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What is the molar mass of c-phycocyanin?
The alpha chain is 18 kda and the beta is 21 kda. But usually Phycocyanin exists as trimer along with some linker peptides. The molecular weight of trimer is 121 kda
What are Molecules made of identical monomers called?
2=dimers, 3=trimer, 4=tetramer, 5-20 I think is deemed oligomers, >20 is polymer
What types of protein are made through protein synthesis?
protein
What is the characteristic of protein?
analysing the function of a particular protein is protein characterization.
Is hemoglobin consider as globular protein and conjugated protein?
Yes, hemoglobin is considered a globular protein because of its compact, roughly spherical structure. It is also classified as a conjugated protein because it consists of a protein component (globin) and a non-protein prosthetic group (heme).
What is the Proper oil gas mixture for a homelite gas trimer?
2%
What is a protein made up of three separate polypeptides called?
A protein made up of three separate polypeptides is called a trimer. Trimeric proteins consist of three individual protein subunits that come together to form a functional complex. Each of the three polypeptides in a trimeric protein may contribute unique structural and functional properties to the overall structure.
What is the gas-oil mix for ryobi 31cc 18 inch trimer?
32:1
What is the molar mass of c-phycocyanin?
The alpha chain is 18 kda and the beta is 21 kda. But usually Phycocyanin exists as trimer along with some linker peptides. The molecular weight of trimer is 121 kda
What is the molar mass of C?
The alpha chain is 18 kda and the beta is 21 kda. But usually Phycocyanin exists as trimer along with some linker peptides. The molecular weight of trimer is 121 kda
How many polypeptide chains are in a protein?
There is one polypeptide chain in a single protein chain. Polypeptides refer to short protein chains - for example insulin is a 53 amino acid protein and is considered a large polypeptide. Complex multi-component [strand] protein coalescences exist - each uniquely identified component protein strand is called - of course - a subunit: two subunits is called a dimer, three subunits is called a trimer, four is a tetramer etc. A Protein is a string of Pearls {Amino Acids} of which [out of the quadrillion possible] there are ONLY Twenty Biologically Active Types ( with two, sometimes three, more reserved for special occasions ). A common example of a biological multi-strand protein grouping is: 4 strands will combine thusly - 2 strands of one type and 2 strands of another type.
What are Molecules made of identical monomers called?
2=dimers, 3=trimer, 4=tetramer, 5-20 I think is deemed oligomers, >20 is polymer
Why does water behave differently at 0 C?
At 0C water is divided in two forms (H20)3 and (H20)4. One is a Trimer and other is a quadramer this is the reason . Dhrubajyoti Gupta dhruba.gupta.56@gmail.com
How is egg protein different from meat protein?
Egg protein gives off less protein then meat protein.
Which protein can be phosphorylated by protein kinase AA?
The protein that can be phosphorylated by protein kinase AA is called protein X.
What are some highly recommended protein powders for body builders?
Some highly recommended protein powders for body builders are: Whey protein, soy protein, hydrolysed whey protein, whey protein isolate, egg protein, micellar casein protein, beef protein and plant protein.
Difference between native page and sds page?
In SDS-PAGE complexes are separated to their subunits, proteins are denatured and covered by SDS molecules at a ratio of approximately 1 SDS molecule per 2 amino acids. Thus any charge that the protein might have is masked by he huge negative charge by the SDS molecules and migration and thus separation of proteins depends mainly on their size. That's why SDS page is commonly used for determing approximate molecular weight of proteins, for following the progress of protein purification, etc. In native PAGE proteins retain their natural fold and can remain in complex. So the migration depends on the charge of the protein, the size, shape and if it is in complex with other molecules or if it oligomerizes. For a example a protein that forms tetramers will give one band in an SDS-PAGE that corresponds to the monomer (provided that denaturation is complete) while on a native PAGE it can give more than one band, depending on the amount of each species (monomer, dimer, trimer, tetramer) From native PAGE usually in combination with other techniques you can see the oligomerization state of your protein or study complexation reactions like protein-DNA (band-shift assays).
