What macromolecule is affected by high temperatures?
489365
Protiens are denatured when body temperatures are raised. Protien shape is what gives them their function. The shape of protiens are changed, because the heat breaks the bonds which unravels the polypeptide chains, and ultimately their shape. When shape changes, they lose their function.
285837
High temperatures, limit or exclude oxygen.
236096
1) Covalent modification, e.g. phosphorylation\n2) Induction or depression of gene expression (affecting\n   enzyme synthesis\n3) Allosteric inhibition or activation, e.g. feedback \n   inhibition\n4) Competitive inhibition\n5) Noncompetitive inhibition\n\nNow do your homework to figure out which ones affect B-galactosidase activity.
1047081
DNA\nRNA\ncarbohydrate (eg glycogen)\npolypeptides (proteins)\nmucopolysaccharides (proteins joined to carbohydrates)\nlipopolysaccharides (proteins joined to lipids)\nother lipids eg in membranes, and storage fat\n\nThere may be others.
1107805
study on intermolecular particals and there behavior
196147
At higher temperatures, reactions proceed faster, so metablic activity increases.  Also, pressure and/or volume may increase.  At high enough temperatures, proteins will start to denature, but this usually doesn't happen with a fever.
1031172
The effects of temperature may be explained on the basis of kinetic theory - increased temperature increases the speed of molecular movement and thus the chances of molecular collisions, so within a narrow range (often 0-45 °C), the rate of reaction is proportional to the temperature. It is often said that an enzyme's rate of reaction doubles for every10° C rise in temperature. In this respect, the biochemistry of enzymes is similar to chemistry as studied elsewhere, However, the interaction between this positive effect of increased temperature and the negative effect described below results in a different situation, so that enzymes may be said to have an optimum temperature for their action. \n 4 Above normal temperatures (say 60 °C), heat alters irreversibly the enzyme molecule. This denaturation is due to molecular vibrations (caused by heat) which change the shape of the protein, altering the folding and internal cross-linkages in its polypeptide chains. These changes - especially in the region of the active site - mean that the enzyme is inactivated, even when returned to normal temperature. \nIt would be wrong to say that an enzyme is KILLED by heat, since it is only a molecule, not an organism. \nHowever, misconceptions of this sort are easily spread (see the BASC enzymes booklet!) \n\n\n\nThe higher the temperature to which the enzyme is subjected and the longer the heating is continued, the greater the proportion of damaged enzyme molecules and the result is that the conversion process becomes less and less efficient.\n\n\n\n\n\nBelow normal temperatures, enzymes become less and less active, due to reductions in speed of molecular movement, but this is reversible, so enzymes work effectively when returned to normal temperature.
941659
Denaturation usually occurs with boiling or mild reaction conditions; a, c, and d will alll occur. These are all relatively weak bonds. However amino acid sequence will remain, you need harsh conditions to break these strong peptide bonds.\nb) is answer
694888
yes of course ..\n\nMany of the enzymes in our bodies work best at body temperature. At significantly lower temperatures the substrate molecules do not have enough kinetic energy for the reaction to take place even in the presence of the enzyme. At body temperatures significantly higher than normal, the enzyme will not work well because the kinetic energy from the molecules in the solution containing the enzyme is so high, that the enzyme's shape is pulled apart to he point that the enzyme is not able to properly function. \n\nIndeed the enzyme's structure may be so disrupted or denatured hat the enzyme molecule cannot return to its original shape. Indeed the danger of high fevers stems in large part from the potential damage to enzymes and other proteins from the high temperature
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
1027970
Simply that during the induction period, the actual concentrations may not be 100% homogeneous and the rates will increase of decrease from theoretical.  This is much more important with macromolecules, but can be seen in other cases.  See\n\nwww.uem.mz/faculdade/ciencias/ ciencias_revista/textos/elalves.pdf\n\ndx.doi.org/10.1063/1.1954769\n\nwww.platinummetalsreview.com/ dynamic/article/view/50-2-54-63\n\nwww.citadel.edu/chemistry/scas2005.pdf
1128649
Has to do with the kenetics of the enzyme.  \n\nI need you to be a bit more specific on the origin of the enzyme.  For example, Taq polymerase is from Thermus aquaticus, a thermophyle bacterium that lives in extremely high temperatures.  This is the organism's normal habitat.  \n\nIf the enzyme is of human origin, this makes a difference.  Some enzymes operate optimally during a fever or heatstroke to keep the major organs alive.  Your immune cells typically function better at higher temperatures because of their specilized enzymes. \n\nSo it all depends.  If you're looking for speculation on why this enzyme's kenetics work this way, just think a little bit.  Is it a regulatory function?  What would happen if this enzyme was "on" all the time?  Could something bad come of it?  What is the organism of origin?  Does it typically function at that temperature?  What do the stability data show when overlayed over the kinetics data?  Is it less stable at lower temperatures even though the function is enhanced at higher temperatures?  What is the cost to the cell for making this enzyme?  Is it energetically efficient to produce?  What about degredation?  What else would be going on in that cell at that temperature?  Does the kinetics data show any relation between binding and pH?  How does this relate when looking at temperature?\n\nHope this helps!
672714
See if these help\n\nhttp://www.pslc.ws/macrog.htm\n\nhttp://www-classes.usc.edu/engr/ms/125/MDA125/polymers_files/frame.htm
860270
Hi - here are some ideas without seeing your actual data.  First - the system was too hot during transfer to  the membrane - be sure you aren't running it at too high  a voltage.   Second, not an issue with the  blot,  but with  the gel  - was it expired?  not fully polymerized? were the  wells free of debris when loading  samples?   sometimes with highly concentrated samples, especially cell lysates,  this  can  happen  because  of  viscosity  in t he  sample  (from  DNA for example). good  luck.
785808
usually protein with some metallic ions
558318
Answer is B.\n\nPart A is half true, half false.  The shape *and* function are affected by the sequence.\nParts B and D go together.  The HYDROPHILIC molecules -- usually translated as "water-loving" -- will remain outside while the HYDROPHOBIC molecules (these fats/lipids are "water-fearing") will remain inside.  The shape of the protein is formed in part by this association and disassociation with water.\nPart C is incorrect.  The linking of amino acids is part of the same amine-alkyl-carboxylic acid backbone.  There is no molecule separating each amino acid.\n\nHope this helps!
723838
ATP maybe.\nGlucose if not.