Positional dependence of the effects of negatively charged Glu side chains on the stability of two-stranded α-helical coiled-coils (Q73527610)

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4 November 2019

title

Positional dependence of the effects of negatively charged Glu side chains on the stability of two-stranded alpha-helical coiled-coils (English)

1 reference

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4 November 2019

Positional dependence of the effects of negatively charged Glu side chains on the stability of two-stranded α-helical coiled-coils (English)

1 reference

10.1002/(SICI)1099-1387(199705)3:3<209::AID-PSC102>3.0.CO;2-S

https://api.crossref.org/works/10.1002/(SICI)1099-1387(199705)3:3%3C209::AID-PSC102%3E3.0.CO;2-S

protein secondary structure

8 November 2024

main subject

1 reference

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8 November 2024

author name string

W. D. Kohn

1

1 reference

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8 November 2024

C. M. Kay

2

1 reference

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8 November 2024

R. S. Hodges

3

1 reference

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8 November 2024

language of work or name

English

1 reference

National Center for Biotechnology Information

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/esummary.fcgi?db=pubmed&retmode=json&id=9230486

8 November 2024

publication date

1 May 1997

1 reference

https://www.ebi.ac.uk/europepmc/webservices/rest/search?query=EXT_ID:9230486%20AND%20SRC:MED&resulttype=core&format=json

4 November 2019

May 1997

1 reference

National Center for Biotechnology Information

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/esummary.fcgi?db=pubmed&retmode=json&id=9230486

full work available at URL

8 November 2024

number of pages

15

1 reference

based on heuristic

inferred from page(s)

https://api.wiley.com/onlinelibrary/tdm/v1/articles/10.1002%2F(SICI)1099-1387(199705)3:3%3C209::AID-PSC102%3E3.0.CO;2-S

1 reference

10.1002/(SICI)1099-1387(199705)3:3<209::AID-PSC102>3.0.CO;2-S

https://api.crossref.org/works/10.1002/(SICI)1099-1387(199705)3:3%3C209::AID-PSC102%3E3.0.CO;2-S

https://onlinelibrary.wiley.com/doi/full/10.1002/(SICI)1099-1387(199705)3:3%3C209::AID-PSC102%3E3.0.CO;2-S

8 November 2024

1 reference

10.1002/(SICI)1099-1387(199705)3:3<209::AID-PSC102>3.0.CO;2-S

https://api.crossref.org/works/10.1002/(SICI)1099-1387(199705)3:3%3C209::AID-PSC102%3E3.0.CO;2-S

Journal of Peptide Science

8 November 2024

published in

1 reference

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4 November 2019

volume

3

1 reference

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4 November 2019

issue

3

1 reference

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4 November 2019

page(s)

209-223

1 reference

https://www.ebi.ac.uk/europepmc/webservices/rest/search?query=EXT_ID:9230486%20AND%20SRC:MED&resulttype=core&format=json

The pKa values of two histidine residues in human haemoglobin, the Bohr effect, and the dipole moments of α-helices

4 November 2019

cites work

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5 June 2022

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Hydrogen-bond geometry in organic crystals

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Letter: Mechanisms of protein and polypeptide helix initiation

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Conformational parameters for amino acids in helical, beta-sheet, and random coil regions calculated from proteins

8 November 2024

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Amino acid preferences for specific locations at the ends of alpha helices

8 November 2024

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Helix signals in proteins

8 November 2024

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N‐ and C‐capping preferences for all 20 amino acids in α‐helical peptides

8 November 2024

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Capping interactions in isolated alpha helices: position-dependent substitution effects and structure of a serine-capped peptide helix

8 November 2024

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Capping and alpha-helix stability

8 November 2024

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10.1002/(SICI)1099-1387(199705)3:3<209::AID-PSC102>3.0.CO;2-S

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Alpha helix capping in synthetic model peptides by reciprocal side chain-main chain interactions: evidence for an N terminal "capping box"

