Sequence-Specific Ni(II)-Dependent Peptide Bond Hydrolysis for Protein Engineering: Reaction Conditions and Molecular Mechanism

2010 ◽  
Vol 49 (14) ◽  
pp. 6636-6645 ◽  
Author(s):  
Edyta Kopera ◽  
Artur Krȩżel ◽  
Anna Maria Protas ◽  
Agnieszka Belczyk ◽  
Arkadiusz Bonna ◽  
...  
Keyword(s):  
Protein Engineering ◽  
Molecular Mechanism ◽  
Peptide Bond ◽  
Reaction Conditions

scholarly journals Adaptation of bird hemoglobins to high altitudes: demonstration of molecular mechanism by protein engineering.

1991 ◽  
Vol 88 (15) ◽  
pp. 6519-6522 ◽  
Author(s):  
T. H. Jessen ◽  
R. E. Weber ◽  
G. Fermi ◽  
J. Tame ◽  
G. Braunitzer
Keyword(s):  
Protein Engineering ◽  
Molecular Mechanism ◽  
High Altitudes

scholarly journals Sequence-specific Ni(II)-dependent peptide bond hydrolysis for protein engineering: Active sequence optimization

2013 ◽  
Vol 127 ◽  
pp. 99-106 ◽  
Author(s):  
Anna Maria Protas ◽  
Hanieh Hossein Nejad Ariani ◽  
Arkadiusz Bonna ◽  
Agnieszka Polkowska-Nowakowska ◽  
Jarosław Poznański ◽  
...  
Keyword(s):  
Protein Engineering ◽  
Peptide Bond ◽  
Sequence Optimization

scholarly journals The interaction of α2-macroglobulin with proteinases. Characteristics and specificity of the reaction, and a hypothesis concerning its molecular mechanism

1973 ◽  
Vol 133 (4) ◽  
pp. 709-724 ◽  
Author(s):  
Alan J. Barrett ◽  
Phyllis M. Starkey
Keyword(s):  
Conformational Change ◽  
Molecular Mechanism ◽  
Active Site ◽  
Peptide Bond ◽  
Serine Proteinases ◽  
Equimolar Ratio ◽  
Binding Characteristics ◽  
Sensitive Region ◽  
Physiological Importance ◽  
Α2 Macroglobulin

1. α2-Macroglobulin is known to bind and inhibit a number of serine proteinases. We show that it binds thiol and carboxyl proteinases, and there is now reason to believe that α2-macroglobulin can bind essentially all proteinases. 2. Radiochemically labelled trypsin, chymotrypsin, cathepsin B1 and papain are bound by α2-macroglobulin in an approximately equimolar ratio. Equimolar binding was confirmed for trypsin by activesite titration. 3. Pretreatment of α2-macroglobulin with a saturating amount of one proteinase prevented the subsequent binding of another. We conclude that each molecule of α2-macroglobulin is able to react with one molecule of proteinase only. 4. α2-Macroglobulin did not react with exopeptidases, non-proteolytic hydrolases or inactive forms of endopeptidases. 5. The literature on binding and inhibition of proteinases by α2-macroglobulin is reviewed, and from consideration of this and our own work several general characteristics of the interaction can be discerned. 6. A model is proposed for the molecular mechanism of the interaction of α2-macroglobulin with proteinases. It is suggested that the enzyme cleaves a peptide bond in a sensitive region of the macroglobulin, and that this results in a conformational change in the α2-macroglobulin molecule that traps the enzyme irreversibly. Access of substrates to the active site of the enzyme becomes sterically hindered, causing inhibition that is most pronounced with large substrate molecules. 7. The possible physiological importance of the unique binding characteristics of α2-macroglobulin is discussed.

