So... mRNA = planner "Architect" who makes the blueprint. tRNA = supplier "Home Depot" who gets the material and brings it to the job site. rRNA = builder "Carpenter" who assembles the material (proteins) brought in by tRNA and puts them together according to the instructions given by mRNA. I know that's overly-simplified, but is it pretty much on track Andrey?
The Thymine structure looks a little different in my textbook which shows that Thymine has two double O bonds instead of one double O bond and an NH2 group.
I just don't know how to appreciate your good work towards me, you are such an amazing tutor , you will live long to enjoy the goodness of the Lord in the land of the living,💖 once again, thank you so much.
The Thymine molecule have a carbonyl group between the nitrogen atoms. it is identical to the uracil, but in addition it has a methyl group left to the first carbonyl group.
7.08 Is a mistake. My comment: In Eucariotic cells single gene is used to make many different proteins due to alternative splicing of introns, and procariotic gene usually code for single protein, cause procariotic genes mostly do not have introns.
well explained and in a very effective style of speaking. i look forward to watching more of your lectures to help myself better understand these processes. thank you.
Thank you so much! Your lectures are really helpful and easy to understand. Cleared up many important concepts for me, especially for biochemistry and biology.
I find all these lectures fascinating as I'm just starting out in this field. I have a three questions which I simply can't find answers to, but perhaps nobody knows yet!! If you're able to point me to a source I'd be very appreciative... 1) How do molecular machines know what to do? What signal / code / instruction / information do they receive, and from where? For example, there are many tRNA molecules carrying their amino acids in the cytoplasm - how do they know its their ‘turn’ to descend to the ribosome and release their amino acid on the correct codon? I could think of dozens more……! 2) Regarding the 23 pairs of chromosomes, how does the RNA polymerase know which gene to transcribe, and how is the tightly-knit DNA unwound from the chromosome? What coils it back again? 3) How does the barrel receiving the recently folded protein know what shape to fold it? If the cell is producing a protein, its because the body needs it. So, did the barrel receive this information? Does it recognise the protein and understand what it needs to become? Does it have a ‘memory bank’ of all the types of proteins the body produces? Thanks in advance....
Drumming Spain I think its much more productive to you if you discover these answers on your own. Its natural to have these questions at the beginning and you will appreciate it much more if you get to the answers yourself. However you should note that to really appreciate nature and its many micro-processes, you have to study it from all different sorts of angles (don't only focus on biology but also on physics, chemistry, biochemistry). To fully appreciate the answers to the questions you've listed above, you should probably have a strong foundation in biochemistry and physics.
1. Everything is signaled/coded/instructed originally from DNA. Trial and error similar to hydrogen bonding will take place with tRNAs that are trying to attach to the mRNA until there is a right fit. If the bonding isn't strong enough it will leave the ribosome either be broken down for parts or reused. There are only 21 different amino acids. This brings up the idea that our genetic code is redundant. That is, we have 64 different codons and only 21 amino acids. More than one codon can specify for an amino acid. 2. When mRNA leaves the nucleus, it first goes looking for a ribosome, special proteins built to accept the mRNA strand. When translating at least one kind of tRNA is present for each of the 20 amino acids used in protein synthesis.Topoisomerase deals with super helical DNA. Helicases are enzymes that use ATP-driven motor force to unwind double-stranded DNA or RNA. Recently, increasing evidence demonstrates that some helicases also possess rewinding activity-in other words, they can anneal two complementary single-stranded nucleic acids. Single stranded binding proteins prevent premature annealing, to protect the single-stranded DNA from being digested by nucleases, and to remove secondary structure from the DNA to allow other enzymes to function effectively upon it. 3.The amino-acid sequence of a protein determines its conformation. A protein molecule folds spontaneously during or after biosynthesis. While these macromolecules may be regarded as "folding themselves", the process also depends on the solvent (water or lipid bilayer), the concentration of salts, the pH, the temperature, the possible presence of cofactors and of molecular chaperones. Minimizing the number of hydrophobic side-chains exposed to water is an important driving force behind the folding process. Formation of intramolecular hydrogen bonds provides another important contribution to protein stability. The strength of hydrogen bonds depends on their environment, thus H-bonds enveloped in a hydrophobic core contribute more than H-bonds exposed to the aqueous environment to the stability of the native state. Also reference Anfinsen's dogma and Levinthal's paradox. Hope this could help! These answers are from several sources: www.hindawi.com/journals/jna/2012/140601/ education-portal.com/academy/lesson/trna-role-function-synthesis.html en.wikipedia.org/ education-portal.com/academy/lesson/the-role-of-ribosomes-and-peptide-bonds-in-genetic-translation.html
Yes, perhaps I should have cleared that up. The rRNA are assembled in the nucleolus and trimmed there as well. They then bind to their appropriate proteins (which come from the cytoplasm) to form the 40S and 60S subunits. However, the two subunits do not combine inside the nucleolus to form the ribosome. They are transported out of the nucleus at different times and then combine with their appropriate mRNA molecule in the cytoplasm. Sorry for the confusion! I put an annotation to clear that up.
