(Q74567671)

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The use of sodium dodecyl sulfate to model the apolipoprotein environment. Evidence for peptide-SDS complexes using pulsed-field-gradient NMR spectroscopy

scientific article published on 01 May 1998

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scholarly article

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11 November 2019

The use of sodium dodecyl sulfate to model the apolipoprotein environment. Evidence for peptide-SDS complexes using pulsed-field-gradient NMR spectroscopy (English)

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https://www.ebi.ac.uk/europepmc/webservices/rest/search?query=EXT_ID:9593844%20AND%20SRC:MED&resulttype=core&format=json

11 November 2019

NMR spectroscopy

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11 November 2019

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A Rozek

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11 November 2019

D W Hoyt

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11 November 2019

R J Cushley

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11 November 2019

M A Kennedy

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1 May 1998

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11 November 2019

Biochimica et Biophysica Acta

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11 November 2019

1392

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11 November 2019

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11 November 2019

101-108

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11 November 2019

Molecular weight estimation of polypeptide chains by electrophoresis in SDS-polyacrylamide gels

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Solubilization of membranes by detergents

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Characterization of membrane proteins in detergent solutions

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Use of fully deuterated micelles for conformational studies of membrane proteins by high resolution 1H nuclear magnetic resonance

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Methods to study membrane protein structure in solution

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Conformation of two peptides corresponding to human apolipoprotein C-I residues 7-24 and 35-53 in the presence of sodium dodecyl sulfate by CD and NMR spectroscopy

1 reference

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Conformational studies of the N-terminal lipid-associating domain of human apolipoprotein C-I by CD and 1H NMR spectroscopy

1 reference

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Conformational studies of an amphipathic peptide corresponding to human apolipoprotein A-II residues 18-30 with a C-terminal lipid binding motif EWLNS

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Conformation of human serum apolipoprotein A-I(166-185) in the presence of sodium dodecyl sulfate or dodecylphosphocholine by 1H-NMR and CD. Evidence for specific peptide-SDS interactions

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A molecular model of high density lipoproteins

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Structure of human serum lipoproteins inferred from compositional analysis

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Recombinant lipoproteins: implications for structure and assembly of native lipoproteins

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7 January 2021

Spin Diffusion Measurements: Spin Echoes in the Presence of a Time-Dependent Field Gradient

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Measuring protein self-association using pulsed-field-gradient NMR spectroscopy: application to myosin light chain 2

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A pulsed-field gradient NMR study of bovine pancreatic trypsin inhibitor self-association

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Two-dimensional 1H-NMR of transmembrane peptides from Escherichia coli phosphatidylglycerophosphate synthase in micelles.

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Automated chemical synthesis of a protein growth factor for hemopoietic cells, interleukin-3.

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NMR studies of the influence of dodecyl sulfate on the amide hydrogen exchange kinetics of a micelle-solubilized hydrophobic tripeptide

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A general method for the preparation of mixed micelles of hydrophobic peptides and sodium dodecyl sulphate

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Hydrodynamics and protein hydration

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Conformational studies of human [15-2-aminohexanoic acid]little gastrin in sodium dodecyl sulfate micelles by 1H NMR.

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NMR study of the solution conformation of rat atrial natriuretic factor 7-23 in sodium dodecyl sulfate micelles

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Evidence for Sodium Dodecyl Sulfate/Protein Complexes Adopting a Necklace Structure

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Use of nile red as a fluorescent probe for the study of the hydrophobic properties of protein-sodium dodecyl sulfate complexes in solution.

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Conformational and associative behaviours of the third helix of antennapedia homeodomain in membrane-mimetic environments

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Micelle Formation by Bile Salts

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Lipid-protein interactions in the plasma lipoproteins

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Identifiers

10.1016/S0005-2760(98)00028-9

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Europe PubMed Central

PubMed publication ID

https://www.ebi.ac.uk/europepmc/webservices/rest/search?query=EXT_ID:9593844%20AND%20SRC:MED&resulttype=core&format=json

11 November 2019

PubMed publication ID

1 reference

Europe PubMed Central

PubMed publication ID

https://www.ebi.ac.uk/europepmc/webservices/rest/search?query=EXT_ID:9593844%20AND%20SRC:MED&resulttype=core&format=json

11 November 2019

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