8 November 2024

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10.1002/(SICI)1099-1387(199705)3:3<209::AID-PSC102>3.0.CO;2-S

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The alpha-helix dipole and the properties of proteins

8 November 2024

11

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Dipoles localized at helix termini of proteins stabilize charges

8 November 2024

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Sulphate sequestered in the sulphate-binding protein of Salmonella typhimurium is bound solely by hydrogen bonds

8 November 2024

13

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10.1002/(SICI)1099-1387(199705)3:3<209::AID-PSC102>3.0.CO;2-S

https://api.crossref.org/works/10.1002/(SICI)1099-1387(199705)3:3%3C209::AID-PSC102%3E3.0.CO;2-S

Helix-capping interaction in lambda Cro protein: a free energy simulation analysis.

8 November 2024

14

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10.1002/(SICI)1099-1387(199705)3:3<209::AID-PSC102>3.0.CO;2-S

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Nature of the charged-group effect on the stability of the C-peptide helix

8 November 2024

15

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10.1002/(SICI)1099-1387(199705)3:3<209::AID-PSC102>3.0.CO;2-S

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

8 November 2024

16

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10.1002/(SICI)1099-1387(199705)3:3<209::AID-PSC102>3.0.CO;2-S

https://api.crossref.org/works/10.1002/(SICI)1099-1387(199705)3:3%3C209::AID-PSC102%3E3.0.CO;2-S

Further studies of the helix dipole model: effects of a free alpha-NH3+ or alpha-COO- group on helix stability

8 November 2024

17

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10.1002/(SICI)1099-1387(199705)3:3<209::AID-PSC102>3.0.CO;2-S

https://api.crossref.org/works/10.1002/(SICI)1099-1387(199705)3:3%3C209::AID-PSC102%3E3.0.CO;2-S

Comparison of alpha-helix stability in peptides having a negatively or positively charged residue block attached either to the N- or C-terminus of an alpha-helix: the electrostatic contribution and anisotropic stability of the alpha-helix

8 November 2024

18

1 reference

10.1002/(SICI)1099-1387(199705)3:3<209::AID-PSC102>3.0.CO;2-S

https://api.crossref.org/works/10.1002/(SICI)1099-1387(199705)3:3%3C209::AID-PSC102%3E3.0.CO;2-S

Electrostatic screening of charge and dipole interactions with the helix backbone

8 November 2024

19

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10.1002/(SICI)1099-1387(199705)3:3<209::AID-PSC102>3.0.CO;2-S

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Charged histidine affects alpha-helix stability at all positions in the helix by interacting with the backbone charges

8 November 2024

20

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10.1002/(SICI)1099-1387(199705)3:3<209::AID-PSC102>3.0.CO;2-S

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Effect of a single aspartate on helix stability at different positions in a neutral alanine-based peptide

8 November 2024

21

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10.1002/(SICI)1099-1387(199705)3:3<209::AID-PSC102>3.0.CO;2-S

https://api.crossref.org/works/10.1002/(SICI)1099-1387(199705)3:3%3C209::AID-PSC102%3E3.0.CO;2-S

Structural studies on peptides corresponding to mutants of the major alpha-helix of barnase

8 November 2024

22

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10.1002/(SICI)1099-1387(199705)3:3<209::AID-PSC102>3.0.CO;2-S

https://api.crossref.org/works/10.1002/(SICI)1099-1387(199705)3:3%3C209::AID-PSC102%3E3.0.CO;2-S

Stabilization of protein structure by interaction of alpha-helix dipole with a charged side chain

8 November 2024

23

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10.1002/(SICI)1099-1387(199705)3:3<209::AID-PSC102>3.0.CO;2-S

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Enhanced protein thermostability from designed mutations that interact with alpha-helix dipoles

8 November 2024

24

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10.1002/(SICI)1099-1387(199705)3:3<209::AID-PSC102>3.0.CO;2-S

