Which protein bind heme non-covalently?
89988
- Methaemoglobin..?\n----------
863396
Each molecule of catalase is a tetramer of four polypeptide chains. Each chain is composed of more than 500 amino acids. Located within this tetramer are four porphyrin heme groups that are very much like the familiar hemoglobins, cytochromes, chlorophylls and nitrogen-fixing enzymes in legumes.  For the same reason hemoglobin (blood) is red, so is catalase.  The heme group has an iron (Fe) atom that is the source of the red color.  It's also the same reason rust (iron oxide) is reddish-orange.
434938
Bound and unbound. Bound with hemoglobin as a carrier (red blood cells) and simply dissolved in plasma (in the same way you can dissolve air in water by shaking a half full bottle up).
278992
label the known protein with a radioactive isotope, or better yet, maybe you could label the protein with a flourescent dye (dont know how, its beyond my expertise) and where ever the protein binds on the receptive cell may be what you're looking for.  but i dont know of any assays per se for it.
431813
Tag it with a poly ubiquitin chain.  You can make a chimera of the protein plus a couple of ubiquitins.  We did this for our protein (one ubiquitin tag at C terminus) and found it was degraded very efficiently.
478310
As far as using for detection, its very vulnerable to showing false positives from non-specific binding.  In addition, because of the relatively low level of mRNA, it can only be used for fairly abundant messages.  It is somewhat difficult to separate non-specific from specific binding, but of course it can be done.  In addition, it only shows the presence of message-it does not tell about the level of protein translation.
56795
"silent information regulator" proteins.
313675
do you mean interactions BETWEEN nucleic acids and proteins?  If so there's a lot of ways you can study that - you can do a footprint analysis - digest the nucleic acid in the presence of the protein and see what piece gets protected to see where the protein binds if you know the identity of the two interacting molecules.  If you don't know their identity you can try a gel-shift assay where DNA will move at different rates on a gel in the presence and absence of various proteins.  If you know the protein but not the DNA you can try an affinity column with the protein immobilized and then try to determine which DNA sequences bind.  You can also try to determine the crystal structure of a co-crystal if you have a lot of the two materials.  good luck!
392229
At the alveoli; the capillary bed is dense and near the surface there, so oxygen binds to hemoglobin there.
432294
Each hemoglobin molecule has 4 heme groups. Each heme group binds to one oxygen molecule. This happens in the lung. The hemoglobin is 98-100% saturated. In the tissues, in normal conditions, the saturation is reduced to 75%. So not all the oxgen molecules are given up. Only 25%.
197308
C.  hemoglobin will bind more O2 when pH is increased - meaning less acidic.  This is because, in the lungs, where O2 needs to be bound in order for it to be transported to the tissues, the pH is higher that in the tissues due to a decreased CO2 content. (CO2 acts like an acid in the body).  In the tissues, CO2 content is higher, and O2 is released.
930454
I can definitely tell you the enzyme is not an initiator. The DNA polymerase has a sequence that initiates replication. \n\nThe protein you are talking about is called SSB (Single Starnd Binding) protein. I am very amazed where you got this question from. I have never before heard such a function related name for SSB protein. But if it is a must, I would go for straightener since SSB unbound single starnded DNA forms folds (loops) as in RNA. But it definitely is not initiator.
787248
If they're embedded in the membrane, they are called integral membrane proteins.  If they are covalently associated with the membrane, but don't go through the membrane (ie GPI linked proteins), then it is called a peripheral membrane protein.
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.
282016
Examples of proteins include keratin, stuff that makes hair and nails, or haemoglobin that transports oxygen in the blood. Examples of proteins that are enzymes are kinases which cause an energy increase due to the addition of a phosphate. Proteins function as enzymes due to the manner they fold causes then to form a site which will be attractive as a binding site for the substrates allowing 2 molecules which may meet at random to meet more often and bond increasing the speed of a reaction.
1037043
The D1 protein, also known as the 32-kDa thylakoid membrane protein, is a key component of the photosynthetic electron transport chain acting at the reducing side of photosystem II.\n\nSee the links below for more information. \n\nHope this helps!
465870
Iron from the hemoglobin