Conformational Substates of Myoglobin Intermediate Resolved by Picosecond X‑ray Solution Scattering Yazar: 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 Yazar: 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 Yazar: 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 Yazar: 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 Yazar: 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 Yazar: 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 Yazar: 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 Yazar: 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 Yazar: 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 Yazar: 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 Yazar: 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 Yazar: 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 Yazar: 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 Yazar: Mario Piris (2054899)

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

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

Polarization-resolved microscopy—A method to determine actin order in biological systems. Yazar: Olivier Loison (5150705)

“…<p>(A) Polarization-resolved microscopy provides information about F-actin molecular order Ψ and the average actin filament orientation ρ. …”

Amyloid Core Formed of Full-Length Recombinant Mouse Prion Protein Involves Sequence 127–143 but Not Sequence 107–126 Yazar: Biswanath Chatterjee (430221)

Konular:

Involvement of MICU2 in the CRC tumor phenotype. Yazar: Alison Robert (19959563)

Key structural features involved in ion permeation and gating in C1C2. Yazar: Lindsey A. Prignano (19556855)

“…Regions outside the permeation pathway that are involved in pore formation and cation conductance are (side views): <b>(D)</b> A highly conserved cluster of residues that borders the predicted channel entrance in cation ChRs. …”