alanine and n-(3-pyrene)maleimide

alanine has been researched along with n-(3-pyrene)maleimide in 4 studies

Research

Studies (4)

TimeframeStudies, this research(%)All Research%
pre-19900 (0.00)18.7374
1990's0 (0.00)18.2507
2000's4 (100.00)29.6817
2010's0 (0.00)24.3611
2020's0 (0.00)2.80

Authors

AuthorsStudies
Beena, K; Panse, VG; Philipp, R; Trommer, WE; Varadarajan, R; Vogel, PD1
Bigelow, DJ; Li, J; Squier, TC; Xiong, Y1
Bigelow, DJ; Li, J; Squier, TC1
Cass, CE; Eriksson, S; Mani, RS; Usova, EV1

Other Studies

4 other study(ies) available for alanine and n-(3-pyrene)maleimide

ArticleYear
Electron spin resonance and fluorescence studies of the bound-state conformation of a model protein substrate to the chaperone SecB.
    The Journal of biological chemistry, 2001, Sep-07, Volume: 276, Issue:36

    Topics: Alanine; Amino Acid Sequence; Animals; Aprotinin; Bacterial Proteins; Binding Sites; Cattle; Electron Spin Resonance Spectroscopy; Escherichia coli; Fluorescent Dyes; Hydrogen-Ion Concentration; Kinetics; Maleimides; Molecular Sequence Data; Protein Binding; Protein Conformation; Protein Folding; Spectrometry, Fluorescence; Spin Labels; Temperature

2001
Phospholamban binds in a compact and ordered conformation to the Ca-ATPase.
    Biochemistry, 2004, Jan-20, Volume: 43, Issue:2

    Topics: Alanine; Amino Acid Sequence; Animals; Calcium-Binding Proteins; Calcium-Transporting ATPases; Cysteine; Cytosol; Fluorescence Polarization; Fluorescence Resonance Energy Transfer; Maleimides; Membrane Lipids; Models, Molecular; Molecular Sequence Data; Mutagenesis, Site-Directed; Protein Binding; Protein Conformation; Protein Structure, Tertiary; Rabbits

2004
Conformational changes within the cytosolic portion of phospholamban upon release of Ca-ATPase inhibition.
    Biochemistry, 2004, Apr-06, Volume: 43, Issue:13

    Topics: Alanine; Amino Acid Sequence; Animals; Calcium; Calcium-Binding Proteins; Calcium-Transporting ATPases; Cyclic AMP-Dependent Protein Kinases; Cysteine; Cytosol; Enzyme Activation; Enzyme Inhibitors; Fluorescence Polarization; Fluorescence Resonance Energy Transfer; Maleimides; Molecular Sequence Data; Muscle Fibers, Fast-Twitch; Mutagenesis, Site-Directed; Phosphorylation; Protein Conformation; Protein Structure, Tertiary; Rabbits

2004
Fluorescence energy transfer studies of human deoxycytidine kinase: role of cysteine 185 in the conformational changes that occur upon substrate binding.
    Biochemistry, 2006, Mar-21, Volume: 45, Issue:11

    Topics: Alanine; Binding Sites; Cysteine; Deoxycytidine Kinase; Energy Transfer; Enzyme Activation; Fluorescence Resonance Energy Transfer; Fluorescent Dyes; Humans; Kinetics; Maleimides; Models, Molecular; Mutagenesis, Site-Directed; Mutation; Nucleosides; Phosphates; Protein Binding; Protein Conformation; Substrate Specificity; Tryptophan

2006