why do proteins froth?
485222
I think its bcoz of some lyophobic particles present... im not sure..... jus guessin...
756226
The proteins shape determines its function.  Most proteins have to bind to something else in order to do its job.  If it's not a specif shape, it can't bind.
736055
when the solvent (liquid) can no longer dissolve any more solute (solid) and particles of the solute remain in the solution.\n\neg: sugar in tea...if you add too much sugar (solute) to the tea (solvent) the sugar sinks to the bottom and wont dissolve. \n\nTasty but saturated!
54079
There are numerous proteins embedded in the lipid bilayer of the cell membrane; some, like adrenergic receptors and porins (channels things move through), perforate the membrane; others protrude out one part, not another.  Others, like the G-proteins and the enzymes that phosphorlate and dephosphorylate other membrane proteins, stay pretty much entirely in the membrane.\nMany of the proteins, such as receptors and porins, move fairly freely; others, particularly the proteins that cause adherence between cells, are fixed in place.\nI guess the best answer is that the arrangement of the proteins in the cell membrane is complex, and for many proteins, ever changing, but for others, static.  It's not nearly as simple as it looks.  For instance, in modeling the large membrane proteins, the cell membrane is effectively a gas in two of three dimensions, and a solid in the third...  Go figure.
566418
they are a protein that speed up chemical reactions.
807463
Think of the cell as a factory.   The cell membrane the walls.   \n\nUnfortunaly proteins have many functions so there isn't just one analogy that you could correctly use.  \n\nMany proteins are proteins that do jobs or functional.  Those would be like the machines in the factory.  There are many different types of machines and while most of them do different jobs some do similar ones.\n\nOther proteins are more structural.  Think of large scafolds holding the factory up.  Some of them are even used for transporting things around the factory.\n\nHope that helps
266654
Picture a string of beads- the beads are different sizes and shapes. \n\nNow, "proteins" are basically like a string of beads that could be a very long string or a short string. AND instead of beads, there are amino acids- with different shapes and sizes. \n\nBut these strings don't lie flat. Depending upon the amino acids and other factors, the protein strings bend and fold in certain ways. So the string may become more like a ball or other strange shapes; this affects the way the protein works and interacts with other protein or chemicals. \n\nHope that mental picture helps answer your question...
745249
the molecules in the uppermost layer of a liquid,taken in cup/jar shares their bonds to make the surface hard to pierce with light forces.\neg: if you put a blade in a cup of water,it will float on its surface.It is due to the Surface tension.
145668
In biochemistry, denaturation is a structural change in biomolecules such as nucleic acids and proteins, such that they are no longer in their native state, and their shape which allows for optimal activity.\n\nThis change is usually caused by heat, acids, bases, detergents, alcohols, heavy metal salts, reducing agents or certain chemicals such as urea.\n\nContents [hide]\n1 Protein denaturation \n1.1 How denaturation occurs at levels of protein structure \n1.2 Loss of function \n1.3 Reversibility and irreversibility \n1.4 Some common examples \n2 Nucleic acid denaturation \n \n\n\n[edit]\nProtein denaturation\nProteins denature when they lose their three-dimensional structure - their chemical conformation and thus their characteristic folded structure. Proteins may be denatured at the secondary, tertiary and quaternary structural levels, but not at the primary structural level.\n\nProteins are long strands of amino acids linked together in specific sequences. A protein is created by ribosomes that "read" codons in the gene and assemble the requisite amino acid combination from the genetic instruction, in a process known as translation. The newly created protein strand then undergoes post-translational modification in which additional atoms or molecules are added, for example copper, zinc, iron. Once this post-translational modification process has been completed, the protein begins to fold (spontaneously, and sometimes with enzymatic assistance), curling up on itself so that hydrophobic elements of the protein are buried deep inside the structure and hydrophilic elements end up on the outside. The final shape of a protein determines how it interacts with its environment. If the shape of the protein is altered through some form of external stress (for example, by applying heat, acid or alkali) then it will no longer be able to carry out its cellular function. This is called denaturation of the protein.