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6

These are are completely different concepts, which sometimes may be connected. A motif in biology is a mathematical model, typically of a sequence, which is predictive of which sequences to some defined group. For example, a DNA sequence motif can characterize the binding site of a transcription factor, i.e. which sequences tend to be bound by this factor. ...


5

Hsp70 and Hsp90 are not single proteins, but entire protein families. And those two protein families are not the only ones of their kind. There are different groups of heat shock proteins, Hsp70 and Hsp90 are molecular chaperones that assist in protein folding. There are five major families of molecular chaperones: Hsp100, Hsp90, Hsp70, Hsp60 and Hsps. ...


4

Often cells have multiple types of the same protein — this redundancy can have different effects for different requirements such as having proteins function under different physiological conditions, or providing specificity to a certain class of ligand proteins or so on. But here, it seems like the two have some synergistic interaction, a tag team if you ...


4

If the process of evolution is driven by completely random process... It's not. The evolution of "better" protein (and other) molecules happens because of selection, a very non-random process. The repeated selection of better molecules, and then of the variants of the better molecules, repeated many times, will lead to "good" molecules (in the sense ...


4

The main problem is that Mad Cow disease is not caused by a "normal" pathogen but by a prion, a protein. Traditionally, disease causing agents can be classified into viruses, bacteria, fungi, and parasites. Bacteria, fungi and parasites are all living organisms, alive in the traditional sense. It is, therefore, possible to design drugs that kill them. ...


3

I think you've got the list of good predictions from the Bragg, Perutz, and Kendrick paper. And the 310 helix was not really right either - it did turn out to show up occasionally in protein structures though. At the time all of these secondary structure elements were well evidenced from noncrystalline diffraction data and small molecule crystal ...


3

I am also about to undertake some FRET studies (this week in fact). FRET linkers are a thing of tinkering, unfortunately. Förster resonance energy transfer, or FRET, is a phenomena that decays with $ 1/{r^6} $, the radius between the donor and acceptor. When constructing FRET reporters, there are a few things to keep in mind: Length of linker. The length ...


3

One of the quickest ways to get oriented on what is going in the world of protein folding and modeling is to look at the proceedings of the Critical Assessment of Structure Prediction (CASP). CASP is basically a contest, held every 2 years where anyone can use their algorithm to predict the 3D structure of a protein whose structure is known, but not ...


2

Since we only have one planet that we know of with life, it's a bit difficult to make good estimates on the probability of various events in the history of life. To make a good estimate, you'd want to have thousands of planets very similar to earth to compare. Since we don't have access to that kind of data, one proxy which you can look at is how long did ...


2

Exactly how genetic material changes from one generation to the next is a very complex subject. But essentially you are right. The change in genes from one generation to the next is not only mutations though. It is also mixing of the genes carried by the male and the genes carried by the female. The selection process is also very complex, and sexual ...


2

The principal difference is that domains are independently stable, while motifs are not. Here is a bit on motifs: http://www.sinauer.com/pdf/nsp-protein-1-16.pdf A motif can be part of a domain. From there: The second, equally common, use of the term motif refers to a set of contiguous secondary structure elements that either have a particular ...


1

Do you have a textbook? That will definitely have the answer early on in the chapter. Also, have you tried reading the protein Wikipedia article, in particular the structure subsection. You will find the information you want there.


1

Membrane proteins have to go to the ER from where they are transported to the Golgi apparatus. Usually these proteins are translocated into the ER while translation is still going on. There are chaperones (such as calbindin) in ER which help in translocation and also catalyze initial steps of folding. ER is also involved in unfolded protein response. Unless ...


1

The answer is more like "It depends on the protein, and the renaturation (or refolding) process." There are a lot of factors that contribute to an individual protein's ability to refold, including size, sequence, secondary structure, amount and type of inter-amino acid links like disulfide bonds, number of subunits, the presence of chaperones/heat shock ...



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