Showing results (21-30 of 31) with videos related to
Sort By:
Pageof 4
Lab on a Chip|May 3, 2019
Direct writing of optical microresonators in a lab-on-a-chip for label-free biosensingL Kelemen, E Lepera, B Horváth, et al.Biophysical Journal|September 22, 2001
The voltage-dependent proton pumping in bacteriorhodopsin is characterized by optoelectric behaviorS Geibel, T Friedrich, P Ormos, et al.Nature|August 19, 2000
Structural alterations for proton translocation in the M state of wild-type bacteriorhodopsinH J Sass, G Büldt, R Gessenich, et al.Proceedings of the National Academy of Sciences of the United States of America|March 17, 1999
Interpretation of the spatial charge displacements in bacteriorhodopsin in terms of structural changes during the photocycleA Dér, L Oroszi, A Kulcsár, et al.Biophysical Journal|October 1, 1993
Ligand binding to heme proteins: II. Transitions in the heme pocket of myoglobinJ R Mourant, D P Braunstein, K Chu, et al.Proceedings of the National Academy of Sciences of the United States of America|November 1, 1988
Orientation of carbon monoxide and structure-function relationship in carbonmonoxymyoglobinP Ormos, D Braunstein, H Frauenfelder, et al.Proceedings of the National Academy of Sciences of the United States of America|November 1, 1988
Ligand binding to synthetic mutant myoglobin (His-E7----Gly): role of the distal histidineD Braunstein, A Ansari, J Berendzen, et al.Biophysical Chemistry|May 9, 1987
Rebinding and relaxation in the myoglobin pocketA Ansari, J Berendzen, D Braunstein, et al.Biophysical Journal|August 1, 1990
Conformational substates and motions in myoglobin. External influences on structure and dynamicsM K Hong, D Braunstein, B R Cowen, et al.Biophysical Journal|February 1, 1990
Inhomogeneous broadening in spectral bands of carbonmonoxymyoglobin. The connection between spectral and functional heterogeneityP Ormos, A Ansari, D Braunstein, et al.Pageof 4