what would be an expected consequence of changing one amino acid in a particular protein?
81856
All answers are correct. The primary aminoacid sequence is changed which may have implications for the structure and funtion of the protein
282912
By serum protein electrophoresis, or by subtracting Serum albumin value from serum total protein value
47679
You will still have to read the info at the links below as it is "assumed that you have a rudimentary understanding of basic concepts of protein and nucleic acid structure, as well as enzyme kinetics and mechanisms."\n\nI digress to say that "amino acids are the principal building blocks of proteins and enzymes. They are incorporated into proteins by transfer RNA according to the genetic code while messenger RNA is being decoded by ribosomes. During and after the final assembly of a protein, the amino acid content dictates the spatial and biochemical properties of the protein or enzyme."\n\n"The amino acid backbone determines the primary sequence of a protein, but the nature of the side chains determines the protein's properties. Amino acid side chains can be polar, non-polar, or practically neutral. Polar side chains tend to be present on the surface of a protein where they can interact with the aqueous environment found in cells. On the other hand, non-polar amino acids tend to reside within the center of the protein where they can interact with similar non-polar neighbors. This can create a hydrophobic region within an enzyme where chemical reactions can be conducted in a non-polar atmosphere. Likewise, enzymes can also have polar amino acid substituents within the active site that provide a polar region in which to conduct biochemical synthesis."\n\n\n1. Structure of Amino Acids\n2. Review: Basic Concepts of Protein Structure\n3. The Basics & Definitions
1019559
Amino acids are the basic structural building units of proteins. They form short polymer chains called peptides or polypeptides which in turn form structures called proteins. The process of such formation from an mRNA template is known as translation, which is part of protein synthesis.\nPhenylalanine is one of the standard amino acids.\nEnlarge\nPhenylalanine is one of the standard amino acids.\n\nTwenty amino acids are encoded by the standard genetic code and are called proteinogenic or standard amino acids. Combinations of these amino acids produce every single essential protein for the homeostasis of the human body. At least two others are also coded by DNA in a non-standard manner as follows:\n\n    * Selenocysteine is incorporated into some proteins at a UGA codon, which is normally a stop codon.\n    * Pyrrolysine is used by some methanogens in enzymes that they use to produce methane. It is coded for similarly to selenocysteine but with the codon UAG instead.\n\nOther amino acids contained in proteins are usually formed by post-translational modification, which is modification after translation in protein synthesis. These modifications are often essential for the function of the protein.\n\nProline is the only proteinogenic amino acid whose side group cyclizes onto the backbone: it links to the α-amino group, and thus is also the only proteinogenic amino acid containing a secondary amine at this position. Proline has sometimes been termed an imino acid, but this is not correct by current nomenclature rules.\n\nOver one hundred amino acids have been found in nature. Some of these have been detected in meteorites, especially in a type known as carbonaceous chondrites. Microorganisms and plants can produce uncommon amino acids, which can be found in peptidic antibiotics (e.g., nisin or alamethicin). Lanthionine is a sulfide-bridged alanine dimer which is found together with unsaturated amino acids in lantibiotics (antibiotic peptides of microbial origin). 1-Aminocyclopropane-1-carboxylic acid (ACC) is a small disubstituted cyclic amino acid and a key intermediate in the production of the plant hormone ethylene.\n\nIn addition to protein synthesis, amino acids have other biologically-important roles. Glycine and glutamate are neurotransmitters as well as standard amino acids in proteins. Many amino acids are used to synthesize other molecules, for example:\n\n    * tryptophan is a precursor of the neurotransmitter serotonin\n    * glycine is one of the reactants in the synthesis of porphyrins such as heme.\n\nNumerous non-standard amino acids are also biologically-important: Gamma-aminobutyric acid is another neurotransmitter, carnitine is used in lipid transport within a cell, ornithine, citrulline, homocysteine, hydroxyproline, hydroxylysine, and sarcosine.\n\nSome of the 20 standard amino acids are called essential amino acids because they cannot be synthesized by the body from other compounds through chemical reactions, but instead must be taken in with food. In humans, the essential amino acids are lysine, leucine, isoleucine, methionine, phenylalanine, threonine, tryptophan, valine. Histidine and arginine are generally considered essential only in children, because of their inability to synthesise them given their undeveloped metabolisms.\n\nThe phrase "branched-chain amino acids" is sometimes used to refer to the aliphatic amino acids: leucine, isoleucine and valine.
