(Q71823665)

English

The Effects of Interhelical Electrostatic Repulsions between Glutamic Acid Residues in Controlling the Dimerization and Stability of Two-stranded α-Helical Coiled-coils

scientific article published on October 27, 1995

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scholarly article

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https://www.ebi.ac.uk/europepmc/webservices/rest/search?query=EXT_ID:7592719%20AND%20SRC:MED&resulttype=core&format=json

21 October 2019

The effects of interhelical electrostatic repulsions between glutamic acid residues in controlling the dimerization and stability of two-stranded alpha-helical coiled-coils (English)

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https://www.ebi.ac.uk/europepmc/webservices/rest/search?query=EXT_ID:7592719%20AND%20SRC:MED&resulttype=core&format=json

21 October 2019

The Effects of Interhelical Electrostatic Repulsions between Glutamic Acid Residues in Controlling the Dimerization and Stability of Two-stranded α-Helical Coiled-coils (English)

1 reference

10.1074/JBC.270.43.25495

https://api.crossref.org/works/10.1074/JBC.270.43.25495

31 May 2024

protein secondary structure

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31 May 2024

author name string

W. D. Kohn

1

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31 May 2024

O. D. Monera

2

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31 May 2024

C. M. Kay

3

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31 May 2024

R. S. Hodges

4

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31 May 2024

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publication date

1 October 1995

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21 October 2019

27 October 1995

1 reference

National Center for Biotechnology Information

PubMed publication ID

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/esummary.fcgi?db=pubmed&retmode=json&id=7592719

31 May 2024

full work available at URL

http://www.jbc.org/article/S0021925818923525/pdf

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31 May 2024

https://api.elsevier.com/content/article/PII:S0021925818923525?httpAccept=text/xml

1 reference

10.1074/JBC.270.43.25495

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31 May 2024

https://api.elsevier.com/content/article/PII:S0021925818923525?httpAccept=text/plain

1 reference

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31 May 2024

https://syndication.highwire.org/content/doi/10.1074/jbc.270.43.25495

1 reference

10.1074/JBC.270.43.25495

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Journal of Biological Chemistry

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21 October 2019

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21 October 2019

43

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21 October 2019

25495-25506

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Europe PubMed Central

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21 October 2019

Structure, function and application of the coiled-coil protein folding motif

1

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Structure of the leucine zipper

2

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Genetic analysis of the leucine heptad repeats of Lac repressor: evidence for a 4-helical bundle.

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Molecular weights of glycosylated and nonglycosylated forms of recombinant human stem cell factor determined by low-angle laser light scattering

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Interactions of coiled coils in transcription factors: where is the specificity?

5

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An intermolecular disulfide bond stabilizes E2A homodimers and is required for DNA binding at physiological temperatures

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Helix propensities of the amino acids measured in alanine-based peptides without helix-stabilizing side-chain interactions.

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Determination of the helix and beta form of proteins in aqueous solution by circular dichroism.

11

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Alpha-helical coiled coils and bundles: how to design an alpha-helical protein

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Folding of immunogenic peptide fragments of proteins in water solution. II. The nascent helix

14

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Designed coiled-coil proteins: synthesis and spectroscopy of two 78-residue .alpha.-helical dimers

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Backbone dynamics of a free and phosphopeptide-complexed Src homology 2 domain studied by 15N NMR relaxation

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Mechanism of acid-induced folding of proteins

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Controlled formation of model homo- and heterodimer coiled coil polypeptides

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Conformational intermediates in the folding of a coiled-coil model peptide of the N-terminus of tropomyosin and alpha alpha-tropomyosin

20

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Guanidine hydrochloride-induced folding of proteins

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Comparison of the conformational stability of the molten globule and native states of horse cytochrome c. Effects of acetylation, heat, urea and guanidine-hydrochloride

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A switch between two-, three-, and four-stranded coiled coils in GCN4 leucine zipper mutants

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Unzipping the secrets of coiled-coils

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Reversed-phase liquid chromatography as a useful probe of hydrophobic interactions involved in protein folding and protein stability

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Dipoles of the α-helix and β-sheet: their role in protein folding

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Sequence requirements for coiled-coils: analysis with lambda repressor-GCN4 leucine zipper fusions

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Probing the roles of residues at the e and g positions of the GCN4 leucine zipper by combinatorial mutagenesis.

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Transcriptional regulation by dimerization: two sides to an incestuous relationship

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Solution structure of a polypeptide dimer comprising the fourth calcium-binding site of troponin C by nuclear magnetic resonance spectroscopy

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Protein destabilization by electrostatic repulsions in the two-stranded alpha-helical coiled-coil/leucine zipper

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Salt-dependent properties of proteins from extremely halophilic bacteria

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Synthesis of a model protein of defined secondary and quaternary structure. Effect of chain length on the stabilization and formation of two-stranded alpha-helical coiled-coils

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Preferential assembly of the tropomyosin heterodimer: equilibrium studies

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Assembly of the native heterodimer of Rana esculenta tropomyosin by chain exchange

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Crystal structure of a synthetic triple-stranded alpha-helical bundle

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Measurement of interhelical electrostatic interactions in the GCN4 leucine zipper

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Predicting coiled coils from protein sequences

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Protein interactions with urea and guanidinium chloride. A calorimetric study

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Stabilization of a protein by guanidinium chloride

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Periodic charge distributions in the myosin rod amino acid sequence match cross-bridge spacings in muscle

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Electrostatic interactions control the parallel and antiparallel orientation of alpha-helical chains in two-stranded alpha-helical coiled-coils

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Protein denaturation with guanidine hydrochloride or urea provides a different estimate of stability depending on the contributions of electrostatic interactions

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Guanidine hydrochloride stabilization of a partially unfolded intermediate during the reversible denaturation of protein disulfide isomerase.

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X-ray structure of the GCN4 leucine zipper, a two-stranded, parallel coiled coil

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Determination and analysis of urea and guanidine hydrochloride denaturation curves

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Dimerization of leucine zippers analyzed by random selection

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Identifiers

10.1074/JBC.270.43.25495

1 reference

Europe PubMed Central

PubMed publication ID

https://www.ebi.ac.uk/europepmc/webservices/rest/search?query=EXT_ID:7592719%20AND%20SRC:MED&resulttype=core&format=json

21 October 2019

PubMed publication ID

1 reference

Europe PubMed Central

PubMed publication ID

https://www.ebi.ac.uk/europepmc/webservices/rest/search?query=EXT_ID:7592719%20AND%20SRC:MED&resulttype=core&format=json

21 October 2019

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