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Mateyman Mateyman
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3 years ago Edited: 3 years ago, Mateyman
So we did a lab that went over hydrophobicity plotting and we did that by plugging a protein sequence into Protscale (not sure if you have used this website before) and then it would give us a hydrophobicity plot and I just wanted to double check some of my answers. Also we did a Chou-Fasman plot of a different protein sequence (basically the Chou-Fasman algorithm predicts protein secondary structure based on primary sequence). Anyways I only have 3 questions just wanted to double check, they don't necessarily have much to do with understanding these different scales but more about reading different plots because I am not so good at reading plots to be honest.

1) Here is a plot using Kyte-Doolittle and Eisenberg hydrophobicity scale of the same protein sequence. How do they compare in terms of transmembrane predictions?

Here is Kyte-Doolitte scale: https://imgur.com/yqGCEqO

Here is Eisenberg scale: https://imgur.com/QowwqJ1

The obvious thing is that the plots look fairly similar its just that the scaling in Eisenberg is different however you can still tell which regions are hydrophobic and which ones are hydrophilic, thoughts on my answer?

2) We also used the same sequence and inserted it into TMHMM. How does the TMHMM plot compare to the Kyte-Doolitte scale and Eisenberg scale above?

Here is the TMHMM plot by the way: https://imgur.com/vcGrf48

The obvious one is that the TMHMM plot uses probability of trans-membrane helices in proteins instead of free energy y axis in the other graphs. Also  it kind of looks at a protein in terms of a cell that include intra and extracellular instead of just peaks. It shows what parts are inside the cell and are hydrophobic and which parts are outside the cell and are hydrophilic, what you think about this answer?

3) For final question I am being asked to use a protein sequence and use the Chou-Fasman alpha-helical predictions. ANYWAYS I am being asked to to analyze the plot of the Chou-Fasman and the question is how many regions exceed a threshold of 1.1?

Here is the Chou-Fasman plot: https://imgur.com/qoIpwdz

My answer is that the only region that exceeds 1.1 is only 1 region and its between positions 120 ish to 145 ish, thoughts?

Thanks guys! Again you don't need to know the stuff I am talking about but mainly just comparing the plots if you are not familiar with this then no problem!
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bio_manbio_man
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3 years ago
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Mateyman Author
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3 years ago
Well from what I understand so far, is that trans-membrane proteins are highly hydrophobic, especially the ones inside the membrane. Now the regions of the proteins that are intra or extra celluar are hydrophilic. The issue is that I am not sure how to relate this to the Kyte-Doolitte scale and the Eisenberg scale. I know the Kyte-Doolittle scale detects for hydrophobic regions that have positive value along the y-axis.

But actually looking at it again now, it looks like the Eisenberg scal shows less hydrophilic regions compared to the Kyte-Doolittle which exposes more hydrophobic regions and therefore shows more clearly the transmembrane domains compared to the Eisenberg which uses a fairly close y-axis of -1 to 1. I don't know maybe I'm stupid lol....
wrote...
Educator
3 years ago
Honestly, I just can't get past the name, Kyte-Doolittle, it reminds me of that movie Dr. Dolittle. In all seriousness, however, I'm not sure how to interpret these graphs, but given what you wrote in that first paragraph in your reply, I'd tie that into your response given originally. That's all I can add to this...
Mateyman Author
wrote...
3 years ago
LOL same thoughts as me :DDD

Do you know of any bioinformatics focused forums that has people that can help out college students?
wrote...
Educator
3 years ago
Not sure of another community, it's so specific.

Here's something that might open you eyes on the subject. It's the answer-key to a Kyte-Doolittle worksheet. Maybe you can extract some ideas from the solutions given, let me know

Also, I can get you more
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