Real-time and equilibrium (19)F-NMR studies reveal the role of domain-domain interactions in the folding of the chaperone PapD. (Q33894363)

29 July 2017

title

Real-time and equilibrium (19)F-NMR studies reveal the role of domain-domain interactions in the folding of the chaperone PapD. (English)

1 reference

29 July 2017

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3

Scott J Hultgren

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29 July 2017

4

Carl Frieden

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29 July 2017

James G Bann

1

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29 July 2017

Jerome Pinkner

series ordinal

2

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29 July 2017

language of work or name

English

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publication date

15 January 2002

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Proceedings of the National Academy of Sciences of the United States of America

29 July 2017

published in

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29 July 2017

volume

99

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29 July 2017

issue

2

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29 July 2017

page(s)

709-714

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Intestinal fatty acid binding protein: the folding mechanism as determined by NMR studies

29 July 2017

cites work

1 reference

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28 July 2018

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Structural basis of chaperone function and pilus biogenesis

28 July 2018

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Turn scanning by site-directed mutagenesis: application to the protein folding problem using the intestinal fatty acid binding protein

28 July 2018

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Intestinal fatty acid binding protein: a specific residue in one turn appears to stabilize the native structure and be responsible for slow refolding

28 July 2018

1 reference

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Molecular basis of two subfamilies of immunoglobulin-like chaperones

28 July 2018

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The immunoglobulin fold. Structural classification, sequence patterns and common core

28 July 2018

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The crystal structure of porcine pancreatic alpha-amylase in complex with the microbial inhibitor Tendamistat

28 July 2018

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Amino acid replacements of the glutamic acid residue at position 48 in the tryptophan synthetase A protein of Escherichia coli

28 July 2018

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Unfolding free energy changes determined by the linear extrapolation method. 1. Unfolding of phenylmethanesulfonyl alpha-chymotrypsin using different denaturants

28 July 2018

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Analysis of prepro-alpha-lytic protease expression in Escherichia coli reveals that the pro region is required for activity

28 July 2018

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PapD, a periplasmic transport protein in P-pilus biogenesis

28 July 2018

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Dynamic NMR spectral analysis and protein folding: identification of a highly populated folding intermediate of rat intestinal fatty acid-binding protein by 19F NMR

28 July 2018

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Interactive surface in the PapD chaperone cleft is conserved in pilus chaperone superfamily and essential in subunit recognition and assembly

28 July 2018

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PapD-like chaperones provide the missing information for folding of pilin proteins

28 July 2018

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Real-time refolding studies of 6-19F-tryptophan labeled Escherichia coli dihydrofolate reductase using stopped-flow NMR spectroscopy.

21 January 2018

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Protein memory through altered folding mediated by intramolecular chaperones.

21 January 2018

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Characterization of FimC, a periplasmic assembly factor for biogenesis of type 1 pili in Escherichia coli

21 January 2018

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A PCR-based strategy for extensive mutagenesis of a target DNA sequence

21 January 2018

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PubMed

https://pubmed.ncbi.nlm.nih.gov/11792867

inferred from PubMed ID database lookup

12 December 2020

based on heuristic

The Immunoglobulin Fold

1 reference

PubMed

https://pubmed.ncbi.nlm.nih.gov/11792867

inferred from PubMed ID database lookup

12 December 2020

based on heuristic

Identifiers

DOI

10.1073/PNAS.022649599

1 reference

29 July 2017

0 references

1 reference

29 July 2017

1 reference