I think you made a slight oversimplification when saying that RNA consists primarily in the linear form. For example, the yeast phenylanyl-tRNA molicule primarily exists in an L-shaped structure that is formed as a result of hydrogen-base pairing. This three dimensional structure of RNA is what gives it many of its unique properties
Can you be specific as to where I said that? Im pretty sure that by linear I meant single-stranded. The three-dimensional structure of RNA does in fact give it its unique properties (i.e. the structure of tRNA gives it the ability to act as a carrier of amino acids)
Question: So the tRNA brings the raw material amino acids to the ribosome factory to make longer chain proteins. Who makes these "raw material" amino acids then?
If rRNA makes ribosomes utilizing proteins that mRNA created with the ribosomes, thjs sounds like a logical fallacy... Which came first? How do you create the ribosome with a protein that required a ribosome to be created?
according to my biology teacher, uracil requires less energy than thymine and because proteins are constantly being synthesized in large numbers, the body tries to save as much as energy as possible
![Quando Rondo - Grow Up [Official Music Video]](http://i.ytimg.com/vi/8zFnCg3BO4Q/mqdefault.jpg)
So...
mRNA = planner "Architect" who makes the blueprint.
tRNA = supplier "Home Depot" who gets the material and brings it to the job site.
rRNA = builder "Carpenter" who assembles the material (proteins) brought in by tRNA and puts them together according to the instructions given by mRNA.
I know that's overly-simplified, but is it pretty much on track Andrey?
Thank you for organizing!
정리해 주셔서 감사합니다!
^-^♡
This couldn't have been more clear. Briliantly explained.
8 years later and your videos are still helpful. God bless you!
Biochemistry made so simple. Good work. Great lecture. Thank you so much.
ihuoma chukuigwe You're welcome ! :)
THE THYMINE STRUCTURE IS INCORRECT!!
This was incredibly helpful. I couldn't have asked for a better video to describe all of this confusing information.
I'm in optometry school and find this helpful to brush up on the basics of molecular biology. Good job!
Thank you I was going through many videos trying to find one that made sense to me and yours made this all very clear! I'm going to ace my test!!!
Emma Jaworowski thats great to hear Emma! good luck on your exam :)
Your lectures have saved me from failing biochem! Thank you! Friendly reminder to review thymine's structure :)
Thank you so much🙏✨ I wish you also had free lectures on population genetics
this guy deserves so many more subscribers
Pardoned me for mentioning, but this man’s intelligence is attractive😍😍
The Thymine structure looks a little different in my textbook which shows that Thymine has two double O bonds instead of one double O bond and an NH2 group.
Thank you so much for this lecture!!! You're totally making my Biology test possible to pass! :)
It's chemistry bruhhh
Hope ua still alive to see this after six years😂😂
5:50 thank me later for the saving time.
