azobenzene and glycine

azobenzene has been researched along with glycine 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
Aemissegger, A; Hilvert, D; Kräutler, V; van Gunsteren, WF	1
Akiyama, H; Kameta, N; Masuda, M; Shimizu, T	1

Other Studies

2 other study(ies) available for azobenzene and glycine

Article	Year
A photoinducible beta-hairpin. Journal of the American Chemical Society, 2005, Mar-09, Volume: 127, Issue:9 Topics: Azo Compounds; Bacterial Proteins; Cross-Linking Reagents; Glycine; Models, Molecular; Nuclear Magnetic Resonance, Biomolecular; Oligopeptides; Peptide Fragments; Photochemistry; Proline; Protein Folding; Protein Structure, Secondary; Thermodynamics	2005
Effect of Photoinduced Size Changes on Protein Refolding and Transport Abilities of Soft Nanotubes. Chemistry (Weinheim an der Bergstrasse, Germany), 2016, 05-17, Volume: 22, Issue:21 Topics: Animals; Azo Compounds; Carbonic Anhydrases; Cattle; Enzymes, Immobilized; Glycine; Isomerism; Light; Models, Molecular; Nanotubes; Photochemical Processes; Protein Denaturation; Protein Refolding; Surface-Active Agents	2016

Article

Year

A photoinducible beta-hairpin.

Journal of the American Chemical Society, 2005, Mar-09, Volume: 127, Issue:9

Topics: Azo Compounds; Bacterial Proteins; Cross-Linking Reagents; Glycine; Models, Molecular; Nuclear Magnetic Resonance, Biomolecular; Oligopeptides; Peptide Fragments; Photochemistry; Proline; Protein Folding; Protein Structure, Secondary; Thermodynamics

2005

Effect of Photoinduced Size Changes on Protein Refolding and Transport Abilities of Soft Nanotubes.

Chemistry (Weinheim an der Bergstrasse, Germany), 2016, 05-17, Volume: 22, Issue:21

Topics: Animals; Azo Compounds; Carbonic Anhydrases; Cattle; Enzymes, Immobilized; Glycine; Isomerism; Light; Models, Molecular; Nanotubes; Photochemical Processes; Protein Denaturation; Protein Refolding; Surface-Active Agents

2016