This question has to be answered depending upon the meaning of a research project that involves proteins.
The estimation of proteins can be done to know the protein fraction of a sample collected from the field, either if the protein content will be isolated to be studied, or to remove protein fraction from the sample (sometimes the investigator does not want that proteolytic enzymes chew a target molecules or cellular structures).
Another application is when an enzymatic reaction is going to be performed to digest a particular protein in an aliquot, the protein content is crucial for stoichometric purposes.
On the other hand, if the research imply the work with nucleic acids, is very important "to inactivate" the nucleolytic enzymes present in cytoplasmic fluids from lysed cells with specific inactivators, chemical or biochemical, added in correct levels according to protein contents.
Protein estimation is very useful when planning diet and exercise. A person needs to know what foods contain proteins so that they are sure to eat healthy.
folin lowry method,
biuret method,
bradfoard method
bb b n nbn n
lowrys method
No. It is a non-invasive method
because folin lowry reagent has absorption maxima at 660 nm
Most molecules can move in and out of a cell, but different molecules have different methods of getting in- Small Non-Polar molecules can diffuse across the lipid bilayer Medium sized molecules of any kind require a specific protein channel HUGE MOLECULES require a process called endo and exocytosis
When you use methods such as Solvent precipitation, you precipitate a protein molecule but this protein molecule normally does not have the same structure as that of protein in a solution (for example disulfide bonds do not connect the same amino acids) and it is not easy to change this to that of original structure even when the same solution is present. The percent of recovery means the percent that these denatured protein molecules can gain the same structure that they have in the solution before precipitation.
a denature protein may re-form to its functional shape when returned to its normal environment. what does that indicate about a protein's conformation? Proteins fold in natural environment (water) in a way that they are stable, but a non-polar solvent provides a very different environment, so the protein has to unfold and adopt a very different shape.
There are a few methods in estimation. Like framework, unknown parameters, empirical dist and substitution principle most of these methods can be used using substitution principles.
diphenylamine reagent
gand mara
by comparing the colours or the amount of precipitate
For example concentration determination with a salinometer.
Sodium bicarbonate is not necessarily used in the estimation of protein. There are very many protein assays on the market, and the vast majority of them do NOT use NaHCO3. Look up Lowry, Biuret, Bradford, etc.
No. It is a non-invasive method
There is no single word. Mathematical methods, alone, could involve analytical methods, statistical methods of estimation or numerical methods for approximation.
here the amount of protein in a sample can be determined, using different protocols, wherein the reagent mixture( ex: FC reagent) which when added to the sample containing protein reacts with the specific amino acids giving colour, thus the amount of protein in a sample can be estimated and the data used for further protein studies.
High Performance Liquid Chromatography can be used for the estimation ofmost of the antiepilleptic drugs
O. Richter has written: 'Parameter estimation in ecology' -- subject(s): Ecology, Mathematical models, Parameter estimation, Statistical methods
Average protein estimation in snake venom is from 49.8 to 96.4% . the age of the snake may affect the percentage of protein content found in the venom