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Analysis of the interaction between charged side chains and the alpha-helix dipole using designed thermostable mutants of phage T4 lysozyme

8 November 2024

25

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10.1002/(SICI)1099-1387(199705)3:3<209::AID-PSC102>3.0.CO;2-S

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Increasing the thermostability of a neutral protease by replacing positively charged amino acids in the N-terminal turn of alpha-helices

8 November 2024

26

1 reference

10.1002/(SICI)1099-1387(199705)3:3<209::AID-PSC102>3.0.CO;2-S

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Histidine residues at the N- and C-termini of alpha-helices: perturbed pKas and protein stability

8 November 2024

27

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10.1002/(SICI)1099-1387(199705)3:3<209::AID-PSC102>3.0.CO;2-S

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Large differences in the helix propensities of alanine and glycine

8 November 2024

28

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10.1002/(SICI)1099-1387(199705)3:3<209::AID-PSC102>3.0.CO;2-S

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Peptide models of protein folding initiation sites. 1. Secondary structure formation by peptides corresponding to the G- and H-helices of myoglobin

8 November 2024

29

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The two-stranded alpha-helical coiled-coil is an ideal model for studying protein stability and subunit interactions

8 November 2024

31

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

8 November 2024

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

8 November 2024

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

8 November 2024

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

8 November 2024

36

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Thermodynamic characterization of the structural stability of the coiled-coil region of the bZIP transcription factor GCN4.

8 November 2024

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

8 November 2024

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Circular dichroism study on the conformational stability of the dimerization domain of transcription factor LFB1

8 November 2024

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Determination and analysis of urea and guanidine hydrochloride denaturation curves

8 November 2024

40

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Contributions of the polar, uncharged amino acids to the stability of staphylococcal nuclease: evidence for mutational effects on the free energy of the denatured state.

8 November 2024

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https://api.crossref.org/works/10.1002/(SICI)1099-1387(199705)3:3%3C209::AID-PSC102%3E3.0.CO;2-S

Tropomyosin coiled-coil interactions: Evidence for an unstaggered structure

8 November 2024

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https://api.crossref.org/works/10.1002/(SICI)1099-1387(199705)3:3%3C209::AID-PSC102%3E3.0.CO;2-S

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

8 November 2024

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The role of interhelical ionic interactions in controlling protein folding and stability. De novo designed synthetic two-stranded alpha-helical coiled-coils

8 November 2024

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https://api.crossref.org/works/10.1002/(SICI)1099-1387(199705)3:3%3C209::AID-PSC102%3E3.0.CO;2-S

Disulfide bond contribution to protein stability: positional effects of substitution in the hydrophobic core of the two-stranded alpha-helical coiled-coil

8 November 2024

45

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10.1002/(SICI)1099-1387(199705)3:3<209::AID-PSC102>3.0.CO;2-S

https://api.crossref.org/works/10.1002/(SICI)1099-1387(199705)3:3%3C209::AID-PSC102%3E3.0.CO;2-S

The net energetic contribution of interhelical electrostatic attractions to coiled-coil stability

8 November 2024

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https://api.crossref.org/works/10.1002/(SICI)1099-1387(199705)3:3%3C209::AID-PSC102%3E3.0.CO;2-S

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

8 November 2024

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Prediction of peptide retention times in reversed-phase high-performance liquid chromatography I. Determination of retention coefficients of amino acid residues of model synthetic peptides

8 November 2024

51

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10.1002/(SICI)1099-1387(199705)3:3<209::AID-PSC102>3.0.CO;2-S

https://api.crossref.org/works/10.1002/(SICI)1099-1387(199705)3:3%3C209::AID-PSC102%3E3.0.CO;2-S

Reversed-phase chromatography of synthetic amphipathic α-helical peptides as a model for ligand/receptor interactions Effect of changing hydrophobic environment on the relative hydrophilicity/hydrophobicity of amino acid side-chains

