments comprising the complete sequence of proteins

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7 January 2021

Local structures in unfolded lysozyme and correlation with secondary structures in the native conformation: helix-forming or -breaking propensity of peptide segments.

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7 January 2021

Conformational Properties of Four Peptides Spanning the Sequence of Hen Lysozyme

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Effect of trifluoroethanol on protein secondary structure: an NMR and CD study using a synthetic actin peptide

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7 January 2021

Elucidating the folding problem of helical peptides using empirical parameters.

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7 January 2021

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7 January 2021

Combining evolutionary information and neural networks to predict protein secondary structure

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7 January 2021

Prediction of protein secondary structure at better than 70% accuracy

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7 January 2021

A salt bridge stabilizes the helix formed by isolated C-peptide of RNase A

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7 January 2021

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

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7 January 2021

Parameters of helix-coil transition theory for alanine-based peptides of varying chain lengths in water

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Identifiers

DOI

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1 November 2019

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