why replacing lycine with arginine not effect protein conformation and structure?
608961
wat in da hek r u talk in abawt!
800173
carboxly and amine groups.\n\nCheck out, http://en.wikipedia.org/wiki/Amino_acid for more info about amino acids and what the structure looks like.
457527
Amino acids are organic molecules with amino groups (-NH2) and acidic groups (-COOH).  When the amino group (-NH2) of one amino acid reacts with the acidic group (-COOH) of another, the bond is called a "peptide" bond (IIRC.)\n\nIf you link a small number of amino acids in this way, the product is often just called a "peptide".  The better term is "oligopeptide", as "oligo" comes from Greek, meaning "few".\n\nReally long peptides are called polypeptides or proteins.  ("poly" comes from Greek, too, meaning "many")\n\nSome proteins have different polypeptides that stick together, held by weaker forces such as electrostatic attraction.\n\nDoes that help?
350998
It's the least reactive. It's non-polar. It's pKa is simply the average of the N and C terminus. It's also Ambivalent, meaning it can be inside and outside a protein. Because of these properties, if it was replaced with a polar AA, it would change the protein property, and in 99% of time, change in AA is deleterious.
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.
290735
a mutation which changes the 6 th amino acid in the the protein made up of 146 amino acid found in haemoglobinn
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.
908056
Alanine (Ala) also 2-aminopropanoic acid is a non-essential α-amino acid. It exists as two distinct enantiomers - L-alanine and D-alanine. L-alanine is one of the 20 amino acids most widely used in protein synthesis, second to leucine, accounting for 7.8% of the primary structure in a sample of 1,150 proteins [1]. D-alanine occurs in bacterial cell walls and in some peptide antibiotics.\n\nStructure\nThe α-carbon atom of alanine is bound with a methyl group (-CH3), making it one of the simplest α-amino acids with respect to molecular structure and also resulting in alanine being classified as an aliphatic amino acid.\n\n\nSynthesis\nAlanine is most commonly made by transfer of an amine group to pyruvate. Because transamination reactions are readily reversible, alanine can be easily formed from pyruvate and thus has close links to metabolic pathways such as glycolysis, gluconeogenesis, and the citric acid cycle.\n\n\nFunction\nThe methyl group of alanine is very non-reactive, and is thus rarely directly involved in protein function. However, alanine can play a role in substrate recognition or specificity, particularly in interactions with other non-reactive atoms such as carbon.\n\nIt goes through alanine cycle to generate glucose from protein.\n\n\nSources\nAny protein containing food such as meat, poultry, fish, eggs, and dairy products are rich in alanine.
1176807
Sounds like somebody is working on a biochem lab. :) \n\nDenaturation lowers enzyme activity because it changes the shape of the protein. Heat disrupts the tertiary structure by breaking covalent, non-covalent and van der waals interations between side chains of the protein. Proteins must be in the right conformation in order to perform their functions correctly. When they are denatured substrates can no longer bind to the active site, key amino acids are no longer in the correct position. \n\npH affects enzyme activity in the following ways: 1-enzyme binding to the active site 2-catalytic activity 3-ionization of the substrate 4-variation of protein structure. This is because pH will change the ionization state of certain side chains. (H+ ions will interact with \n\nOptimum conditions for alpha amylase (ptyalin) from wikipedia.com:\n Optimum pH-5.6 - 6.9\n Room temperatue- 37 degrees Celsius
230567
If the two processes don't copy the templates exactly everytime, that leads to mutations in the following strand.  If there are mutations, that leads to different properties of the proteins made in translation.  Depending on the mutation, this can have either a beneficial or very adverse effect, or even none at all, depending on where the mutation is, and if different amino acids are used.\n\nFor example, sickle cell anemia is caused by a single mutation.  Genotypically, one nucleotide is substituted for another, leading to a different amino acid.  Phenotypically, this different amino acid causes different bonding patterns in the hemoglobin protein, causing red blood cells to sickle.
1075604
High temperatures often denature the tertiary structures of a protein (break the 3D structure down caused by H-bonding between adjacent polypeptide bonds).  The breakdown of the tertiary structure exposes the entire peptide chain and makes the entire protein sequence easier to break down into amino acids using a weak base or water (hydrolysis).  Thus, high temperature increases rate of protein hydrolysis.
