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Biochemistry (Washington)

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  1. Correction to Metal Binding Properties of Escherichia coli YjiA, a Member of the Metal Homeostasis-Associated COG0523 Family of GTPases

    Biochemistry (Washington) 52(23):4105 (2013) PMCID PMC3680914

  2. Correction to NMR of CCCC RNA Reveals a Right-Handed Helix and Revised Parameters for AMBER Force Field Torsions Improve Structural Predictions from Molecular Dynamics

    Biochemistry (Washington) 52(19):3390 (2013) PMCID PMC3656770

  3. Volume and free energy of folding for troponin C C-domain: linkage to ion binding and N-domain interaction.

    Biochemistry (Washington) 47(17):5047 (2008) PMID 18393534

    Troponin C (TnC) is an 18-kDa acidic protein of the EF-hand family that serves as the trigger for muscle contraction. In this study, we investigated the thermodynamic stability of the C-domain of TnC in all its occupancy states (apo, Mg (2+)-, and Ca (2+)-bound states) using a fluorescent mutant...
  4. Comparative kinetics of cofactor association and dissociation for the human and trypanosomal S-adenosylhomocysteine hydrolases. 2. The role of helix 18 stability.

    Biochemistry (Washington) 47(17):4983 (2008) PMID 18393535

    The S-adenosyl- l-homocysteine (AdoHcy) hydrolases (SAHH) from Homo sapiens (Hs-SAHH) and from the parasite Trypanosoma cruzi (Tc-SAHH) are very similar in structure and catalytic properties but differ in the kinetics and thermodynamics of association and dissociation of the cofactor NAD (+). Th...
  5. A selenocysteine variant of the human copper chaperone for superoxide dismutase. A Se-XAS probe of cluster composition at the domain 3-domain 3 dimer interface.

    Biochemistry (Washington) 47(17):4916 (2008) PMID 18393442

    We report the semisynthesis of a selenocysteine (Sec) derivative of the human copper chaperone for superoxide dismutase, substituted with Sec at the C-terminal C246 residue. Measurements of hCCS-induced SOD1 activation were used to show that the C-terminal CXC sequence is both necessary and suff...
  6. Domain stabilities in protein kinase R (PKR): evidence for weak interdomain interactions.

    Biochemistry (Washington) 47(17):4887 (2008) PMID 18393532 PMCID PMC2729556

    PKR (protein kinase R) is induced by interferon and is a key component of the innate immunity antiviral pathway. Upon binding dsRNA, PKR undergoes autophosphorylation reactions that activate the kinase, leading it to phosphorylate eIF2alpha, thus inhibiting protein synthesis in virally infected ...
  7. Cu(II) binding to monomeric, oligomeric, and fibrillar forms of the Alzheimer's disease amyloid-beta peptide.

    Biochemistry (Washington) 47(17):5006 (2008) PMID 18393444

    Copper has been proposed to play a role in Alzheimer's disease through interactions with the amyoid-beta (Abeta) peptide. The coordination environment of bound copper as a function of Cu:Abeta stoichiometry and Abeta oligomerization state are particularly contentious. Using low-temperature elect...
  8. Biochemical origins of lactaldehyde and hydroxyacetone in Methanocaldococcus jannaschii.

    Biochemistry (Washington) 47(17):5037 (2008) PMID 18363381

    The biochemical routes for the metabolism of methylglyoxal and the formation of lactaldehyde and hydroxyacetone in Methanocaldococcus jannaschii have been established. The addition of methylglyoxal and NADH, NADPH, F 420H 2, or DTT to a M. jannaschii cell extract stimulated the production of bot...
  9. Effector-induced structural fluctuation regulates the ligand affinity of an allosteric protein: binding of inositol hexaphosphate has distinct dynamic consequences for the T and R states of hemoglobin.

    Biochemistry (Washington) 47(17):4907 (2008) PMID 18376851 PMCID PMC2493540

    The present study reports distinct dynamic consequences for the T- and R-states of human normal adult hemoglobin (Hb A) due to the binding of a heterotropic allosteric effector, inositol hexaphosphate (IHP). A nuclear magnetic resonance (NMR) technique based on modified transverse relaxation opt...
  10. Glucose modulation of glucokinase activation by small molecules.

    Biochemistry (Washington) 47(17):5028 (2008) PMID 18370405

    Small molecule activators of glucokinase (GK) were used in kinetic and equilibrium binding studies to probe the biochemical basis for their allosteric effects. These small molecules decreased the glucose K 0.5 ( approximately 1 mM vs approximately 8 mM) and the glucose cooperativity (Hill coeffi...