Tetrameric Collection

Bacteriophage DNA recombination F006 / 9554
Bacteriophage DNA recombination. Molecular model showing DNA manipulation and recombination taking place at a Holliday junction with a bacteriophage enzyme

Carbamoylsarcosine amidase enzyme, molecular model. This enzyme catalyses the chemical reaction that converts the chemical N-carbamoylsarcosine in the presence of water to sarcosine (N-methylglycine)

Influenza proton pump, molecular model
Influenza proton pump. Molecular model showing the protein structure of a proton pump from an influenza virus. Proton pumps are membrane proteins that move protons across a cell membrane

Cat allergen protein, molecular model C015 / 3962
Cat allergen protein. Molecular model of the tetrameric form of the major cat allergen fel d 1 (Felis domesticus allergen 1)

Cat allergen protein, molecular model
Cat allergen protein. Molecular model of the tetrameric form of the major cat allergen fel d 1 (Felis domesticus allergen 1)

cAMP-dependent protein kinase molecule C016 / 2063
cAMP-dependent protein kinase, molecular model. This enzyme is also known as protein kinase A (PKA). This is the holoenzyme, which consists of two regulatory subunits and two catalytic subunits

Newcastle disease virus protein C015 / 6912
Newcastle disease virus protein, molecular model. This is a hemagglutinin-neuromidase (HN) protein that enables the virus to bind to and infect host cells

Plant agglutinin protein C015 / 6107
Plant agglutinin protein, molecular model. This example, from the hedge-apple (Maclura pomifera), is known as Maclura pomifera agglutinin (MPA). It is a tetrameric plant seed lectin

Plant agglutinin protein C015 / 6106
Plant agglutinin protein, molecular model. This example, from the hedge-apple (Maclura pomifera), is known as Maclura pomifera agglutinin (MPA). It is a tetrameric plant seed lectin

Cholera virulence regulator protein C015 / 6727
Cholera virulence regulator protein, molecular model. This protein is AphB, a virulence gene activator from the Vibrio cholerae bacterium

Cholera virulence regulator protein C015 / 6726
Cholera virulence regulator protein, molecular model. This protein is AphB, a virulence gene activator from the Vibrio cholerae bacterium

Interferon antagonism by viral protein C015 / 5421
Interferon (IFN) antagonism by viral protein. Molecular model of an orthopoxvirus IFN-gamma-binding protein tetramer bound to an IFN-gamma dimer

Interferon antagonism by viral protein C015 / 5420
Interferon (IFN) antagonism by viral protein. Molecular model of an orthopoxvirus IFN-gamma-binding protein tetramer bound to an IFN-gamma dimer

Transthyretin blood protein C016 / 2327
Transthyretin blood protein. Molecular model of the thyroid hormone binding protein transthyretin, also known as prealbumin

Transthyretin blood protein C016 / 2326
Transthyretin blood protein. Molecular model of the thyroid hormone binding protein transthyretin, also known as prealbumin

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"Tetrameric Marvels: Unveiling the Intricate World of Protein Structures" In the realm of molecular biology, tetrameric structures have emerged as captivating entities that hold immense significance in various biological processes. These remarkable assemblies consist of four subunits intricately arranged to form a cohesive unit, exhibiting extraordinary functionality and versatility. One such example is the cAMP-dependent protein kinase molecule F006/9728. This tetrameric powerhouse plays a pivotal role in cellular signaling pathways, orchestrating crucial biochemical reactions within our cells. Delving further into the intricate web of tetramerism, we encounter Bacteriophage DNA recombination F006/9554. This fascinating structure showcases how these tetramers facilitate genetic exchange between viral DNA strands, enabling bacteriophages to evolve and adapt rapidly. Moving on to another intriguing aspect, we explore the Influenza proton pump's molecular model. Here, we witness not one but two instances of this mesmerizing tetramer formation. These pumps play an indispensable role in maintaining pH balance within influenza viruses' interior compartments – an essential mechanism for their survival and replication. Shifting gears slightly while still reveling in the world of enzymes, Carbamoylsarcosine amidase enzyme emerges as yet another captivating example. Its unique tetrameric architecture enables it to catalyze vital metabolic reactions with exceptional efficiency and precision. Returning once again to Bacteriophage DNA recombination and Influenza proton pump models, we are reminded of their recurrent presence among these awe-inspiring structures. Their prevalence underscores their fundamental importance across diverse biological systems. Finally, let us not forget Cat allergen protein C015/3962 – a striking molecular model showcasing yet another instance where nature harnesses the power of tetramerism. Understanding its structure aids scientists in developing strategies for combating allergies caused by feline companionship.