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)

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

Polarization-resolved microscopy—A method to determine actin order in biological systems. per 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 per Biswanath Chatterjee (430221)

Matèries:

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

Key structural features involved in ion permeation and gating in C1C2. per 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. …”

Resolving the Nanoscale Structure of β‑Sheet Peptide Self-Assemblies Using Single-Molecule Orientation–Localization Microscopy per Weiyan Zhou (493547)

CAP treatment of <i>F. keratoplasticum</i> mycelia induces non-resolving reduction in biofilm thickness, alone and in the presence of antifungal drugs. per Darby M. Roberts (22032789)

Tat is involved in <i>S</i>. Tm-induced colitis. per Mayuka Fujimoto (4710303)