Which type of protein is used in Shampoos?
913655
yeah, i agree with what Smokeybon said and some examples of those amino acids are proline, histidine and others look at some shampoo bottles
978346
use coconut based shampoo
1174148
try a medicated shampoo
904005
hair is made up of proteins. and the monomer of a protein is an amino acid, in that it has an amino complex on it that can accept a proton of hydrogen, it also has a carboxyl end that can donate a hydrogen proton... in the case of bleach, you end up with the carboxyl end donating a proton and it binds with the Cl to form HCl aqueous, causing a change in pH. Now dont be quoting that to your teachers.... that is only my understanding of how it could be a acid/base rxn.
960830
Proteins, amino acids.
27974
Each cell in the human body contains thousands of different proteins, the most abundant and diverse class of biomolecules. Proteins are, in fact, present in the cells of all living organisms, though each different species contains a slight to major variation in the number and type of the biomolecules so that there are literally millions of different proteins that exist in the biological world. Proteins play a major role both in cellular structure and function, some being involved in such activities as transport, catalysis, storage, contraction, and protection, while others form critical parts of the cytoskeleton. The types of protein differ from cell to cell, but all have the same basic structure with respect to the constituent amino acids that make up the backbone. Most proteins are biological macromolecules that range in molecular weight from about 6,000 to several million Daltons. They are all polymers that are composed of covalently linked amino acids. The number, chemical nature, and sequential order of amino acids in a protein chain determine the distinctive structure and characteristic chemical behavior of each protein.\n\nAs for order of quantities:\n ~25% of the proteins found in the body are classified as collagens. Followed by keratins, the muscle proteins actin and myosin then hemoglobin.
511902
proteins and calcium carbonate.
785808
usually protein with some metallic ions
789020
moisture\nsoap\ntoner\ncleanser\nvitamins
849528
In order to perform in vitro analyses, a protein must be purified away from other cellular components. This process usually begins with cell lysis, in which a cell's membrane is disrupted and its internal contents released into a solution known as a crude lysate. The resulting mixture can be purified using ultracentrifugation, which fractionates the various cellular components into fractions containing soluble proteins; membrane lipids and proteins; cellular organelles, and nucleic acids. Precipitation by a method known as salting out can concentrate the proteins from this lysate. Various types of chromatography are then used to isolate the protein or proteins of interest based on properties such as molecular weight, net charge and binding affinity. The level of purification can be monitored using gel electrophoresis if the desired protein's molecular weight is known, by spectroscopy if the protein has distinguishable spectroscopic features, or by enzyme assays if the protein has enzymatic activity.\n\nFor natural proteins, a series of purification steps may be necessary to obtain protein sufficiently pure for laboratory applications. To simplify this process, genetic engineering is often used to add chemical features to proteins that make them easier to purify without affecting their structure or activity. Here, a "tag" consisting of a specific amino acid sequence, often a series of histidine residues (a "His-tag"), is attached to one terminus of the protein. As a result, when the lysate is passed over a chromatography column containing nickel, the histidine residues ligate the nickel and attach to the column while the untagged components of the lysate pass unimpeded.\n\n\n[edit] Cellular localization\n \nProteins in different cellular compartments and structures tagged with green fluorescent protein.The study of proteins in vivo is often concerned with the synthesis and localization of the protein within the cell. Although many intracellular proteins are synthesized in the cytoplasm and membrane-bound or secreted proteins in the endoplasmic reticulum, the specifics of how proteins are targeted to specific organelles or cellular structures is often unclear. A useful technique for assessing cellular localization uses genetic engineering to express in a cell a fusion protein or chimera consisting of the natural protein of interest linked to a "reporter" such as green fluorescent protein (GFP). The fused protein's position within the cell can be cleanly and efficiently visualized using microscopy, as shown in the figure opposite.\n\nThrough another genetic engineering application known as site-directed mutagenesis, researchers can alter the protein sequence and hence its structure, cellular localization, and susceptibility to regulation, which can be followed in vivo by GFP tagging or in vitro by enzyme kinetics and binding studies.\n\n\n[edit] Proteomics and bioinformatics\nMain articles: Proteomics and Bioinformatics\nThe total complement of proteins present in a cell or cell type is known as its proteome, and the study of such large-scale data sets defines the field of proteomics, named by analogy to the related field of genomics. Key experimental techniques in proteomics include protein microarrays, which allow the detection of the relative levels of a large number of proteins present in a cell, and two-hybrid screening, which allows the systematic exploration of protein-protein interactions. The total complement of biologically possible such interactions is known as the interactome. A systematic attempt to determine the structures of proteins representing every possible fold is known as structural genomics.\n\nThe large amount of genomic and proteomic data available for a variety of organisms, including the human genome, allows researchers to efficiently identify homologous proteins in distantly related organisms by sequence alignment. Sequence profiling tools can perform more speci
193794
Formalin doesnt directly bind the protein, it catalyzes proteins to bind each other, making a large protein-polymer structure.  There isnt any way of reversing this other than to use proteases, which will merely chop the protein up.
928892
Sucrose -- carbon, hydrogen, oxygen\nFat -- carbon, hydrogen, oxygen\nNitrogen -- carbon, hydrogen, oxygen, nitrogen (2 of the 20 commonly incorporated into protein contain sulfur)
750861
Glucose and proteins are not ions.
832426
Soap is a molecule that consist of long carbon chain ending in -COONa. The latter endchain easily attaches to water and the carbon chain attaches to fats and grease.  Although grease will normally adhere to skin or clothing, the soap molecules can attach to it as a "handle" and make it easier to rinse away.
1141956
I haven't tried this, but often the best people to answer these type of questions are the companies that make the membranes. For protein work we use a number of different types of membrane including nitrocellulose and PVDF. \nI have not heard of people electroblotting RNA, regular capillary blotting is most commonly used. You could try the following website for some info (but try some other manufacturers as well).\n\nhttp://www6.amershambiosciences.com/aptrix/upp01151.nsf/Content/e-tech_support_homePage
109653
Did you know that raw eggs can be used as part of your beauty routine and not just on your face? You can also use them in your hair for conditioning and adding shine. Here are some recipes that you can use before you shampoo or after. The choice is yours. \nThese conditioners you use before shampooing: \n\nFirst of all an egg yolk makes a great conditioner for your hair. Simply mix it with 2 tsp of a castor oil and massage into your hair. Rinse thoroughly.\n\nOne raw egg...\nWhisk one or two raw eggs together and then work into your hair. Allow to dry and then shampoo out, followed by a vinegar and water rinse. This treatment will soften your hair nicely.
327822
Are you looking at any protein in particular?  Look up in situ hybrdization for proteins ( at least it will give you an idea where it is localised).  I think that it would really depend on the system ad proteins that you want to study, so I am not sure how much else I can tell you, sorry.