The equilibrium unfolding pathway of a (beta/alpha)8 barrel (Q44241858)

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scientific article published in December 2002

Language	Label	Description	Also known as
English	The equilibrium unfolding pathway of a (beta/alpha)8 barrel	scientific article published in December 2002

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scholarly article

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Europe PubMed Central

PubMed publication ID

1 December 2017

The equilibrium unfolding pathway of a (beta/alpha)8 barrel (English)

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Europe PubMed Central

PubMed publication ID

1 December 2017

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author name string

Joshua A Silverman

1

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Europe PubMed Central

PubMed publication ID

1 December 2017

Pehr B Harbury

2

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Europe PubMed Central

PubMed publication ID

1 December 2017

language of work or name

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publication date

1 December 2002

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Europe PubMed Central

PubMed publication ID

1 December 2017

number of pages

10

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Journal of Molecular Biology

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Europe PubMed Central

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1 December 2017

324

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PubMed publication ID

1 December 2017

5

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Europe PubMed Central

PubMed publication ID

1 December 2017

1031-1040

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Europe PubMed Central

PubMed publication ID

1 December 2017

Identification of unfolding domains in large proteins by their unfolding rates

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Stable substructures of eightfold beta alpha-barrel proteins: fragment complementation of phosphoribosylanthranilate isomerase

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Detection of an intermediate in the folding of the (beta alpha)8-barrel N-(5'-phosphoribosyl)anthranilate isomerase from Escherichia coli.

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Folding, stability, and physical properties of the alpha subunit of bacterial luciferase

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Molecular dissection of the folding mechanism of the alpha subunit of tryptophan synthase: an amino-terminal autonomous folding unit controls several rate-limiting steps in the folding of a single domain protein

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Protein folding intermediates and pathways studied by hydrogen exchange

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Hydrogen exchange studies of protein structure

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Comparison of equilibrium and kinetic approaches for determining protein folding mechanisms

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Protein folding intermediates: native-state hydrogen exchange

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

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On the nature of conformational openings: native and unfolded-state hydrogen and thiol-disulfide exchange studies of ferric aquomyoglobin

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Changes in side chain packing during apomyoglobin folding characterized by pulsed thiol-disulfide exchange

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Rapid mapping of protein structure, interactions, and ligand binding by misincorporation proton-alkyl exchange.

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A thermodynamic scale for the helix-forming tendencies of the commonly occurring amino acids

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A direct comparison of helix propensity in proteins and peptides

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Helix propensities are identical in proteins and peptides

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Hydrogen-exchange stabilities of RNase T1 and variants with buried and solvent-exposed Ala --> Gly mutations in the helix

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A compact monomeric intermediate identified by NMR in the denaturation of dimeric triose phosphate isomerase

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Role of non-native aromatic and hydrophobic interactions in the folding of hen egg white lysozyme.

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A protein folding intermediate of ribonuclease T1 characterized at high resolution by 1D and 2D real-time NMR spectroscopy

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Exploring the folding funnel of a polypeptide chain by biophysical studies on protein fragments

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Native and non-native secondary structure and dynamics in the pH 4 intermediate of apomyoglobin

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Is folding of beta-lactoglobulin non-hierarchic? Intermediate with native-like beta-sheet and non-native alpha-helix

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Transient non-native secondary structures during the refolding of alpha-lactalbumin detected by infrared spectroscopy

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Identifying the structural boundaries of independent folding domains in the alpha subunit of tryptophan synthase, a beta/alpha barrel protein

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MOLSCRIPT: a program to produce both detailed and schematic plots of protein structures

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Hydrogen Exchange in Proteins

1 reference

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Identifiers

10.1016/S0022-2836(02)01100-2

1 reference

Europe PubMed Central

PubMed publication ID

1 December 2017

PubMed publication ID

1 reference

Europe PubMed Central

PubMed publication ID

1 December 2017

ResearchGate publication ID

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