• metabolism
  • Correlated changes in energy and protein metabolism were investigated by determining the rates of oxygen consumption at various levels of P CO 2 , of intra- and extracellular pH, and after inhibition of protein synthesis by cycloheximide. (biologists.org)
  • Arginine Histidine Lysine Negatively charged side chains Aspartic acid Glutamic acid Polar uncharged side chains Serine Threonine Asparagine Glutamine Special cases Cysteine Selenocysteine Glycine Proline Hydrophobic side chains Alanine Valine Isoleucine Leucine Methionine Phenylalanine Tyrosine Tryptophan Mehta, S. Digestion of Dietary Proteins Mehta, S. Metabolism of amino acids- bimolecular ping pong mechanism of transamination. (wikipedia.org)
  • inhibit
  • Isoniazid (isonicotinic acid hydrazide), ethionamide, triclosan [5-chloro-2-(2,4-dichlorophenoxy)-phenol] and TLM are known to specifically inhibit mycolic acid biosynthesis. (wikipedia.org)
  • translation
  • Cycloheximide-mediated blockade of protein translation reveals that C75- or FASN siRNA-induced shutdown of FASN accelerates decomposition of signaling proteins. (aacrjournals.org)
  • Two examples of this type of reaction occur during the formation of nucleic acids and the charging of tRNA prior to translation. (wikipedia.org)
  • microorganisms
  • Growing microorganisms incorporate isotopically labeled amino acids, increasing protein masses and thereby leading to mass shifts of their corresponding peaks in the profile spectra. (asm.org)
  • naturally
  • The exchange of naturally occurring amino acids with their nonradioactive isotopically labeled versions in a growth medium leads to the incorporation of these "heavy" amino acids into the newly synthesized proteins. (asm.org)
  • residues
  • O-acylation (esters), N-acylation (amides), S-acylation (thioesters) acetylation, the addition of an acetyl group, either at the N-terminus of the protein or at lysine residues. (wikipedia.org)
  • amide bond formation amino acid addition arginylation, a tRNA-mediation addition polyglutamylation, covalent linkage of glutamic acid residues to the N-terminus of tubulin and some other proteins. (wikipedia.org)
  • found
  • C-reactive proteins are found in the blood and are present in large numbers during a period of inflammation. (brighthub.com)
  • FNR is a soluble protein that is found both free in the chloroplast stroma and bound to the thylakoid membrane. (wikipedia.org)
  • By 1999, they produced recombinant Dox A, a Cytochrome P450 oxidase, and found that it catalyzes multiple steps in DXR biosynthesis, including steps leading to daunorubicin. (wikipedia.org)
  • Tryptophan is among the less common amino acids found in proteins, but it plays important structural or functional roles whenever it occurs. (wikipedia.org)
  • typically
  • biotinylation: covalent attachment of a biotin moiety using a biotinylation reagent, typically for the purpose of labeling a protein. (wikipedia.org)
  • known
  • However, little is known about the expression characteristics of miRNAs and how they regulate protein accumulation in wheat caryopsis under drought stress. (frontiersin.org)
  • This break-down of amino acids to α-keto acids occurs in the liver by a process known as transamination, which follows a bimolecular ping pong mechanism. (wikipedia.org)
  • humans
  • As an essential amino acid, tryptophan is not synthesized from simpler substances in humans and other animals, so it needs to be present in the diet in the form of tryptophan-containing proteins. (wikipedia.org)
  • Humans and other animals must ingest histidine or histidine-containing proteins. (wikipedia.org)
  • level
  • Over the past decade, technological innovations have made it possible to overview the changes that occur at the transcriptomic level under environmental stress conditions. (biomedcentral.com)