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Biochemistry (Washington)

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  1. Hydrophobic blocks facilitate lipid compatibility and translocon recognition of transmembrane protein sequences.

    Biochemistry (Washington) 54(7):1465 (2015) PMID 25635746

    We designed and synthesized a library of Lys-tagged peptides of a core length sufficient to span a bilayer but with varying patterns of sequence, each composed of nine Leu residues, nine Ser residues, and one (central) Trp residue. We found that peptides containing contiguous Leu residues (Leu-block...
  2. Ligand Recognition Specificity of Leukocyte Integrin αMβ2 (Mac-1, CD11b/CD18) and Its Functional Consequences.

    Biochemistry (Washington) 54(6):1408 (2015) PMID 25613106

    We know little about how and why αMβ2 binds its multiple ligands. Within αMβ2, the αMI-domain is responsible for integrin's multiligand binding properties. To identify its recognition motif, we screened peptide libraries spanning sequences of many known protein ligands for αMI-domain binding and als...
  3. Structural and Functional Characterization of the Acidic Region from the RIZ Tumor Suppressor.

    Biochemistry (Washington) 54(6):1390 (2015) PMID 25640033

    We investigated the interaction between purified recombinant AR and the pocket domain of Rb using nuclear magnetic resonance spectroscopy, isothermal titration calorimetry, and fluorescence anisotropy experiments. We show that AR is intrinsically disordered and that it binds the pocket domain with s...
  4. Insights into the structure of intrastrand cross-link DNA lesion-containing oligonucleotides: g[8-5m]T and g[8-5]C from molecular dynamics s...

    Biochemistry (Washington) 54(5):1259 (2015) PMID 25600505

    We propose the use of explicit solvent molecular dynamics simulations to build up damaged oligonucleotides containing two intrastrand cross-link defects, namely, the guanine-thymine and guanine-cytosine defects. Each of these lesions, G[8-5m]T and G[8-5]C, is placed in the middle of a dodecameric se...
  5. Distal regulation of heme binding of heme oxygenase-1 mediated by conformational fluctuations.

    Biochemistry (Washington) 54(2):340 (2015) PMID 25496210

    We characterized conformational dynamics of HO-1 using NMR to elucidate the mechanism by which HO-1 recognizes heme. NMR relaxation experiments showed that the heme-binding site in heme-free HO-1 fluctuates in concert with a surface-exposed loop and transiently forms a partially unfolded structure....
  6. Dynamic asymmetry and the role of the conserved active-site thiol in rabbit muscle creatine kinase.

    Biochemistry (Washington) 54(1):83 (2015) PMID 25347386

    Symmetric and asymmetric crystal structures of the apo and transition state analogue forms, respectively, of the dimeric rabbit muscle creatine kinase have invoked an "induced fit" explanation for asymmetry between the two subunits and their active sites. However, previously reported thiol reactivit...
  7. Avian synaptopodin 2 (fesselin) stabilizes myosin filaments and actomyosin in the presence of ATP.

    Biochemistry (Washington) 52(43):7641 (2013) PMID 24083890 PMCID PMC3859813

    These results support the view that one role of fesselin is to organize contractile units of myosin and actin....
  8. Correction to Redox Potential and Peroxide Reactivity of Human Peroxiredoxin 3.

    Biochemistry (Washington) :101014152422031 (2010) PMID 20945918

  9. Crystal Structures of Human Δ4-3-Ketosteroid 5β-Reductase (AKR1D1) Reveal the Presence of an Alternative Binding Site Responsible for Substr...

    Biochemistry (Washington) 48(5):1144 (2009) PMID 19187037

  10. Proteolytic activation of recombinant pro-memapsin 2 (Pro-beta-secretase) studied with new fluorogenic substrates

    Biochemistry (Washington) 39(51):16263 (2000) PMID 11123957