Chromatography is a group of techniques to divide components of a mixtures basically on the ground of their physical dimension, even if elected types of chromatography exists where separation happens for example on the ground of electron affinity.
In general terms the mixture is dissolved in a fluid called the mobile phase, which carries it through a structure holding another material called the stationary phase. The various constituents of the mixture travel at different speeds in the stationary phase, causing them to separate.
Liquid phase chromatography is the most used type of chromatography, where the mobile phase is a liquid and the stationary phase a material composed of very small particles strictly packed one with the other. Also gas chromatography, where the mobile phase is a gas, is largely used.
The name chromatography derives from the fact that the very first version of this separation techniques used different colors added to the mobile phase in different moments to visually distinguish the components coming out from the chromatographic column in different moments, but this technique is no more used, substituted by more sophisticate ways to quantify components that comes out in different instants from the chromatographic column.
Optical detection is frequently used, generally illuminating the flow out of the column with UV light and observing fluorescence lines. The fluorescence intensity is proportional for diluted solutions to the concentration of the substance presenting the observed optical transition. Since many proteins are characterized by well identified fluorescence lines this detection method can be used for proteins quantification.
Most often it doesn't. Are you thinking about gas chromatography? I have used HPLC at room temperature for reversed phase analysis of organics and I have used it at 4 degrees C for protein purification. Only once have I done any at elevated temperature. Gas chromatography uses gas-liquid partitioning though and is almost always done at higher temperatures.
I think Sodium is protein because I forget what is a protein and a sodium
Protein Protein
A protein chemist is a chemist that studies the properties of proteins. Protein chemists study the structure of protein and how it is absorbed into the body.
The polymer of protein is protein .
chromatography has many varieties -paper chromatography, sometime complexe mixtures cant be separated, TLC plates do not have long stationary phases -gaz chromatography: the molecule should be volatile -Chiral Chromatography can be expensive - Ion Exchange or Ion Chromatography: Turbidity should be low below 10ppm -Size Exclusion Chromatography: low resolution technique which gives few peaks and requires large differences in molecular weight for resolution -Gel chromatography: the target protein frequently becomes an abundant substrate for proteases that may also be present in the mixture. Another disadvantage is low sample handling.
molecular exclusion chromatography is the exclusion or separation of protein particles based on their molecular size. Bhubanyu Basu
affinity chromotography
Protein complementation is a technique that combines foods with limiting amino acids. this is done to improve protein quality in the human body.
To answer this question, the mass of the spherical protein is needed. the fact that the protein is a sphere and that it has a density of 1gcm3 is not enough information to determine the diameter.
Ion chromatography involves the separation of ions and polar molecules and is used for protein purification, among other things. Information about this process can be found at Wikipedia or InnovaTech.
A binding buffer is a substance used in chromatography to fix a specific compound.For example this buffer can be linked to a protein.
Chi-Wei Lan has written: 'Protein purification using fluidised bed chromatography'
Protein would be most helpful for muscle growth. Bone density is affected most by calcium intake...which you can get from milk or a pill.
Blood typing
If you meant "protein gel electrophoresis" (considering the image on this page) is a very powerful technique and widely used to separate proteins according to their mass, molecular weight and charge. The support most used for this technique is the polyacrylamide.
site-direct mutagenesis