proline and dimyristoylphosphatidylcholine

proline has been researched along with dimyristoylphosphatidylcholine in 4 studies

Research

Studies (4)

TimeframeStudies, this research(%)All Research%
pre-19902 (50.00)18.7374
1990's1 (25.00)18.2507
2000's0 (0.00)29.6817
2010's1 (25.00)24.3611
2020's0 (0.00)2.80

Authors

AuthorsStudies
Gotto, AM; Hester, L; Ponsin, G; Pownall, HJ; Sparrow, JT1
Cramer, WA; Dankert, JR; Grabau, C; Hermodson, M; Uratani, Y1
Woolf, TB1
Bessonov, K; Harauz, G; Vassall, KA1

Other Studies

4 other study(ies) available for proline and dimyristoylphosphatidylcholine

ArticleYear
Lipid-peptide association and activation of lecithin:cholesterol acyltransferase. Effect of alpha-helicity.
    The Journal of biological chemistry, 1986, Jul-15, Volume: 261, Issue:20

    Topics: Amino Acid Sequence; Apolipoproteins; Circular Dichroism; Dimyristoylphosphatidylcholine; Enzyme Activation; Lipid Metabolism; Lipids; Lipoproteins, HDL; Phosphatidylcholine-Sterol O-Acyltransferase; Phosphatidylcholines; Proline; Protein Conformation; Spectrometry, Fluorescence; Structure-Activity Relationship

1986
On a domain structure of colicin E1. A COOH-terminal peptide fragment active in membrane depolarization.
    The Journal of biological chemistry, 1982, Apr-10, Volume: 257, Issue:7

    Topics: Amino Acid Sequence; Amino Acids; Biological Transport; Cell Membrane; Circular Dichroism; Colicins; Dimyristoylphosphatidylcholine; Escherichia coli; Kinetics; Liposomes; Molecular Weight; Peptide Fragments; Phosphatidylcholines; Proline; Trypsin

1982
Molecular dynamics of individual alpha-helices of bacteriorhodopsin in dimyristol phosphatidylocholine. I. Structure and dynamics.
    Biophysical journal, 1997, Volume: 73, Issue:5

    Topics: Amino Acid Sequence; Bacteriorhodopsins; Computer Simulation; Dimyristoylphosphatidylcholine; Hydrogen Bonding; Lipid Bilayers; Liposomes; Models, Molecular; Molecular Sequence Data; Proline; Protein Structure, Secondary; Software; Tryptophan; Tyrosine

1997
Docking and molecular dynamics simulations of the Fyn-SH3 domain with free and phospholipid bilayer-associated 18.5-kDa myelin basic protein (MBP)-Insights into a noncanonical and fuzzy interaction.
    Proteins, 2017, Volume: 85, Issue:7

    Topics: Amino Acid Sequence; Animals; Binding Sites; Dimyristoylphosphatidylcholine; Humans; Lipid Bilayers; Mice; Molecular Docking Simulation; Molecular Dynamics Simulation; Myelin Basic Protein; Peptides; Phosphorylcholine; Proline; Protein Binding; Protein Conformation, alpha-Helical; Protein Conformation, beta-Strand; Protein Structure, Tertiary; Proto-Oncogene Proteins c-fyn; src Homology Domains; Thermodynamics; Unithiol; Water

2017