Time-Resolved CIDNP Study of Native-State Bovine and Human α-Lactalbumins od 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 od 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 od 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 od 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 od 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 od 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 od 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 od 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 od 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 od 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 od 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 od 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 od Mario Piris (2054899)

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

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

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

Hasła przedmiotowe:

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

Data_Sheet_1_Help Is in Your Blood—Incentive to “Double Altruism” Resolves the Plasma Donation Paradox.PDF od Petra Gyuris (6583133)

“…<p>Blood donation is considered as one of the purest forms of altruism. Plasma donation, in contrast, despite being a similar process, is mostly a paid activity in which donors are compensated for their contribution to the production of therapeutic preparations. …”

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