Peptide Chain Elongation: Discrimination against the Initiator Transfer RNA by Microbial Amino-acid Polymerization Factors

Nature ◽  
1968 ◽  
Vol 220 (5174) ◽  
pp. 1304-1307 ◽  
Author(s):  
YASUSHI ONO ◽  
ARTHUR SKOULTCHI ◽  
ALBRECHT KLEIN ◽  
PETER LENGYEL
Keyword(s):  
Amino Acid ◽  
Transfer Rna ◽  
Peptide Chain ◽  
Chain Elongation

Convergent peptide synthesis

1999 ◽  
Author(s):  
Kleomenis Barlos ◽  
Dimitrios Gatos
Keyword(s):  
Amino Acids ◽  
Amino Acid ◽  
Peptide Synthesis ◽  
Solid Phase ◽  
Peptide Chain ◽  
Chain Elongation ◽  
Peptide Fragments ◽  
Terminal Amino Acid ◽  
Convergent Synthesis ◽  
Terminal Amino

Besides the classical step-by-step synthesis, the convergent solid phase peptide synthesis (CSPPS) was developed for the preparation of complex and difficult peptides and small proteins. According to this method, suitably protected peptide fragments spanning the entire peptide sequence and prepared on the solid phase are condensed, either on a solid support or in solution, to the target peptide. Convergent synthesis is reviewed in recent publications. In this chapter, full experimental details are given for the preparation of complex peptides by applying convergent techniques, using 2-chlorotrityl chloride resin (CLTR) and Fmoc-amino acids. In the step-by-step peptide chain elongation the resin-bound C-terminal amino acid is reacted sequentially with suitably protected and activated amino acids. The peptide is thus elongated steadily towards the N-terminal direction. This is advantageous over the opposite direction where the elongation is performed from the N- to the C-terminus, because in the second case the growing peptide is activated at the C-terminal amino acid, which leads to its extensive racemization. This limits considerably the synthetic possibilities of the method. In convergent synthesis, no directional restrictions exist and the chain elongation can be performed with equal possibility to be successful to any direction. Figure 1 describes schematically the C- to N-terminal synthesis which is the most studied to date. The strategies where the synthesis begins from a central fragment and the peptide chain is extended to both C- and N-terminal directions and from the N-terminal towards the C-terminal can be considered, at the present time, to be in its infancy. In general, protected peptide fragments of any length can be used in the condensation reaction, if they are of satisfactory purity and solubility. Usually, fragments of up to 15 amino acids in length are used, because of their simpler purification by RP-HPLC compared with the longer peptides. The solubility of protected peptide acids is independent of their length. The selection of the correct fragments is very important for the success of convergent synthesis. It is helpful to analyse all available structural information, determined or calculated, for the target peptide. Peptide regions where β-turns are known to occur are readily identified as ‘difficult’ sequences during their synthesis.

Peptide Chain Elongation: GTP Cleavage catalysed by Factors binding Aminoacyl-Transfer RNA to the Ribosome

Nature ◽  
1969 ◽  
Vol 222 (5194) ◽  
pp. 645-648 ◽  
Author(s):  
Y. ONO ◽  
A. SKOULTCHI ◽  
J. WATERSON ◽  
P. LENGYEL
Keyword(s):  
Transfer Rna ◽  
Peptide Chain ◽  
Chain Elongation ◽  
Aminoacyl Transfer

scholarly journals Transfer RNA-dependent amino acid biosynthesis: An essential route to asparagine formation

2002 ◽  
Vol 99 (5) ◽  
pp. 2678-2683 ◽  
Author(s):  
B. Min ◽  
J. T. Pelaschier ◽  
D. E. Graham ◽  
D. Tumbula-Hansen ◽  
D. Soll
Keyword(s):  
Amino Acid ◽  
Amino Acid Biosynthesis ◽  
Transfer Rna ◽  
Acid Biosynthesis

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.

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