\n\nDenatured proteins can exhibit a wide range of characteristics, from loss of solubility to communal aggregation.\n\n[edit]\nHow denaturation occurs at levels of protein structure\nIn quaternary structure denaturation, protein sub-units are dissociated and/or the spatial arrangement of protein subunits is disrupted. \nTertiary structure denaturation involves the disruption of: \nCovalent interactions between amino acid side chains (such as disulfide bridges between cysteine groups) \nNoncovalent dipole-dipole interactions between polar amino acid side chains (and the surrounding solvent) \nVan der Waals (induced dipole) interactions between nonpolar amino acid side chains. \nIn secondary structure denaturation, proteins lose all regular repeating patterns such as alpha-helices and beta-pleated sheets, and adopt a random coil configuration. \nPrimary structure, such as the sequence of amino acids held together by covalent peptide bonds, is not disrupted by denaturation. \n[edit]\nLoss of function\nMost biological proteins lose their biological function when denatured, For example, enzymes lose their catalytic activity, because the substrates can no longer bind to the active site, and because amino acid residues involved in stabilizing substrates' transition states are no longer positioned to be able to do so.\n\n[edit]\nReversibility and irreversibility\nIn many proteins (unlike egg whites), denaturation is reversible (the proteins can regain their native state when the denaturing influence is removed). This was important historically, as it led to the notion that all the information needed for proteins to assume their native state was encoded in the primary structure of the protein, and hence in the DNA that codes for the protein.\n\n[edit]\nSome common examples\nWhen food is cooked, some of its proteins become denatured. This is why boiled eggs become hard and cooked meat becomes firm.\n\nA classic example of denaturing in proteins comes from egg whites, which are largely egg albumins in water. Fresh from the eg
40328
Proteins, including enzymes.
233031
One function of proteins is structural.  They are kind of like the framework of a cell, known as a cytoskeleton.  Proteins also make up structural features such as your hair.  The second function of proteins in the human body is a biochemical function.  Our enzymes are proteins.  Without them we would not be able to digest our food, use the energy we get from food, repair our cells, carry oxygen from the air we breathe around our body, fight off infection, and many, many other things.  Proteins are so important to the human body that the function of our DNA is to code for our proteins!  That's what DNA mostly does, it just tells our body what protiens to make and in what amounts.
99331
>>>>Does the heat of coffee break down whey protein?\n\nIt denatures the protein, which is not excatly the same thing. Think of a dentured protein as being like a crumpled pecie of paper. It's still in one piece but it can't be used for anything in that shape. I doubt if the heat of coffe would be enough to break down the protein, as in physcially break it to peices, at least not in the few minutes that it normally stays hot.\n\n>>>>Is the protein just as effective if mixed with hot coffee?\n\nIt's just as effective nutritionally, IOW it makes no difference if you just intend to eat it. It will be pretty useless chemically, ie if you want to use it for chemical reactions.
366004
All biological processes are catalyzed by enzymes (proteins). The tertiary structure of all proteins is affected by pH. Why? Because the hydrogen and ionic bonds that maintain the tertiary structure can be broken by extremes in Hydrogen and Hydroxyl ion concentration. pH measures this concentration.
857859
mostly phospholipids (the bulk of the membrane is the phospholipid bilayer, with hydrophobic tails pointed towards each other and hydrophilic heads pointing out), with a bunch of proteins stuck in it like little potatoes :) \n\nmixed in the sea of phospholipids are small amounts of cholesterol (roughly the same size) to help prevent weakening of the cell membrane at high temperatures.\n\nAs for proteins, there are many types with many functions!\n- transport proteins\n- identity markers\n- junctioning proteins (stick to other cells)\n- anchors for cytoskeleton\n- enzymes\n- hormone receivers
255214
Proteins are large molecules that are made from amino acids, which are small molecules.
728538
MILK / VEG / PROTEINS
938144
you're very correct in that you should mention those things. some other proteins you could mention is albumin and if you don't have enough, the pressure will be different in your Extracellular Fluid, also if you don't have the right amount of proteins your cells won't be able to do protein synthesis and divide....