oleic acid and guanidine

oleic acid has been researched along with guanidine in 2 studies

Research

Studies (2)

Timeframe	Studies, this research(%)	All Research%
pre-1990	0 (0.00)	18.7374
1990's	0 (0.00)	18.2507
2000's	1 (50.00)	29.6817
2010's	1 (50.00)	24.3611
2020's	0 (0.00)	2.80

Authors

Authors	Studies
Cistola, DP; Dekoster, GT; Ogbay, B	1
Hansted, JG; Nielsen, SB; Otzen, DE; Pedersen, LR; Petersen, TE; Sørensen, ES	1

Other Studies

2 other study(ies) available for oleic acid and guanidine

Article	Year
The NMR structure of a stable and compact all-beta-sheet variant of intestinal fatty acid-binding protein. Protein science : a publication of the Protein Society, 2004, Volume: 13, Issue:5 Topics: Carrier Proteins; Fatty Acid-Binding Proteins; Guanidine; Nuclear Magnetic Resonance, Biomolecular; Oleic Acid; Protein Binding; Protein Denaturation; Protein Structure, Secondary; Spectrometry, Fluorescence; Urea	2004
PP3 forms stable tetrameric structures through hydrophobic interactions via the C-terminal amphipathic helix and undergoes reversible thermal dissociation and denaturation. The FEBS journal, 2012, Volume: 279, Issue:2 Topics: Animals; Anisotropy; Caseins; Cattle; Circular Dichroism; Dimerization; Fluorescence Polarization; Fractionation, Field Flow; Glucosides; Glycoproteins; Guanidine; Hot Temperature; Hydrogen-Ion Concentration; Milk Proteins; Molecular Weight; Oleic Acid; Peptide Fragments; Protein Denaturation; Protein Interaction Domains and Motifs; Protein Refolding; Surface-Active Agents	2012

Article

Year

The NMR structure of a stable and compact all-beta-sheet variant of intestinal fatty acid-binding protein.

Protein science : a publication of the Protein Society, 2004, Volume: 13, Issue:5

Topics: Carrier Proteins; Fatty Acid-Binding Proteins; Guanidine; Nuclear Magnetic Resonance, Biomolecular; Oleic Acid; Protein Binding; Protein Denaturation; Protein Structure, Secondary; Spectrometry, Fluorescence; Urea

2004

PP3 forms stable tetrameric structures through hydrophobic interactions via the C-terminal amphipathic helix and undergoes reversible thermal dissociation and denaturation.

The FEBS journal, 2012, Volume: 279, Issue:2

Topics: Animals; Anisotropy; Caseins; Cattle; Circular Dichroism; Dimerization; Fluorescence Polarization; Fractionation, Field Flow; Glucosides; Glycoproteins; Guanidine; Hot Temperature; Hydrogen-Ion Concentration; Milk Proteins; Molecular Weight; Oleic Acid; Peptide Fragments; Protein Denaturation; Protein Interaction Domains and Motifs; Protein Refolding; Surface-Active Agents

2012