proline and phosphoglycolate

proline has been researched along with phosphoglycolate in 3 studies

Research

Studies (3)

TimeframeStudies, this research(%)All Research%
pre-19900 (0.00)18.7374
1990's1 (33.33)18.2507
2000's2 (66.67)29.6817
2010's0 (0.00)24.3611
2020's0 (0.00)2.80

Authors

AuthorsStudies
Delboni, LF; Hol, WG; Mainfroid, V; Mande, SC; Martial, JA; Rentier-Delrue, F; Turley, S; Vellieux, FM1
Cabrera, N; de Gómez-Puyou, MT; Gómez-Puyou, A; Hernández-Alcantara, G; López-Velazquez, G; Pérez-Montfort, R; Reyes-Vivas, H1
Kursula, I; Wierenga, RK1

Other Studies

3 other study(ies) available for proline and phosphoglycolate

ArticleYear
Crystal structure of recombinant triosephosphate isomerase from Bacillus stearothermophilus. An analysis of potential thermostability factors in six isomerases with known three-dimensional structures points to the importance of hydrophobic interactions.
    Protein science : a publication of the Protein Society, 1995, Volume: 4, Issue:12

    Topics: Amino Acid Sequence; Binding Sites; Binding, Competitive; Chemical Phenomena; Chemistry, Physical; Crystallization; Crystallography, X-Ray; Enzyme Inhibitors; Enzyme Stability; Geobacillus stearothermophilus; Glycolates; Hot Temperature; Hydrogen Bonding; Models, Molecular; Molecular Sequence Data; Molecular Structure; Proline; Recombinant Proteins; Structure-Activity Relationship; Triose-Phosphate Isomerase

1995
Factors that control the reactivity of the interface cysteine of triosephosphate isomerase from Trypanosoma brucei and Trypanosoma cruzi.
    Biochemistry, 2001, Mar-13, Volume: 40, Issue:10

    Topics: Amino Acid Sequence; Amino Acid Substitution; Animals; Cysteine; Dimerization; Enzyme Activation; Enzyme Inhibitors; Glutamic Acid; Glutamine; Glycolates; Hydrogen-Ion Concentration; Leishmania mexicana; Methyl Methanesulfonate; Molecular Sequence Data; Mutagenesis, Site-Directed; Peptide Fragments; Proline; Protein Structure, Tertiary; Triose-Phosphate Isomerase; Trypanosoma brucei brucei; Trypanosoma cruzi

2001
Crystal structure of triosephosphate isomerase complexed with 2-phosphoglycolate at 0.83-A resolution.
    The Journal of biological chemistry, 2003, Mar-14, Volume: 278, Issue:11

    Topics: Animals; Anisotropy; Binding Sites; Crystallography, X-Ray; Dimerization; Glutamic Acid; Glycolates; Histidine; Hydrogen Bonding; Leishmania mexicana; Models, Chemical; Models, Molecular; Proline; Protein Binding; Protein Conformation; Protein Structure, Tertiary; Protons; Triose-Phosphate Isomerase

2003