Evidence for involvement of endocytosis in <i>T</i>. <i>gondii</i> motility. per Simon Gras (328719)

Dynamics and Flexibility of Human Aromatase Probed by FTIR and Time Resolved Fluorescence Spectroscopy per Giovanna Di Nardo (301574)

“…Together the results are consistent with different degrees of flexibility of the access channel and therefore different conformations adopted by the enzyme in the free, substrate- and inhibitor-bound forms.</p></div>…”

ASIC1 oligomeric states resolved by SDS-PAGE after crosslinking with BMOE. per Miguel Xavier van Bemmelen (781306)

Applying an Anti-Kasha Model Resolves Differences Between Photosynthetic and Artificial Pigments per Jan P. Götze (2063170)

“…The pigments are further found to form strongly delocalized excitons, especially between the higher excited states usually responsible for anti-Kasha pathways. …”

Schematic representation of the populations involved in the response to SRS. per Beatriz Ocaña-Tienda (17873813)

Conformational Substates of Myoglobin Intermediate Resolved by Picosecond X‑ray Solution Scattering per Key Young Oang (1285278)

“…We attribute the biphasic kinetics to the involvement of two conformational substates of the first intermediate, which are generated by the interplay between the distal histidine and the photodissociated CO.…”

Time-Resolved CIDNP Study of Native-State Bovine and Human α-Lactalbumins per Olga B. Morozova (1521157)

“…The nuclear spin−lattice relaxation times in the radicals formed in these reactions have been determined from the CIDNP kinetics:  <i>T</i>₁ = 60 μs for H2,4,7 of Trp118, <i>T</i>₁ = 53 μs for H3,5 of Tyr103, <i>T</i>₁ = 16 μs for H3,5 of Tyr18, and <i>T</i>₁ = 10 μs for the H2 and H4 of His68. …”

Time-Resolved CIDNP Study of Native-State Bovine and Human α-Lactalbumins per Olga B. Morozova (1521157)

“…The nuclear spin−lattice relaxation times in the radicals formed in these reactions have been determined from the CIDNP kinetics:  <i>T</i>₁ = 60 μs for H2,4,7 of Trp118, <i>T</i>₁ = 53 μs for H3,5 of Tyr103, <i>T</i>₁ = 16 μs for H3,5 of Tyr18, and <i>T</i>₁ = 10 μs for the H2 and H4 of His68. …”

Time-Resolved CIDNP Study of Native-State Bovine and Human α-Lactalbumins per Olga B. Morozova (1521157)

“…The nuclear spin−lattice relaxation times in the radicals formed in these reactions have been determined from the CIDNP kinetics:  <i>T</i>₁ = 60 μs for H2,4,7 of Trp118, <i>T</i>₁ = 53 μs for H3,5 of Tyr103, <i>T</i>₁ = 16 μs for H3,5 of Tyr18, and <i>T</i>₁ = 10 μs for the H2 and H4 of His68. …”

Time-Resolved CIDNP Study of Native-State Bovine and Human α-Lactalbumins per Olga B. Morozova (1521157)

“…The nuclear spin−lattice relaxation times in the radicals formed in these reactions have been determined from the CIDNP kinetics:  <i>T</i>₁ = 60 μs for H2,4,7 of Trp118, <i>T</i>₁ = 53 μs for H3,5 of Tyr103, <i>T</i>₁ = 16 μs for H3,5 of Tyr18, and <i>T</i>₁ = 10 μs for the H2 and H4 of His68. …”

Time-Resolved CIDNP Study of Native-State Bovine and Human α-Lactalbumins per Olga B. Morozova (1521157)

“…The nuclear spin−lattice relaxation times in the radicals formed in these reactions have been determined from the CIDNP kinetics:  <i>T</i>₁ = 60 μs for H2,4,7 of Trp118, <i>T</i>₁ = 53 μs for H3,5 of Tyr103, <i>T</i>₁ = 16 μs for H3,5 of Tyr18, and <i>T</i>₁ = 10 μs for the H2 and H4 of His68. …”

