What is the molecular weight of cytochrome c?

What is the molecular weight of cytochrome c?

12,000 Da
Cytochrome c (Cytc) comprises 104 amino acids and is a nuclear-encoded mitochondrial protein. This peripheral membrane protein is in spherical shape and has a molecular weight of 12,000 Da.

How many Daltons is cytochrome c?

12,000 daltons
Cytochrome c is a highly conserved protein across the spectrum of species, found in plants, animals, and many unicellular organisms. This, along with its small size (molecular weight about 12,000 daltons), makes it useful in studies of cladistics.

How do you calculate cytochrome c?

The concentration of equine cytochrome c is calculated using the extinction coefficient at a given wavelength. 30ul of Reduced cytochrome c had an absorbance of 0.702 at 550 nm = 0.0332M (before adding mitochondria) and an absorbance of 0.135 at 550 nm =0.0063M (following the assay).

Why is cytochrome c so highly conserved?

1.5. Why is cytochrome c so conserved? The answer may partially lie in its size, the requirement for a heme-binding pocket, and its role as an interacting partner of proteins involved in both electron transport and apoptosis. These 22 residues are highly conserved.

What is the kDa of cytochrome c?

Cytochrome c is a highly conserved ~12 kDa protein consisting of a single 104 amino acid peptide with a single heme group, which is covalently attached to Cys14 and Cys17. Because of its ubiquitous nature and sequence homology, cytochrome c has been used as a model protein for molecular evolution.

What is the molecular weight of BSA?

The molecular weight of BSA has frequently been cited as 66,1201 or 66,2672, but it was revised in 1990 to 66,4303. All three values are based on amino acid sequence information available at the time of publication.

What is the molecular weight of myoglobin?

approximately 17 kDa
Myoglobin is a small cytoplasmic heme-containing protein with a molecular weight of approximately 17 kDa, which is found in both skeletal and cardiac muscle.

What is cytochrome c do?

Cytochrome c is functionally involved in the electron transport chain of mitochondria. That electron transport is part of the pathway for synthesis of ATP. The role of cytochrome c is to carry electrons from one complex of integral membrane proteins of the inner mitochondrial membrane to another (Fig.

What is cytochrome c amino sequence?

How does cytochrome c cause apoptosis?

In the cytosol, Cyt c mediates the allosteric activation of apoptosis-protease activating factor 1, which is required for the proteolytic maturation of caspase-9 and caspase-3. Activated caspases ultimately lead to apoptotic cell dismantling.

What is the role of cytochrome c in apoptosis?

Mitochondrial cytochrome c (cyt c) has been found to have dual functions in controlling both cellular energetic metabolism and apoptosis. Through interaction with apoptotic protease activating factors (Apaf), cyt c can initiate the activation cascade of caspases once it is released into the cytosol.

How long is cytochrome c?

cytochrome c, somatic: Calculated molecular weight: 12 kDa: Observed molecular weight: 12-15 kDa: GenBank accession number: BC009578: Gene symbol: CYCS: Gene ID (NCBI) 54205 Conjugate: Unconjugated: Form: Liquid: Purification Method: Antigen affinity purification: Storage Buffer: PBS with 0.02% sodium azide and 50% glycerol pH 7.3.

Why is cytochrome c used as a model protein?

Cytochrome c is a highly conserved ~12 kDa protein consisting of a single 104 amino acid peptide with a single heme group, which is covalently attached to Cys 14 and Cys 17. Because of its ubiquitous nature and sequence homology, cytochrome c has been used as a model protein for molecular evolution. 1

How is the cytochrome c’dimer crystallographically created?

The cytochrome c’ dimer is created by a crystallographic twofold axis. Monomer-monomer contacts primarily involve the two A helices, with size complementarity of side chains in a central solvent-excluded portion of the interface and hydrogen bonding at the periphery. Both species have a pyroglutamic acid N-terminal residue.

Is the redox potential of cytochrome c the same for wheat?

For example, human cytochrome oxidase reacts with wheat cytochrome c, in vitro; which held true for all pairs of species tested. In addition, the redox potential of +0.25 volts is the same in all cytochrome c molecules studied.

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