Protein methods

technique used for determining the atomic or molecular structure of a crystal, in which the ordered atoms cause a beam of incident X-rays to diffract into specific directions

protein that converts blue and ultraviolet light ranges to green light

analytical technique used in molecular biology

method for separation and analysis of macromolecules

thumb|230px|Main staining patterns on chromogenic immunohistochemistry. thumb|right|Immunofluorescence of human skin using an anti-IgA antibody. The skin is from a patient with [[Henoch–Schönlein purpura: IgA deposits are found in the walls of small superficial capillaries (yellow arrows). The pale wavy green area on top is the epidermis, the bottom fibrous area is the dermis.]] thumb|"Block" staining: strong nuclear and cytoplasmic expression in a continuous segment of cells. Immunohistochemistry is a form of immunostaining. It involves the process of selectively identifying antigens in cells

chemical test for detecting peptide bonds

technique for separating different molecules by differences in their isoelectric point; a type of zone electrophoresis

Method used to detect protein in a solution

biochemical method

constructing an atomic-resolution model of a protein from its amino acid sequence

method to determine protein concentration

Immunoprecipitation (IP) is the technique of precipitating a protein antigen out of solution using an antibody that specifically binds to that particular protein. This process can be used to isolate and concentrate a particular protein from a sample containing many thousands of different proteins. Immunoprecipitation requires that the antibody be coupled to a solid substrate at some point in the procedure.

laboratory technique

separation of protein

artificial peptide attached to protein for marking purpose

laboratory method for measuring enzymatic activity

Aequorin is a calcium-activated photoprotein isolated from the hydrozoan Aequorea victoria. Its bioluminescence was studied decades before the protein was isolated from the animal by Osamu Shimomura in 1962. In the animal, the protein occurs together with the green fluorescent protein to produce green light by resonant energy transfer, while aequorin by itself generates blue light.

Non-destructive elemental analysis technique

align molecular sequences using sequence and structural information

laboratory technique to analyze protein

Sakaguchi reaction on arginine

thumb|Crossed immunoelectrophoresis of 2 microlitres of normal human serum. The electrophoresis was performed in thin layers of agarose; the pictured gel is about 7x7 cm. The lower part is the first dimension gel without antibodies, where the serum was applied into the slot at the lower left. The upper part is the second dimension gel with Dako antibodies against human serum proteins. More than 50 major serum proteins can be named.

method of protein structure prediction

molecular biology technique for determining protein-nucleic acid interactions in vitro

field of structural biology

biochemical laboratory technique

analytical technique for protein identification

thumb|Immunocytochemistry labels individual proteins within cells, such as Tyrosine hydroxylase|TH (green) in the [[axons of sympathetic autonomic neurons.]]

measures the real and imaginary components of the complex refractive index

Chemical test for amino acid detection

thumb|400px|Workflow overview of a ChIP-on-chip experiment. ChIP-on-chip (also known as ChIP-chip) is a technology that combines chromatin immunoprecipitation ('ChIP') with DNA microarray ("chip"). Like regular ChIP, ChIP-on-chip is used to investigate interactions between proteins and DNA in vivo. Specifically, it allows the identification of the cistrome, the sum of binding sites, for DNA-binding proteins on a genome-wide basis. Whole-genome analysis can be performed to determine the locations of binding sites for almost any protein of interest. As the name of the technique suggests, such pr

a chemical test

biochemical technique

thumb|350px|Micrograph of a GFAP immunostained section of a [[brain tumour.]]

Electrochromatography is a chemical separation technique in analytical chemistry, biochemistry and molecular biology used to resolve and separate mostly large biomolecules such as proteins. It is a combination of size exclusion chromatography (gel filtration chromatography) and gel electrophoresis. These separation mechanisms operate essentially in superposition along the length of a gel filtration column to which an axial electric field gradient has been added. The molecules are separated by size due to the gel filtration mechanism and by electrophoretic mobility due to the gel electrophoresi

molecular biology technique

The effect of high concentrations of macromolecules in living cells

molecular biology technique