about
Expression and function of the human androgen-responsive gene ADI1 in prostate cancerDetection of substrate-dependent conformational changes in the P450 fold by nuclear magnetic resonance.An NMR-derived model for the solution structure of oxidized putidaredoxin, a 2-Fe, 2-S ferredoxin from PseudomonasRedox-dependent dynamics of putidaredoxin characterized by amide proton exchangeUnfolding a molecular trefoil derived from a zwitterionic metallopeptide to form self-assembled nanostructures.Structural and dynamic implications of an effector-induced backbone amide cis-trans isomerization in cytochrome P450cam.Mechanistic studies of two dioxygenases in the methionine salvage pathway of Klebsiella pneumoniae.Communication between the zinc and nickel sites in dimeric HypA: metal recognition and pH sensingXAS investigation of the structure and function of Ni in acireductone dioxygenase.Detection of a high-barrier conformational change in the active site of cytochrome P450cam upon binding of putidaredoxinAcireductone dioxygenase 1 (ARD1) is an effector of the heterotrimeric G protein beta subunit in Arabidopsis.From intrinsically disordered protein to context-dependent folding: The α-synuclein tetramer is teased out of hidingNADH reduction of nitroaromatics as a probe for residual ferric form high-spin in a cytochrome P450.Characterization of metal binding in the active sites of acireductone dioxygenase isoforms from Klebsiella ATCC 8724.Examining how enzymes self-organize in a membrane.Conformational plasticity and structure/function relationships in cytochromes P450.The Metal Drives the Chemistry: Dual Functions of Acireductone Dioxygenase.Thermodynamics of interactions between amino acid side chains: experimental differentiation of aromatic-aromatic, aromatic-aliphatic, and aliphatic-aliphatic side-chain interactions in water.Redox-dependent dynamics in cytochrome P450cam.Substrate recognition by two different P450s: Evidence for conserved roles in a common fold.Redox-dependent conformational selection in a Cys4Fe2S2 ferredoxin.A conserved histidine in vertebrate-type ferredoxins is critical for redox-dependent dynamics.Solution Conformations and Dynamics of Substrate-Bound Cytochrome P450 MycG.1H NMR study of the influence of hydrophobic contacts on protein-prosthetic group recognition in bovine and rat ferricytochrome b5.The dynamic structure of α-synuclein multimers.1H and 15N resonance assignments and secondary structure of the carbon monoxide complex of sperm whale myoglobinWhat Your Crystal Structure Will Not Tell You about Enzyme FunctionSeparation of some enantiomeric di- and tripeptides on chiral stationary phasesProbing the mechanisms of macromolecular recognition: the cytochrome b5-cytochrome c complex1H NMR identification of a beta-sheet structure and description of folding topology in putidaredoxinRedox-dependent 1H NMR spectral features and tertiary structural constraints on the C-terminal region of putidaredoxinA structure-based model for cytochrome P450cam-putidaredoxin interactionsStructural features of the metal binding site and dynamics of gallium putidaredoxin, a diamagnetic derivative of a Cys4Fe2S2 ferredoxinNMR Structure Determination of Ion Pairs Derived from Quinine: A Model for Templating in Asymmetric Phase-Transfer Reductions by BH(4)(-) with Implications for Rational Design of Phase-Transfer CatalystsA new assignment strategy for the hyperfine-shifted 13C and 15N resonances in Fe2S2 ferredoxinsSome Surprising Implications of NMR-directed Simulations of Substrate Recognition and Binding by Cytochrome P450cam (CYP101A1)
P50
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P50
description
hulumtues
@sq
researcher
@en
wetenschapper
@nl
հետազոտող
@hy
name
Thomas C Pochapsky
@ast
Thomas C Pochapsky
@en
Thomas C Pochapsky
@es
Thomas C Pochapsky
@nl
Thomas C Pochapsky
@sl
type
label
Thomas C Pochapsky
@ast
Thomas C Pochapsky
@en
Thomas C Pochapsky
@es
Thomas C Pochapsky
@nl
Thomas C Pochapsky
@sl
prefLabel
Thomas C Pochapsky
@ast
Thomas C Pochapsky
@en
Thomas C Pochapsky
@es
Thomas C Pochapsky
@nl
Thomas C Pochapsky
@sl
P106
P21
P31
P496
0000-0001-8995-1088