305209
All proteins are made of amino acids, so "amino acid protein" is redundant. And it's 4 kcals/g.
209909
try\nhttp://web.indstate.edu/thcme/mwking/amino-acids.html
473805
take a carboxylic acid and couple under normal conditions with an O-alkylated/acylated hydroxylamine.\n\nBy normal conditions, I mean normal peptide coupling conditions usined EDC, DIC/HOBt, CDI, PyBOP, PyBrOP, TBTU etc etc etc
600557
Ultimately all changes in DNA sequence across all living organisms are the result of mutations.  Essentially, the copying process went wrong somewhere along the line and generated a change.  These may occur as a result of many factors.\n\n1.) Substitutions are changes in single bases.  A becomes T for example.  In a large fraction of cases, this will lead to  a change in the amino acid, which in turn changes the protein.\n\n2.) Indels (insertion/deletion events) will add or subtract DNA.  During replication, a segment of DNA may be added or removed leading to a change.  It is also possible that DNA becomes damaged or lost and that change is passed on to future generations.\n\n3.) Recombination can lead to novel arrangements of existing strands of DNA.  It can also occur improperly and generate change (often through indels).\n\n4.) Chromosomal rearrangement.  If chromosomes break they may reattach elsewhere, become a whole new chromosome, or lose parts entirely.  This can lead to moving an allele into a completely new gene environment.  The protein itself may not change, but the expression of the protein might.\n\nFinally, natural selection and random effects (such as bottlenecks) will affect the gene frequencies.  Sometimes these will allow for new interactions of genes.
290735
a mutation which changes the 6 th amino acid in the the protein made up of 146 amino acid found in haemoglobinn
947017
Mutagenesis is basically where one can change the molecular structure ( ultimately function) of a protein/molecule. This can be achieved via the use of chemicals and specific ligands which knowck out nucleotides froma DNA sequence. Thus allowing scientists to see the effects on a particular organism/molecule. One nucleotide difference can be suffiicent to change the whole organism. Site directed mutageneis as the name suggests is where a known area of a sequence be it bacteria/virus or another species is though to possess elements which may be resposbile for say cancer. Hence knoecking these "bits" out specifically means  one can see its direct effects.
905993
In that situation, an A was inserted into the middle codon of the first sequence, between the C's in CCG\nso gca cAcg gag\nthis caused all following nucleotides to be one out of place, and thus all following codons will be different.\nThis is called a frameshift mutation.
347349
None!\n\nSo make it an ice cream float - instant protein increase!\n\nYum.
891448
This would be (d).\n\nThe presence of an amide bond (R-NH-CO-R) is the main part of a peptide bond.\n\nB may look like this too, however in a peptide bond, but the amino group should be on the alpha-carbon of an amino acid.
697365
click on this link http://www.tiem.utk.edu/~gross/bioed/webmodules/aminoacid.htm and look through the table. the answer should be there.
883039
No, I don't really think so. Everything you said is basically true, but digestion occurs and in digestion your body will only take in which specific amino acids it needs at that point in time (we have no real way to store amino acids) and excete everything else.  So if you eat a lot of tryptophan your body will just stop taking it in when it doesn't need any more. \nAlso, your body can switch a lot of amino acids into a different amino acid. So if you have a lot of one and need more of another, your body can just make that one.\nNote that there are some "essential" amino acids, meaning that your body cannot make them and they must be ingested!\nAlso, maybe there's a bit of confusion on the codon thing. A codon is a specific sequence in the mRNA of 3 nucleotides that codes for an amino acid. A tRNA with the complementary anticodon will bring this amino acid to the growing chain. Only the tRNA that matches the codon will come in. This cannot be influenced by what you eat.
722594
I think most theoretical chemists would agree that the holy grail in the field would be accurate prediction of folded protein structure using only the primary amino acid sequence. \n\nWhat makes this difficult is the enormous size of proteins, the numerous non-bonded interactions, and the necessity to model solvent interactions with chemical accuracy. Even with accurate methods to do a single point energy calculation, you still have to find methods to effectively serach the conformational space to locate the global energy minimum. It's a big problem, and would definitely be worth a Nobel prize.
839902
Just reconstituted/altered to another chemical.....