Amino-acids and peptides. XXXV. Analogues of oxytocin modified in positions 1 and 2 of the peptide chain: Protected intermediates

1961 ◽  
Vol 26 (10) ◽  
pp. 2496-2510 ◽  
Author(s):  
K. Jošt ◽  
J. Rudinger ◽  
F. Šorm
Keyword(s):  
Amino Acids ◽  
Peptide Chain

The C-terminal sequence of amino acid residues of κ-casein isolated from buffalo's milk

1967 ◽  
Vol 34 (1) ◽  
pp. 85-88 ◽  
Author(s):  
M. H. Abd El-Salam ◽  
W. Manson
Keyword(s):  
Amino Acids ◽  
Molecular Weight ◽  
Amino Acid ◽  
Peptide Chain ◽  
Amino Acid Residues ◽  
Terminal Sequence ◽  
Carboxypeptidase A ◽  
Phosphorous Content ◽  
Single Peptide

SummaryWhen κ-casein from buffalo's milk was treated with carboxypeptidase A (EC 3. 4. 2. 1),4 amino acids, valine, threonine, serine and alanine were released from the protein in a manner consistent with the view that they originate in the C-terminal sequence of a single peptide chain. The amounts produced suggest a minimum molecular weight for buffalo κ-casein of approximately 17000, in agreement with the value calculated from the phosphorous content on the basis of the presence of 2 phosphorus atoms/molecule. A comparison is made with the C-terminal sequence reported for bovine κ-casein.

scholarly journals The functional importance of the extreme C-terminal tail in the gene 2 organellar Ca2+-transport ATPase (SERCA2a/b)

1994 ◽  
Vol 303 (3) ◽  
pp. 979-984 ◽  
Author(s):  
H Verboomen ◽  
F Wuytack ◽  
L Van den Bosch ◽  
L Mertens ◽  
R Casteels
Keyword(s):  
Amino Acids ◽  
Splice Variant ◽  
Turnover Rate ◽  
Peptide Chain ◽  
Deletion Mutants ◽  
Functional Difference ◽  
Critical Importance ◽  
Transmembrane Segment ◽  
Functional Importance ◽  
Transport Atpase

Ca(2+)-uptake experiments in microsomal fractions from transfected COS-1 cells have revealed a functional difference between the non-muscle SERCA2b Ca2+ pump and its muscle-specific SERCA2a splice variant. Structurally, the two pumps differ only in their C-terminal tail. The last four amino acids of SERCA2a are replaced in SERCA2b by a 49-residue-long peptide chain containing a very hydrophobic stretch which could be an additional transmembrane segment. The functionally important subdomains in the SERCA2b tail were analysed by constructing three SERCA2b deletion mutants lacking 12, 31 or 49 amino acids. The mutants and the parental SERCA2 pumps were expressed in COS-1 cells and analysed for functional difference. SERCA2b had a twofold higher Ca2+ affinity, a twofold lower turnover rate and a 10-fold lower vanadate-sensitivity than SERCA2a and the mutants. Since each of the three truncated versions of SERCA2b acquire the characteristic properties of SERCA2a, it is concluded that the stretch of the last 12 residues of SERCA2b is of critical importance.

scholarly journals Wachstumsgeschwindigkeit der Peptidkette im Tabakmosaikvirus

1967 ◽  
Vol 22 (12) ◽  
pp. 1280-1291 ◽  
Author(s):  
H. Diringer ◽  
F. A. Anderer ◽  
G. Schramm
Keyword(s):  
Amino Acids ◽  
Growth Rate ◽  
Protein Synthesis ◽  
Peptide Chain ◽  
Cell Protein ◽  
Virus Protein ◽  
Animal Cells ◽  
Tobacco Leaves ◽  
Soluble Cell ◽  
C Terminus

The rate of incorporation of labelled amino acids into the complete tobacco mosaic virus (TMV), into soluble virus protein and into soluble cell proteins has been determined in discs of infected and healthy tobacco leaves. The rate of overall protein synthesis is increased by 50% in the infected leaves. At least 60% of the increase derives from the synthesis of virus-specific proteins and the synthesis of cellular proteins is not inhibited. The virus protein synthesis is strongly temperature dependent and shows a maximum at 28 °C.The exchange of free labelled amino acids between the external medium and the inner cellular pool reaches equilibrium within ten minutes. The influence of the exchange rate on the measurement of the kinetics of peptide chain synthesis is discussed in detail.Discs from infected leaves were incubated for short periods at low temperatures in media containing 3H-tyrosine or 3H-proline. Peptides isolated after 5 minutes incubation at 15 °C were found to be uniformly labelled with no apparent gradient of radioactivity from the N- to the C-terminus. The results indicate that the growth rate of the peptide chain at 15 °C is probably higher than 2 - 3 amino acids/sec and at 28 °C higher than 20 amino acids/sec. These values are higher than those for animal cells and similar to those for protein synthesis in Escherichia coli.Comparison of the growth rate of TMV protein with rate of total protein synthesis and the number of ribosomes in the tobacco leaves indicate that only a small portion of the ribosomes takes part in cell protein synthesis.