Time-Resolved CIDNP Study of Native-State Bovine and Human α-Lactalbumins per Olga B. Morozova (1521157)

“…The nuclear spin−lattice relaxation times in the radicals formed in these reactions have been determined from the CIDNP kinetics:  <i>T</i>₁ = 60 μs for H2,4,7 of Trp118, <i>T</i>₁ = 53 μs for H3,5 of Tyr103, <i>T</i>₁ = 16 μs for H3,5 of Tyr18, and <i>T</i>₁ = 10 μs for the H2 and H4 of His68. …”

Time-Resolved CIDNP Study of Native-State Bovine and Human α-Lactalbumins per Olga B. Morozova (1521157)

“…The nuclear spin−lattice relaxation times in the radicals formed in these reactions have been determined from the CIDNP kinetics:  <i>T</i>₁ = 60 μs for H2,4,7 of Trp118, <i>T</i>₁ = 53 μs for H3,5 of Tyr103, <i>T</i>₁ = 16 μs for H3,5 of Tyr18, and <i>T</i>₁ = 10 μs for the H2 and H4 of His68. …”

Time-Resolved CIDNP Study of Native-State Bovine and Human α-Lactalbumins per Olga B. Morozova (1521157)

“…The nuclear spin−lattice relaxation times in the radicals formed in these reactions have been determined from the CIDNP kinetics:  <i>T</i>₁ = 60 μs for H2,4,7 of Trp118, <i>T</i>₁ = 53 μs for H3,5 of Tyr103, <i>T</i>₁ = 16 μs for H3,5 of Tyr18, and <i>T</i>₁ = 10 μs for the H2 and H4 of His68. …”

Time-Resolved CIDNP Study of Native-State Bovine and Human α-Lactalbumins per Olga B. Morozova (1521157)

“…The nuclear spin−lattice relaxation times in the radicals formed in these reactions have been determined from the CIDNP kinetics:  <i>T</i>₁ = 60 μs for H2,4,7 of Trp118, <i>T</i>₁ = 53 μs for H3,5 of Tyr103, <i>T</i>₁ = 16 μs for H3,5 of Tyr18, and <i>T</i>₁ = 10 μs for the H2 and H4 of His68. …”

Time-Resolved CIDNP Study of Native-State Bovine and Human α-Lactalbumins per Olga B. Morozova (1521157)

“…The nuclear spin−lattice relaxation times in the radicals formed in these reactions have been determined from the CIDNP kinetics:  <i>T</i>₁ = 60 μs for H2,4,7 of Trp118, <i>T</i>₁ = 53 μs for H3,5 of Tyr103, <i>T</i>₁ = 16 μs for H3,5 of Tyr18, and <i>T</i>₁ = 10 μs for the H2 and H4 of His68. …”

Time-Resolved CIDNP Study of Native-State Bovine and Human α-Lactalbumins per Olga B. Morozova (1521157)

“…The nuclear spin−lattice relaxation times in the radicals formed in these reactions have been determined from the CIDNP kinetics:  <i>T</i>₁ = 60 μs for H2,4,7 of Trp118, <i>T</i>₁ = 53 μs for H3,5 of Tyr103, <i>T</i>₁ = 16 μs for H3,5 of Tyr18, and <i>T</i>₁ = 10 μs for the H2 and H4 of His68. …”

Time-Resolved CIDNP Study of Native-State Bovine and Human α-Lactalbumins per Olga B. Morozova (1521157)

“…The nuclear spin−lattice relaxation times in the radicals formed in these reactions have been determined from the CIDNP kinetics:  <i>T</i>₁ = 60 μs for H2,4,7 of Trp118, <i>T</i>₁ = 53 μs for H3,5 of Tyr103, <i>T</i>₁ = 16 μs for H3,5 of Tyr18, and <i>T</i>₁ = 10 μs for the H2 and H4 of His68. …”

Time-Resolved Chemical Bonding Structure Evolution by Direct-Dynamics Chemical Simulations per Mario Piris (2054899)

Time-Resolved Chemical Bonding Structure Evolution by Direct-Dynamics Chemical Simulations per Mario Piris (2054899)