Results 311 to 320 of about 1,336,409 (334)

Bacterial cold-shock proteins

Cellular and Molecular Life Sciences, 2002
Members of a family of small cold-shock proteins (CSPs) are induced during bacterial cell response to a temperature decrease. Here we review available data about the structure, molecular properties, mechanism of induction and possible functions of CSPs.
D N, Ermolenko, G I, Makhatadze
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Protein engineering with bacterial display

Current Opinion in Structural Biology, 2007
Recent improvements in bacterial surface display systems coupled with efficient selection and screening strategies are propelling bacterial display systems to the forefront of peptide and protein engineering. The ability to analyze and screen very large protein libraries using cell-sorting instrumentation coupled with the ease of manipulating bacteria ...
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The Structure of Bacterial S-Layer Proteins

2011
S-layers are self-assembled paracrystalline protein lattices that cover many bacteria and almost all archaea. As an important component of the bacterial cell envelope, S-layers can fulfill various biological functions and are usually the most abundantly expressed protein species in a cell. Here we review the structures of the best characterized S-layer
Tea, Pavkov-Keller, Stefan, Howorka, Walter, Keller   +2 more
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Protein conformation in bacterial spinae

Biopolymers, 1976
AbstractThe far uv circular dichroism (CD) and infrared spectra of bacterial spinae are reported. Estimates of the protein secondary structure were obtained by three‐component curve‐fitting methods supplemented by rank and factor analysis of CD data matrices. Native spinae were shown to contain approximately 88% antiparallel β‐sheet, 7% α‐helix, and 5%
R W, Coombs, J A, Verpoorte, K B, Easterbrook   +2 more
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Autophosphorylation of a Bacterial Protein at Tyrosine

Journal of Molecular Biology, 1996
Autophosphorylation at tyrosine is a common process in eukaryotic kinases, which is generally modulated by regulatory ligands and affects the properties of these enzymes. We report that this type of modification occurs also in bacteria, namely in an 81 kDa protein from Acinetobacter johnsonii.
Duclos, B., Grangeasse, C., Vaganay, E., Riberty, M., Cozzone, Aj   +4 more
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Bacterial oligopeptide-binding proteins

Cellular and Molecular Life Sciences (CMLS), 2003
This review focuses on bacterial oligopeptide-binding proteins, which form part of the oligopeptide transport system belonging to the ATP-binding cassette family of transporters. Depending on the bacterial species, these binding proteins (OppA) capture peptides ranging in size from 2 to 18 amino acids from the environment and pass them on to the other ...
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Protein–Protein Interaction: Bacterial Two-Hybrid

2017
The bacterial two-hybrid (BACTH, for "Bacterial Adenylate Cyclase-based Two-Hybrid") system is a simple and fast genetic approach to detect and characterize protein-protein interactions in vivo. This system is based on the interaction-mediated reconstitution of a cAMP signaling cascade in Escherichia coli.
Karimova, Gouzel, Gauliard, Emilie, Davi, Marilyne, Ouellette, Scot, Ladant, Daniel   +4 more
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Bacterial Protein Translocation

1988
Protein translocation is a process common to all cells. Both prokaryotes and eukaryotes are divided into distinct compartments, each containing a unique set of proteins important to specific cellular functions. Except for a few mitochondrial and chloroplast proteins, almost all proteins are synthesized in the cytoplasm; therefore many proteins must ...
Elliott Crooke, William Wickner
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PDZ domains in bacterial proteins

Molecular Microbiology, 1997
M J, Pallen, C P, Ponting
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Bacterial Protein Export

1988
Consideration of protein export by bacteria is of major importance to many research institutions and industrial organisations currently involved in biotechnology. Bacteria (in particular, Escherichia coli), are used as hosts for the biosynthesis of proteins.
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