Untersuchungen zur Struktur und Derivatisierung von Kondensationsprodukten der 2,4-Diaminobuttersäure mit anderen Aminosäuren / Investigations Regarding Structure and Derivatization of the Condensation Products of 2,4-Diaminobutyric Acid with Other Amino Acids

1994 ◽  
Vol 49 (1-2) ◽  
pp. 18-25 ◽  
Author(s):  
G. Filsak ◽  
K. Taraz ◽  
H. Budzikiewicz
Keyword(s):  
Amino Acids ◽  
Fluorescent Pseudomonads ◽  
Peptide Chain ◽  
Diaminobutyric Acid ◽  
Condensation Products ◽  
Ms Analysis ◽  
Model Substances

Condensation of 2,4-diaminobutyric acid (Dab) with other amino acids yields tetrahydropyrimidine derivatives. Such condensation products can be constituents of the peptide chain of pyoverdins and ferribactins (the siderophors of fluorescent pseudomonads). Synthesis of several representatives and model substances allows to confirm earlier structural conclusions based mainly on NMR evidence. Apparent anomalies accompanying the derivatization for GC/MS analysis could be clarified.

Highly Diastereoselective Peptide Chain Extensions of Unprotected Amino Acids withN-(Z-α-Aminoacyl)benzotriazoles

Synthesis ◽  
2004 ◽  
Vol 2004 (16) ◽  
pp. 2645-2652 ◽  
Author(s):  
Alan R. Katritzky ◽  
Kazuyuki Suzuki ◽  
Sandeep K. Singh
Keyword(s):  
Amino Acids ◽  
Peptide Chain

scholarly journals Non-ribosomal peptide synthetase docking domains : structure, function and engineering strategies

2021 ◽  
Author(s):  
◽  
Jonas Watzel
Keyword(s):  
Amino Acids ◽  
Amino Acid ◽  
Building Blocks ◽  
Peptide Chain ◽  
Solution Nmr ◽  
High Affinity ◽  
Single Protein ◽  
T Domain ◽  
Α Helix ◽  
Affinity Interaction