Sequence-Specific Ni(II)-Dependent Peptide Bond Hydrolysis for Protein Engineering. Combinatorial Library Determination of Optimal Sequences

2010 ◽  
Vol 132 (10) ◽  
pp. 3355-3366 ◽  
Author(s):  
Artur Krȩżel ◽  
Edyta Kopera ◽  
Anna Maria Protas ◽  
Jarosław Poznański ◽  
Aleksandra Wysłouch-Cieszyńska ◽  
...  
Keyword(s):  
Protein Engineering ◽  
Combinatorial Library ◽  
Peptide Bond

Backbone-modified oligopeptidic bioregulators. The synthesis and configuration of thioamide, amidoxime, cyanoamidine, and amidrazone analogs of the chemotactic peptide N-formyl-methionyl-leucyl-phenylalanine (f-Met-Leu-Phe-OR)

1985 ◽  
Vol 63 (11) ◽  
pp. 3089-3101 ◽  
Author(s):  
Gilles Sauvé ◽  
Vanga S. Rao ◽  
Gilles Lajoie ◽  
Bernard Belleau
Keyword(s):  
Nuclear Magnetic Resonance ◽  
Biological Activity ◽  
Magnetic Resonance ◽  
Peptide Bond ◽  
Chemotactic Peptide ◽  
Reaction Conditions ◽  
Nuclear Magnetic

Reaction conditions for the synthesis of thioamide, amidoxime, and N-substituted amidine analogs of the peptide bond are described. Several new amidine analogs of the chemotactic peptide f-Met-Leu-Phe-OR were synthesized using the thioamides as precursors. The assignment of the E/Z configuration was accomplished by nuclear magnetic resonance. The biological activity of these analogs is briefly described.

Undecagold labeling of tRNA

1991 ◽  
Vol 49 ◽  
pp. 44-45
Author(s):  
James F. Hainfeld ◽  
Kyra M. Alford ◽  
Mathias Sprinzl ◽  
Valsan Mandiyan ◽  
Santa J. Tumminia ◽  
...  
Keyword(s):  
High Resolution ◽  
Transmission Electron Micrograph ◽  
Anticodon Loop ◽  
Electron Micrograph ◽  
Reaction Conditions ◽  
Scanning Transmission Electron ◽  
Transmission Electron ◽  
Scanning Transmission

The undecagold (Au11) cluster was used to covalently label tRNA molecules at two specific ribonucleotides, one at position 75, and one at position 32 near the anticodon loop. Two different Au11 derivatives were used, one with a monomaleimide and one with a monoiodacetamide to effect efficient reactions.The first tRNA labeled was yeast tRNAphe which had a 2-thiocytidine (s2C) enzymatically introduced at position 75. This was found to react with the iodoacetamide-Aun derivative (Fig. 1) but not the maleimide-Aun (Fig. 2). Reaction conditions were 37° for 16 hours. Addition of dimethylformamide (DMF) up to 70% made no improvement in the labeling yield. A high resolution scanning transmission electron micrograph (STEM) taken using the darkfield elastically scattered electrons is shown in Fig. 3.

Role of the Small (40S) Subunits in the Structure of the Interface of Eukaryotic Ribosomes

1980 ◽  
Vol 38 ◽  
pp. 548-549
Author(s):  
M. Boublik ◽  
N. Robakis ◽  
W. Hellmann ◽  
F. Jenkins
Keyword(s):  
Structural Similarity ◽  
High Resolution Electron Microscopy ◽  
Peptide Bond ◽  
Uranyl Acetate ◽  
Mutual Orientation ◽  
Mutual Position ◽  
Peptide Bond Formation ◽  
Resolution Electron ◽  
Direct Technique ◽  
Structural Details

Ribosomes are ribonucleoprotein particles which process the genetic information coded in mRNA into protein synthesis. The analogy in function and composition of ribosomes from various sources, both prokaryotic and eukaryo-tic, imply a structural similarity. At present, high resolution electron microscopy is the most direct technique with a potential to resolve the extent of the structural homology of ribosomal particles at a macromolecular level. The structure of ribosomes is highly complex as a result of the large number of their constituents. In general, 80S eukaryotic monosomes consist of two uneven subunits - large (60S) and small (40S) - accomodating four different RNAs and approximately 80 different proteins. Mutual orientation of both subunits on the monosome is of particular interest because it determines the interface, the supposed site of interactions of ribosomes with other macro-molecules involved in peptide bond formation. Since entrapping of the contrasting solution (0.5% aqueous uranyl acetate) obscures all structural details in the interface, information on its architecture is limited to an indirect reconstruction based on the established 3-D structure of both sub-units and their mutual position after association.

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