8 November 2024

52

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10.1002/(SICI)1099-1387(199705)3:3<209::AID-PSC102>3.0.CO;2-S

https://api.crossref.org/works/10.1002/(SICI)1099-1387(199705)3:3%3C209::AID-PSC102%3E3.0.CO;2-S

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

8 November 2024

53

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10.1002/(SICI)1099-1387(199705)3:3<209::AID-PSC102>3.0.CO;2-S

https://api.crossref.org/works/10.1002/(SICI)1099-1387(199705)3:3%3C209::AID-PSC102%3E3.0.CO;2-S

Construction, purification, and characterization of a hybrid protein comprising the DNA binding domain of the LexA repressor and the Jun leucine zipper: a circular dichroism and mutagenesis study

8 November 2024

54

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10.1002/(SICI)1099-1387(199705)3:3<209::AID-PSC102>3.0.CO;2-S

https://api.crossref.org/works/10.1002/(SICI)1099-1387(199705)3:3%3C209::AID-PSC102%3E3.0.CO;2-S

Effect of the substitution Ala----Gly at each of five residue positions in the C-peptide helix

8 November 2024

56

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10.1002/(SICI)1099-1387(199705)3:3<209::AID-PSC102>3.0.CO;2-S

https://api.crossref.org/works/10.1002/(SICI)1099-1387(199705)3:3%3C209::AID-PSC102%3E3.0.CO;2-S

Synthetic model proteins: the relative contribution of leucine residues at the nonequivalent positions of the 3-4 hydrophobic repeat to the stability of the two-stranded alpha-helical coiled-coil

8 November 2024

58

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10.1002/(SICI)1099-1387(199705)3:3<209::AID-PSC102>3.0.CO;2-S

https://api.crossref.org/works/10.1002/(SICI)1099-1387(199705)3:3%3C209::AID-PSC102%3E3.0.CO;2-S

Do salt bridges stabilize proteins? A continuum electrostatic analysis.

8 November 2024

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10.1002/(SICI)1099-1387(199705)3:3<209::AID-PSC102>3.0.CO;2-S

https://api.crossref.org/works/10.1002/(SICI)1099-1387(199705)3:3%3C209::AID-PSC102%3E3.0.CO;2-S

Journal of Biological Chemistry

8 November 2024

60

268

1993

Monera

1921

1 reference

10.1002/(SICI)1099-1387(199705)3:3<209::AID-PSC102>3.0.CO;2-S

https://api.crossref.org/works/10.1002/(SICI)1099-1387(199705)3:3%3C209::AID-PSC102%3E3.0.CO;2-S

The thermal denaturation of nonpolymerizable alpha alpha-tropomyosin and its segments as a function of ionic strength

8 November 2024

62

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10.1002/(SICI)1099-1387(199705)3:3<209::AID-PSC102>3.0.CO;2-S

https://api.crossref.org/works/10.1002/(SICI)1099-1387(199705)3:3%3C209::AID-PSC102%3E3.0.CO;2-S

Destabilization of an alpha-helix-bundle protein by helix dipoles

8 November 2024

64

1 reference

10.1002/(SICI)1099-1387(199705)3:3<209::AID-PSC102>3.0.CO;2-S

https://api.crossref.org/works/10.1002/(SICI)1099-1387(199705)3:3%3C209::AID-PSC102%3E3.0.CO;2-S

Electrostatic interactions in globular proteins. Different dielectric models applied to the packing of alpha-helices

8 November 2024

65

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10.1002/(SICI)1099-1387(199705)3:3<209::AID-PSC102>3.0.CO;2-S

https://api.crossref.org/works/10.1002/(SICI)1099-1387(199705)3:3%3C209::AID-PSC102%3E3.0.CO;2-S

Electrostatic stabilization in four-helix bundle proteins

8 November 2024

66

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10.1002/(SICI)1099-1387(199705)3:3<209::AID-PSC102>3.0.CO;2-S

https://api.crossref.org/works/10.1002/(SICI)1099-1387(199705)3:3%3C209::AID-PSC102%3E3.0.CO;2-S

