The activity of IF-MP, a polypeptide chain initiation factor that forms a ternary complex with eukaryotic initiator Met-tRNA and GTP and promotes binding of the initiator to 40S ribosomes, is very low in undeveloped Artemia salina embryos but increases over 20-fold following resumption of development upon hydration of the cysts. The factor is present in both the ribosomal salt wash and high-sp...

Widely used reagents in the peptide functionalization toolbox, Michael acceptors and N-hydroxysuccinimide (NHS) activated esters, are combined NHS-activated acrylamides for efficient chemoselective amino-sulfhydryl stapling on native peptides proteins. allow a fast of N-terminal cysteines (k2=1.54±0.18×103 M−1 s−1) under dilute aqueous conditions, enabling selectivity over other nucleophilic am...

Three new reagents that react against human T cells were synthesized by covalently linking the toxin ricin to monoclonal antibodies recognizing differentiation antigens on the surface of T lymphocytes. Each of these immunotoxins selectively inhibited T-cell proliferation when the cells were incubated in the presence of lactose. Multipotent human stem cells were inhibited only at much higher con...

The relative orientation and proximity of the pseudo-symmetrical inner transmembrane helical pairs 5/8 and 2/11 of Glut1 were analyzed by chemical cross-linking of di-cysteine mutants. Thirteen functional di-cysteine mutants were created from a C-less Glut1 reporter construct containing cysteine substitutions in helices 5 and 8 or helices 2 and 11. The mutants were expressed in Xenopus oocytes ...

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-c...

The arrangement of protein I in the outer membrane of Escherichia coli was investigated by cross-linking whole cells, isolated cell wall, protein-peptidoglycan complexes, and protein I released from peptidoglycan with NaCl. Both cleavable azide cross-linkers and imidoester reagents were used. The data presented suggest that protein I exists in the outer membrane as a trimer.

Human erythrocyte ghosts were chemically cross-linked with a family of bifunctional cross-linking reagents, imidoesters. Since the reagents are identical in their chemical structures, except for the number of methylene groups, they differ by that distance between the functional groups. The maximum distance is 4.9 A in dimethyl malonimidate, 6.1 A in dimethyl succinimidate, 8.6 A in dimethyl adi...

Human erythrocyte ghosts were chemically cross-linked with a family of bifunctional cross-linking reagents, imidoesters. Since the reagents are identical in their chemical structures, except for the number of methylene groups, they differ by that distance between the functional groups. The maximum distance is 4.9 A in dimethyl malonimidate, 6.1 A in dimethyl succinimidate, 8.6 A in dimethyl adi...

Human erythrocyte ghosts were chemically cross-linked with a family of bifunctional cross-linking reagents, imidoesters. Since the reagents are identical in their chemical structures, except for the number of methylene groups, they differ by that distance between the functional groups. The maximum distance is 4.9 A in dimethyl malonimidate, 6.1 A in dimethyl succinimidate, 8.6 A in dimethyl adi...