514398
tryptophan a kind of amino acid
94258
The alpha-amino acid Phenylalanine exists in two forms, the D- and L- forms, which are enantiomers (mirror-image molecules) of each other. It has a benzyl side chain. Its name comes from its chemical structure's consisting of a phenyl group substituted for one of the hydrogens in the side chain of alanine. Because of its phenyl group, phenylalanine is an aromatic compound. At room temperature, it is a white, powdery solid.\nL-Phenylalanine (LPA) is an electrically-neutral amino acid, one of the twenty common amino acids used to biochemically form proteins, coded for by DNA. Its enantiomer, D-phenylalanine (DPA), can be synthesized artificially.\n\nL-phenylalanine is used in living organisms, including the human body, where it is an essential amino acid. L-phenylalanine can also be converted into L-tyrosine, another one of the twenty protein-forming amino acids. L-tyrosine is converted into L-DOPA, which is further converted into dopamine, norepinephrine, and epinephrine (latter three are known as the catecholamines). D-phenylalanine can be converted only into phenylethylamine.\n\nThe genetic disorder phenylketonuria is an inability to metabolize phenylalanine. Individuals with this disorder are known as "phenylketonurics", and must abstain from consumption of phenylalanine. It is present in many sugarless gums and other food products, which are labeled: "Phenylketonurics: Contains phenylalanine."\n\nThe synthesized mix DL-Phenylalanine (DLPA), which is a combination of the D- and L- forms, is used as a nutritional supplement.\n\nThe genetic codon for phenylalanine was the first to be discovered. Marshall W. Nirenberg discovered that, when he inserted m-RNA made up of multiple uracil repeats into E. coli, the bacterium produced a new protein, made up solely of repeated phenylalanine amino acids.\n\nPhenylalanine uses the same active transport channel as tryptophan to cross the blood-brain barrier, and, in large quantities, interferes with the production of serotonin.
50031
There r 20 amino acid,by combination of these amino acids diffirent proteins r formed.simple structure of a amino acidis like a central carbon atom(known as alpha carbon)to which a carboxilic group(-COOH) and a amine group(-NH2) and a side chain(-R group) attached,all amino acid have same structure but they differ to each other by side chain(-R group).
215352
There are four structures; primary, secondary and Tertiary structures. \n\nThe primary structure is the sequence of amino acids in a polypeptide chain, held together by peptide bonds (which occur between the amine group of one amino acid and the carboxyl group of another). \n\nThe secondary structure is the folding of the polypeptide chain into alpha helices and Beta pleated sheets, these are held together due to hydrogen bonding within the polypeptide itself. \n\nTeritary structure is the further folding of a polypeptide chain into a complex globular molecule (also held together by hydrogen bonds).\n\nFinally, Qauternary structure is the folding of two polypeptide chains together, the two chains are held together not only by hydrogen bonds but also by ionic bonds and disulphide bridges(these bonds form between the suplhur atoms on the R groups of the amino acids).
200416
Aren't you confusing glycine with glutamate?\n\nAnyhow, here is a place that sells glycine.
1007534
Denaturation of proteins involves the disruption and possible destruction of both the secondary and tertiary structures. Since denaturation reactions are not strong enough to break the peptide bonds, the primary structure (sequence of amino acids) remains the same after a denaturation process. Denaturation disrupts the normal alpha-helix and beta sheets in a protein and uncoils it into a random shape.\n\nDenaturation occurs because the bonding interactions responsible for the secondary structure (hydrogen bonds to amides) and tertiary structure are disrupted. In tertiary structure there are four types of bonding interactions between "side chains" including: hydrogen bonding, salt bridges, disulfide bonds, and non-polar hydrophobic interactions. which may be disrupted. Therefore, a variety of reagents and conditions can cause denaturation. The most common observation in the denaturation process is the precipitation or coagulation of the protein.\n\nHeat:\n\nHeat can be used to disrupt hydrogen bonds and non-polar hydrophobic interactions. This occurs because heat increases the kinetic energy and causes the molecules to vibrate so rapidly and violently that the bonds are disrupted. The proteins in eggs denature and coagulate during cooking. Other foods are cooked to denature the proteins to make it easier for enzymes to digest them. Medical supplies and instruments are sterilized by heating to denature proteins in bacteria and thus destroy the bacteria.