Non-ribosomal peptide synthetases (NRPSs) are known for their capability to produce a wide range of natural compounds and some of them possess interesting bioactivities relevant for clinical application like antibiotics, anticancer, and immunosuppressive drugs. The diverse bioactivity of non-ribosomal peptides (NRPs) originates from their structural diversity, which results not only from the incorporation of non-proteinogenic amino acids into the growing peptide chain, but also the formation of heterocycles or further peptide modifications like methylation, hydroxylation and acetylation. The biosynthesis of NRPs is achieved via the orchestrated interplay of distinct catalytic domains, which are grouped to modules that are located on one or more polypeptide chains. Each cycle starts with the selection and activation of a specific amino acid by the adenylation (A) domain, which catalyzes the aminoacyl adenylate formation under ATP consumption. This activated amino acid is then bound via a thioester bond to the 4’-phosphopantetheine cofactor (PPant-arm) of the following thiolation (T) domain. Before substrate loading, the PPant-arm is post-translationally added to the T domain by a phosphopantetheinyl transferase (PPTase), which converts the inactive apo-T domain in its active holo-form. In the last step of the catalytic cycle, two T domain bound peptide building blocks are connected by the condensation (C) domain, resulting in peptide bond formation and transfer of the nascent peptide chain to the following module. Each catalytic cycle is performed by a C-A-T elongation module until the termination module with a C-terminal thioesterase (TE) domain is reached. Here, the peptide product is released by hydrolysis or intramolecular cyclisation. In comparison to single-protein NRPSs, where all modules are encoded on a single polypeptide chain, multi-protein NRPS systems must also maintain a specific module order during the peptide biosynthesis. Therefore, small C-terminal and N-terminal communication-mediating (COM) domains/docking domains (DD) were identified in the C- and N-terminal regions of multi-protein NRPSs. It was shown that these domains mediate specific and selective non-covalent protein-protein interaction, even though DD interactions are generally characterized by low affinities. The first publication of this work focuses on the Peptide-Antimicrobial-Xenorhabdus peptide-producing NRPS called PaxS, which consists of the three proteins PaxA, PaxB and PaxC. Here, in particular the trans DD interface between the C-terminal attached DD of PaxB and N-terminal attached DD of PaxC was structurally investigated and thermodynamically characterized by isothermal titration calorimetry (ITC), yielding a dissociation constant (KD) of ~25 µM, which is a DD typical affinity known from further characterized DD pairs. The artificial linking of the PaxB/C C/NDD pair via a glycine-serine (GS) linker facilitated the structure determination of the DD complex by solution nuclear magnetic resonance (NMR) spectroscopy. In comparison to known docking domain structures, this DD complex assembles in a completely new fold which is characterized by a central α-helix of PaxC NDD wrapped in two V-shaped α-helices of PaxB CDD. The first manuscript of this work focuses on the application of synthetic zippers (SZ) to mimic natural docking domains, enabling the easy assembly of NRPS building blocks encoded on different plasmids in a functional way. Here, the high-affinity interaction of SZs unambiguously defines the order of the synthetases derived from single-protein NRPSs in the engineered NRPS system and allows the recombination in a plug-and-play manner. Notably, the SZ engineering strategy even facilitates the functional assembly of NRPSs derived from Gram-positive and Gram-negative bacteria. Furthermore, the functional incorporation of SZs into NRPS modules is not limited to a specific linker region, so we could introduce them within all native NRPS linker regions (A-T, T-C, C-A). The second publication and the second manuscript of this thesis again focus on the multi-protein PaxS, in particular on the trans interface between the proteins PaxA and PaxB on a molecular level by solution NMR. Therefore, the PaxA CDD adjacent T domain was included into the structural investigation besides the native interaction partner PaxB NDD. Before a three-dimensional structure could be obtained from NMR data, the NH groups located in the peptide bonds had to be assigned to the respective amino acids of the proteins (backbone assignment). Based on these backbone assignments, the secondary structure of PaxA T1-CDD and PaxB NDD in the absence and presence of the respective interaction partner were predicted. The structural and functional characterization of the PaxA T1-CDD:PaxB NDD complex is summarized in manuscript two. The thermodynamic analysis of this complex by ITC determined a KD value of ~250 nM, whereas the discrete DDs did not interact at all. The high-affinity interaction allowed to determine the solution NMR structure of the PaxA T1-CDD:PaxB NDD complex without the covalent linkage of the interaction partners and an extended docking domain interface could be determined. This interface comprises on the one hand α-helix 4 of the PaxA T1 domain together with the α-helical CDD, and on the other hand the PaxB NDD, which is composed of two α-helices separated by a sharp bend. ...

An Exceptionally Large Pyoverdin from a Pseudomonas Strain Collected in Thailand+

2000 ◽  
Vol 55 (5-6) ◽  
pp. 323-327 ◽  
Author(s):  
Chalerm Ruangviryachai ◽  
Insa Barelmann ◽  
Regine Fuchs ◽  
Herbert Budzikiewicz
Keyword(s):  
Amino Acids ◽  
Soil Sample ◽  
Structure Elucidation ◽  
Peptide Chain

From a Pseudomonas strain obtained from a soil sample collected in Thailand a pyoverdin was obtained containing twelve amino acids in its peptide chain. The structure elucidation is described.

Muscle protein synthesis: regulation of a translational inhibitor

1984 ◽  
Vol 246 (6) ◽  
pp. E510-E515
Author(s):  
M. G. Buse ◽  
I. R. Cheema ◽  
M. Owens ◽  
B. E. Ledford ◽  
R. A. Galbraith
Keyword(s):  
Amino Acids ◽  
Protein Synthesis ◽  
Muscle Protein ◽  
Muscle Protein Synthesis ◽  
Diabetic Rats ◽  
Hormonal Control ◽  
Peptide Chain ◽  
Chain Initiation ◽  
Reticulocyte Lysates ◽  
Branched Chain

Insulin and branched-chain amino acids are known to stimulate protein synthesis in skeletal muscle. Extracts prepared from rat diaphragms after incubation in balanced salt solution and glucose alone yielded heat- and acid-stable, TCA-precipitable, nondialyzable factor(s) that inhibit protein synthesis when added to rabbit reticulocyte lysates. Polyribosomal profiles of inhibited lysates were consistent with a defect in peptide-chain initiation. Addition of insulin and amino acids to the diaphragm incubation media partially removed the inhibition seen with the muscle extract and was accompanied by an increase in polysomes and decreased subunits. Similarly, extracts prepared from rat hindlimb muscle 48 h after induction of diabetes were much more inhibitory in rabbit reticulocyte lysates than extracts from control rats. Polyribosomal profiles were consistent with defective peptide-chain initiation. Trypsin treatment before assay abolished the inhibitory activity of muscle extracts from diabetic rats. Because translation-inhibiting peptide(s) appear to be under metabolic and/or hormonal control, their possible role in muscle protein homeostasis warrants further study.

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