Page last updated: 2024-08-17

trifluoroethanol and glucagon-like peptide 1

trifluoroethanol has been researched along with glucagon-like peptide 1 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	2 (100.00)	29.6817
2010's	0 (0.00)	24.3611
2020's	0 (0.00)	2.80

Authors

Authors	Studies
Andersen, NH; Fesinmeyer, RM; Neidigh, JW; Prickett, KS	1
Chang, X; Keller, D; Led, JJ; O'Donoghue, SI	1

Other Studies

2 other study(ies) available for trifluoroethanol and glucagon-like peptide 1

Article	Year
Exendin-4 and glucagon-like-peptide-1: NMR structural comparisons in the solution and micelle-associated states. Biochemistry, 2001, Nov-06, Volume: 40, Issue:44 Topics: Amino Acid Sequence; Binding Sites; Circular Dichroism; Exenatide; Glucagon; Glucagon-Like Peptide 1; Glycine; Humans; Magnetic Resonance Spectroscopy; Molecular Sequence Data; Mutation; Peptide Fragments; Peptides; Phosphatidylcholines; Protein Precursors; Protein Structure, Secondary; Sequence Homology, Amino Acid; Stereoisomerism; Trifluoroethanol; Tryptophan; Venoms	2001
NMR studies of the aggregation of glucagon-like peptide-1: formation of a symmetric helical dimer. FEBS letters, 2002, Mar-27, Volume: 515, Issue:1-3 Topics: Amino Acid Sequence; Diffusion; Dimerization; Glucagon; Glucagon-Like Peptide 1; Hydrogen Bonding; Magnetic Resonance Spectroscopy; Models, Molecular; Molecular Sequence Data; Peptide Fragments; Protein Binding; Protein Conformation; Protein Precursors; Protein Structure, Secondary; Trifluoroethanol; Water	2002

Article

Year

Exendin-4 and glucagon-like-peptide-1: NMR structural comparisons in the solution and micelle-associated states.

Biochemistry, 2001, Nov-06, Volume: 40, Issue:44

Topics: Amino Acid Sequence; Binding Sites; Circular Dichroism; Exenatide; Glucagon; Glucagon-Like Peptide 1; Glycine; Humans; Magnetic Resonance Spectroscopy; Molecular Sequence Data; Mutation; Peptide Fragments; Peptides; Phosphatidylcholines; Protein Precursors; Protein Structure, Secondary; Sequence Homology, Amino Acid; Stereoisomerism; Trifluoroethanol; Tryptophan; Venoms

2001

NMR studies of the aggregation of glucagon-like peptide-1: formation of a symmetric helical dimer.

FEBS letters, 2002, Mar-27, Volume: 515, Issue:1-3

Topics: Amino Acid Sequence; Diffusion; Dimerization; Glucagon; Glucagon-Like Peptide 1; Hydrogen Bonding; Magnetic Resonance Spectroscopy; Models, Molecular; Molecular Sequence Data; Peptide Fragments; Protein Binding; Protein Conformation; Protein Precursors; Protein Structure, Secondary; Trifluoroethanol; Water

2002