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Crystal structures of subtilisin BPN' variants containing disulfide bonds and cavities: concerted structural rearrangements induced by mutagenesis.

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The X-ray structures of four genetically engineered disulfide variants of subtilisin have been analyzed to determine the energetic and structural constraints involved in inserting disulfide bonds into proteins. Each of the engineered disulfides exhibited atypical sets of dihedral angles compared

Detection of Melanoma Cancer Biomarker Dimethyl Disulfide Using Cavity Ringdown Spectroscopy at 266 nm.

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Skin cells emit volatile organic compounds (VOCs), and some of them can be used as biomarkers for screening specific diseases. Dimethyl disulfide (DMDS) has been recently reported as a biomarker of melanoma skin cancer (Kwak et al. "Volatile Biomarkers from Human Melanoma Cells". J. Chromatogr. B.

Cavity-creating mutation at the dimer interface of Plasmodium falciparum triosephosphate isomerase: restoration of stability by disulfide cross-linking of subunits.

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Disulfide engineering across subunit interfaces provides a means of inhibiting dissociation during unfolding of multimeric enzymes. Two symmetry-related intersubunit disulfide bridges were introduced across the interface of the dimeric enzyme triosephosphate isomerase from Plasmodium falciparum.

Did evolution create a flexible ligand-binding cavity in the urokinase receptor through deletion of a plesiotypic disulfide bond?

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The urokinase receptor (uPAR) is a founding member of a small protein family with multiple Ly6/uPAR (LU) domains. The motif defining these LU domains contains five plesiotypic disulfide bonds stabilizing its prototypical three-fingered fold having three protruding loops. Notwithstanding the detailed

Drastically decreased reactivity of thiols and disulfides complexed by cucurbit[6]uril.

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The cucurbit[6]uril (CB6) host forms stable complexes with 2-aminoethanethiol (cysteamine) and a derivative that contains a bulky terminal group attached to the amine group, as well as with the related disulfide cystamine. In these complexes, the thiol or the disulfide group is encapsulated inside

Catalytic Formation of Disulfide Bonds in Peptides by Molecularly Imprinted Microgels at Oil/Water Interfaces.

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This work describes the preparation and investigation of molecularly imprinted polymer (MIP) microgel (MG) stabilized Pickering emulsions (PEs) for their ability to catalyze the formation of disulfide bonds in peptides at the O/W interface. The MIP MGs were synthesized via precipitation

Transporter-to-trap conversion: a disulfide bond formation in cellular retinoic acid binding protein I mutant triggered by retinoic acid binding irreversibly locks the ligand inside the protein.

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Transport proteins must bind their ligands reversibly to enable release at the point of delivery, while irreversible binding is usually associated with the extreme cases of ligand sequestration. Protein conformational dynamics is an important modulator of binding kinetics, as increased flexibility

A periplasmic LolA derivative with a lethal disulfide bond activates the Cpx stress response system.

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LolA accommodates the acyl chains of lipoproteins in its hydrophobic cavity and shuttles between the inner and outer membranes through the hydrophilic periplasm to place lipoproteins in the outer membrane. The LolA(I93C/F140C) derivative, in which Cys replaces Ile at position 93 and Phe at position

Scalable and Transfer-Free Fabrication of MoS2/SiO2 Hybrid Nanophotonic Cavity Arrays with Quality Factors Exceeding 4000.

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We report the fully-scalable fabrication of a large array of hybrid molybdenum disulfide (MoS2) - silicon dioxide (SiO2) one-dimensional, free-standing photonic-crystal cavities capable of enhancement of the MoS2 photoluminescence at the narrow cavity resonance. We demonstrate continuous tunability

Three-dimensional structure of a hybrid light chain dimer: protein engineering of a binding cavity.

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An attempt was made to engineer a binding site and check its structure by X-ray analysis. Two human light chains (Mcg and Weir), with "variable" domain sequences differing in 36 positions, were hybridized into a heterologous dimer and crystallized in ammonium sulfate by the same procedure used for

Tuning the cavity of cyclodextrins: altered sugar adaptors in protein pores.

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Cyclodextrins (CDs) have been widely used in host-guest molecular recognition because of their chiral and hydrophobic cavities. For example, β-cyclodextrin (βCD) lodged as a molecular adaptor in protein pores such as α-hemolysin (αHL) is used for stochastic sensing. Here, we have tuned the cavity

Molecularly imprinted protein recognition cavities bearing exchangeable binding sites for postimprinting site-directed introduction of reporter molecules for readout of binding events.

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Protein-imprinted cavities bearing exchangeable domains to be used for postimprinting fluorophore introduction to transform binding events into fluorescence changes were constructed in molecularly imprinted polymer (MIPs) matrixes prepared on glass substrates. Copolymerization was performed with

A cavity-forming mutation in insulin induces segmental unfolding of a surrounding alpha-helix.

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To investigate the cooperativity of insulin's structure, a cavity-forming substitution was introduced within the hydrophobic core of an engineered monomer. The substitution, Ile(A2)-->Ala in the A1-A8 alpha-helix, does not impair disulfide pairing between chains. In accord with past studies of

Fluorescence signaling molecularly imprinted polymers for antibiotics prepared via site-directed post-imprinting introduction of plural fluorescent reporters within the recognition cavity.

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An antibiotic-imprinted cavity with two different fluorescent dyes was prepared by molecular imprinting and subsequent post-imprinting modifications (PIMs), for the readout of a specific binding event as a fluorescence signal. The fluorescent dyes were site-specifically introduced into the cavity

In vitro and cellular self-assembly of a Zn-binding protein cryptand via templated disulfide bonds.

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Simultaneously strong and reversible through redox chemistry, disulfide bonds play a unique and often irreplaceable role in the formation of biological and synthetic assemblies. In an approach inspired by supramolecular chemistry, we report here that engineered noncovalent interactions on the

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