38 research outputs found
Proposing new variables for the identification of strategic groups in franchising
The identification of strategic groups in the Spanish franchising area is the
main aim of this study. The authors have added some new strategic variables (not
used before) to the study and have classified franchisors between sectors and
distribution strategy. The results reveal the existence of four perfectly differentiated
strategic groups (types of franchisors). One of the major implications of this study is
that the variables that build a strategic group vary depending on the respective sector the network operates in and its distribution strategy. This fact indicates that including sector and distribution strategy is absolutely necessary to achieve good classifications of franchisor type
Design, construction, and initial operation of the BNL-coastal transport and diffusion, Air/Sea Interaction research buoy. Data report
Design features of the Brookhaven National Laboratory (BNL) Air/Sea Interaction (A/S-I) buoy are described, and construction, testing, and deployment experiences are related. This two-attitude buoy is similar to the MIT/Navy buoy which it replaces, but it accommodates more instruments and can be towed through shallower water. The BNL A/S-I buoy can be broken down into two, three, or four sections to facilitate overland transport. Compressed air is stored aboard and the controls for deploying, trimming, and recovering the buoy are centralized on the superstructure and are perpetually above water level. The ballast control plumbing is entirely within the hull for maximum protection. The buoy also has a propane storage and distribution system and a 40-watt thermoelectric generator for powering instruments. Two buoys were built and tested in 1978, and one buoy was deployed in 1979 and is in operation off the south coast of Long Island
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Developing an Acidic Residue Reactive and Sulfoxide-Containing MS-Cleavable Homobifunctional Cross-Linker for Probing Protein-Protein Interactions.
Cross-linking mass spectrometry (XL-MS) has become a powerful strategy for defining protein-protein interactions and elucidating architectures of large protein complexes. However, one of the inherent challenges in MS analysis of cross-linked peptides is their unambiguous identification. To facilitate this process, we have previously developed a series of amine-reactive sulfoxide-containing MS-cleavable cross-linkers. These MS-cleavable reagents have allowed us to establish a common robust XL-MS workflow that enables fast and accurate identification of cross-linked peptides using multistage tandem mass spectrometry (MS(n)). Although amine-reactive reagents targeting lysine residues have been successful, it remains difficult to characterize protein interaction interfaces with little or no lysine residues. To expand the coverage of protein interaction regions, we present here the development of a new acidic residue-targeting sulfoxide-containing MS-cleavable homobifunctional cross-linker, dihydrazide sulfoxide (DHSO). We demonstrate that DHSO cross-linked peptides display the same predictable and characteristic fragmentation pattern during collision induced dissociation as amine-reactive sulfoxide-containing MS-cleavable cross-linked peptides, thus permitting their simplified analysis and unambiguous identification by MS(n). Additionally, we show that DHSO can provide complementary data to amine-reactive reagents. Collectively, this work not only enlarges the range of the application of XL-MS approaches but also further demonstrates the robustness and applicability of sulfoxide-based MS-cleavability in conjunction with various cross-linking chemistries
Developing an Acidic Residue Reactive and Sulfoxide-Containing MS-Cleavable Homobifunctional Cross-Linker for Probing ProteinProtein Interactions
EFFECTS OF COUNTERTRADE-DIVERGENT PERCEPTIONS BETWEEN PRACTITIONERS AND NON-PARTICIPANTS [1]
Developing an Acidic Residue Reactive and Sulfoxide-Containing MS-Cleavable Homobifunctional Cross-Linker for Probing Protein鈥揚rotein Interactions
Cross-linking mass spectrometry (XL-MS)
has become a powerful strategy
for defining protein鈥損rotein interactions and elucidating architectures
of large protein complexes. However, one of the inherent challenges
in MS analysis of cross-linked peptides is their unambiguous identification.
To facilitate this process, we have previously developed a series
of amine-reactive sulfoxide-containing MS-cleavable cross-linkers.
These MS-cleavable reagents have allowed us to establish a common
robust XL-MS workflow that enables fast and accurate identification
of cross-linked peptides using multistage tandem mass spectrometry
(MS<sup><i>n</i></sup>). Although amine-reactive reagents
targeting lysine residues have been successful, it remains difficult
to characterize protein interaction interfaces with little or no lysine
residues. To expand the coverage of protein interaction regions, we
present here the development of a new acidic residue-targeting sulfoxide-containing
MS-cleavable homobifunctional cross-linker, dihydrazide sulfoxide
(DHSO). We demonstrate that DHSO cross-linked peptides display the
same predictable and characteristic fragmentation pattern during collision
induced dissociation as amine-reactive sulfoxide-containing MS-cleavable
cross-linked peptides, thus permitting their simplified analysis and
unambiguous identification by MS<sup><i>n</i></sup>. Additionally,
we show that DHSO can provide complementary data to amine-reactive
reagents. Collectively, this work not only enlarges the range of the
application of XL-MS approaches but also further demonstrates the
robustness and applicability of sulfoxide-based MS-cleavability in
conjunction with various cross-linking chemistries
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Development of a Novel Sulfoxide-Containing MS-Cleavable Homobifunctional Cysteine-Reactive Cross-Linker for Studying Protein鈥揚rotein Interactions
Cross-linking mass
spectrometry (XL-MS) has become an emerging
technology for defining protein鈥損rotein interactions (PPIs)
and elucidating architectures of large protein complexes. Up to now,
the most widely used cross-linking reagents target lysines. Although
such reagents have been successfully applied to map PPIs at the proteome-wide
scale, comprehensive PPI profiling would require additional cross-linking
chemistries. Cysteine is one of the most reactive amino acids and
an attractive target for cross-linking owing to its unique role in
protein structures. Although sulfhydryl-reactive cross-linkers are
commercially available, their applications in XL-MS studies remain
sparse, likely due to the difficulty in identifying cysteine cross-linked
peptides. Previously, we developed a new class of sulfoxide-containing
MS-cleavable cross-linkers to enable fast and accurate identification
of cross-linked peptides using multistage tandem mass spectrometry
(MS<sup><i>n</i></sup>). Here, we present the development
of a new sulfoxide-containing MS-cleavable homobifunctional cysteine-reactive
cross-linker, bismaleimide sulfoxide (BMSO). We demonstrate that BMSO-cross-linked
peptides display the same characteristic fragmentation pattern during
collision-induced dissociation (CID) as other sulfoxide-containing
MS-cleavable cross-linked peptides, thus permitting their simplified
analysis and unambiguous identification by MS<sup><i>n</i></sup>. Additionally, we show that BMSO can complement amine- and
acidic-residue-reactive reagents for mapping protein-interaction regions.
Collectively, this work not only enlarges the toolbox of MS-cleavable
cross-linkers with diverse chemistries, but more importantly expands
our capacity and capability of studying PPIs in general