Helical peptides with three pairs of Asp-Arg and Glu-Arg residues in different orientations and spacings

8 November 2024

67

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10.1002/(SICI)1099-1387(199705)3:3<209::AID-PSC102>3.0.CO;2-S

https://api.crossref.org/works/10.1002/(SICI)1099-1387(199705)3:3%3C209::AID-PSC102%3E3.0.CO;2-S

Contribution to global protein stabilization of the N-capping box in human growth hormone

8 November 2024

70

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10.1002/(SICI)1099-1387(199705)3:3<209::AID-PSC102>3.0.CO;2-S

https://api.crossref.org/works/10.1002/(SICI)1099-1387(199705)3:3%3C209::AID-PSC102%3E3.0.CO;2-S

The energetics of ion-pair and hydrogen-bonding interactions in a helical peptide

8 November 2024

71

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10.1002/(SICI)1099-1387(199705)3:3<209::AID-PSC102>3.0.CO;2-S

https://api.crossref.org/works/10.1002/(SICI)1099-1387(199705)3:3%3C209::AID-PSC102%3E3.0.CO;2-S

Measurement of interhelical electrostatic interactions in the GCN4 leucine zipper

8 November 2024

73

1 reference

10.1002/(SICI)1099-1387(199705)3:3<209::AID-PSC102>3.0.CO;2-S

https://api.crossref.org/works/10.1002/(SICI)1099-1387(199705)3:3%3C209::AID-PSC102%3E3.0.CO;2-S

Interhelical Salt Bridges, Coiled-Coil Stability, and Specificity of Dimerization

8 November 2024

74

1 reference

10.1002/(SICI)1099-1387(199705)3:3<209::AID-PSC102>3.0.CO;2-S

https://api.crossref.org/works/10.1002/(SICI)1099-1387(199705)3:3%3C209::AID-PSC102%3E3.0.CO;2-S

Helix capping propensities in peptides parallel those in proteins

8 November 2024

75

1 reference

10.1002/(SICI)1099-1387(199705)3:3<209::AID-PSC102>3.0.CO;2-S

https://api.crossref.org/works/10.1002/(SICI)1099-1387(199705)3:3%3C209::AID-PSC102%3E3.0.CO;2-S

Boehringer Mannheim award lecture 1995. La conference Boehringer Mannheim 1995. De novo design of alpha-helical proteins: basic research to medical applications

8 November 2024

77

1 reference

10.1002/(SICI)1099-1387(199705)3:3<209::AID-PSC102>3.0.CO;2-S

https://api.crossref.org/works/10.1002/(SICI)1099-1387(199705)3:3%3C209::AID-PSC102%3E3.0.CO;2-S

Miniantibodies: use of amphipathic helices to produce functional, flexibly linked dimeric FV fragments with high avidity in Escherichia coli

8 November 2024

79

1 reference

10.1002/(SICI)1099-1387(199705)3:3<209::AID-PSC102>3.0.CO;2-S

https://api.crossref.org/works/10.1002/(SICI)1099-1387(199705)3:3%3C209::AID-PSC102%3E3.0.CO;2-S

Stabilization of proteins by rational design of alpha-helix stability using helix/coil transition theory.

8 November 2024

80

1 reference

10.1002/(SICI)1099-1387(199705)3:3<209::AID-PSC102>3.0.CO;2-S

https://api.crossref.org/works/10.1002/(SICI)1099-1387(199705)3:3%3C209::AID-PSC102%3E3.0.CO;2-S

8 November 2024

Identifiers

10.1002/(SICI)1099-1387(199705)3:3<209::AID-PSC102>3.0.CO;2-S

1 reference

National Center for Biotechnology Information

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/esummary.fcgi?db=pubmed&retmode=json&id=9230486

8 November 2024

1 reference