(Q47295572)

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Effect of mobile phase on the oligomerization state of alpha-helical coiled-coil peptides during high-performance size-exclusion chromatography

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Europe PubMed Central

PubMed publication ID

13 January 2018

http://europepmc.org/abstract/MED/9463895

Effect of mobile phase on the oligomerization state of alpha-helical coiled-coil peptides during high-performance size-exclusion chromatography (English)

1 reference

Europe PubMed Central

PubMed publication ID

13 January 2018

http://europepmc.org/abstract/MED/9463895

1

1 reference

Europe PubMed Central

PubMed publication ID

13 January 2018

http://europepmc.org/abstract/MED/9463895

2

1 reference

Europe PubMed Central

PubMed publication ID

13 January 2018

http://europepmc.org/abstract/MED/9463895

Robert S. Hodges

3

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language of work or name

1 reference

Europe PubMed Central

PubMed publication ID

13 January 2018

http://europepmc.org/abstract/MED/9463895

publication date

1 December 1997

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Europe PubMed Central

PubMed publication ID

13 January 2018

http://europepmc.org/abstract/MED/9463895

number of pages

14

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based on heuristic

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Journal of Chromatography

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Europe PubMed Central

PubMed publication ID

13 January 2018

http://europepmc.org/abstract/MED/9463895

791

1 reference

Europe PubMed Central

PubMed publication ID

13 January 2018

http://europepmc.org/abstract/MED/9463895

1-2

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Europe PubMed Central

PubMed publication ID

13 January 2018

http://europepmc.org/abstract/MED/9463895

85-98

1 reference

Europe PubMed Central

PubMed publication ID

13 January 2018

http://europepmc.org/abstract/MED/9463895

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1 reference

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

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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

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

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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

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Preferential Heterodimeric Parallel Coiled-coil Formation by Synthetic Max and c-Myc Leucine Zippers: A Description of Putative Electrostatic Interactions Responsible for the Specificity of Heterodimerization

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Formation of parallel and antiparallel coiled-coils controlled by the relative positions of alanine residues in the hydrophobic core

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7 January 2021

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

1 reference

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7 January 2021

The relative positions of alanine residues in the hydrophobic core control the formation of two-stranded or four-stranded α-helical coiled-coils

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7 January 2021

Engineering a de novo-designed coiled-coil heterodimerization domain off the rapid detection, purification and characterization of recombinantly expressed peptides and proteins.

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Kinetic study on the formation of a de novo designed heterodimeric coiled-coil: use of surface plasmon resonance to monitor the association and dissociation of polypeptide chains

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Use of a conformationally restricted secondary structural element to display peptide libraries: a two-stranded alpha-helical coiled-coil stabilized by lactam bridges

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7 January 2021

Characterization of a new four-chain coiled-coil: influence of chain length on stability

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Lactam bridge stabilization of alpha-helices: the role of hydrophobicity in controlling dimeric versus monomeric alpha-helices

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7 January 2021

Analysis of peptides by high-performance liquid chromatography

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Size-exclusion high-performance liquid chromatography of peptides. Requirement for peptide standards to monitor column performance and non-ideal behaviour

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Effect of the alpha-amino group on peptide retention behaviour in reversed-phase chromatography. Determination of the pK(a) values of the alpha-amino group of 19 different N-terminal amino acid residues

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

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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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Relationship of sidechain hydrophobicity and alpha-helical propensity on the stability of the single-stranded amphipathic alpha-helix

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Helix stabilization by Glu-...Lys+ salt bridges in short peptides of de novo design

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Effect of amino acid ion pairs on peptide helicity

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10.1016/S0021-9673(97)00767-X

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Europe PubMed Central

PubMed publication ID

13 January 2018

http://europepmc.org/abstract/MED/9463895

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Europe PubMed Central

PubMed publication ID

13 January 2018

http://europepmc.org/abstract/MED/9463895

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