TY SO MUCHHHH
You are truly amazing and getting me through biochem. God bless your soul, you are truly a really good teacher :)
I just don't know how to appreciate your good work towards me, you are such an amazing tutor , you will live long to enjoy the goodness of the Lord in the land of the living,💖 once again, thank you so much.
The Thymine molecule have a carbonyl group between the nitrogen atoms. it is identical to the uracil, but in addition it has a methyl group left to the first carbonyl group.
Thank you. There are some RNA types - hn-RNA(heterogeneous nuclear RNA) or pre-mRNA and small nuclear RNA (snRNA)
and many more than that! but that would of been a very long video :)
7.08 Is a mistake. My comment: In Eucariotic cells single gene is used to make many different proteins due to alternative splicing of introns, and procariotic gene usually code for single protein, cause procariotic genes mostly do not have introns.
But 1 procariotic gene can have many ORF’s => many proteins from one gene
He just messed words eukaryote and prokaryote.
Very good site for studies
well explained and in a very effective style of speaking. i look forward to watching more of your lectures to help myself better understand these processes. thank you.
Very good video! Thanks for taking the time to make these videos. The picture you called Thymine is actually guanosine, I think
My 2 favorite accents are Portuguese and Boston, I can listen to your videos all day😂 oh and thank you for the amazing quality of content😂
Couldn’t have been clearer. Thank you
Wow you covered a lot in 10 minutes. Thanks!
finally i could understand this hardcore concept.
I would die for AK lectures
Thanks so much for creating these lecture videos they are very interesting and helpful!
Thank you so much! Your lectures are really helpful and easy to understand. Cleared up many important concepts for me, especially for biochemistry and biology.
awesome videos
extremely helpful
I find all these lectures fascinating as I'm just starting out in this field. I have a three questions which I simply can't find answers to, but perhaps nobody knows yet!! If you're able to point me to a source I'd be very appreciative...
1) How do molecular machines know what to do? What signal / code / instruction / information do they receive, and from where? For example, there are many tRNA molecules carrying their amino acids in the cytoplasm - how do they know its their ‘turn’ to descend to the ribosome and release their amino acid on the correct codon? I could think of dozens more……!
2) Regarding the 23 pairs of chromosomes, how does the RNA polymerase know which gene to transcribe, and how is the tightly-knit DNA unwound from the chromosome? What coils it back again?
3) How does the barrel receiving the recently folded protein know what shape to fold it? If the cell is producing a protein, its because the body needs it. So, did the barrel receive this information? Does it recognise the protein and understand what it needs to become? Does it have a ‘memory bank’ of all the types of proteins the body produces?
Thanks in advance....
Drumming Spain I think its much more productive to you if you discover these answers on your own. Its natural to have these questions at the beginning and you will appreciate it much more if you get to the answers yourself. However you should note that to really appreciate nature and its many micro-processes, you have to study it from all different sorts of angles (don't only focus on biology but also on physics, chemistry, biochemistry). To fully appreciate the answers to the questions you've listed above, you should probably have a strong foundation in biochemistry and physics.
AK LECTURES
Ok, thanks for the reply
Drumming Spain yup.
1. Everything is signaled/coded/instructed originally from DNA. Trial and error similar to hydrogen bonding will take place with tRNAs that are trying to attach to the mRNA until there is a right fit. If the bonding isn't strong enough it will leave the ribosome either be broken down for parts or reused. There are only 21 different amino acids. This brings up the idea that our genetic code is redundant. That is, we have 64 different codons and only 21 amino acids. More than one codon can specify for an amino acid.
2. When mRNA leaves the nucleus, it first goes looking for a ribosome, special proteins built to accept the mRNA strand. When translating at least one kind of tRNA is present for each of the 20 amino acids used in protein synthesis.Topoisomerase deals with super helical DNA. Helicases are enzymes that use ATP-driven motor force to unwind double-stranded DNA or RNA. Recently, increasing evidence demonstrates that some helicases also possess rewinding activity-in other words, they can anneal two complementary single-stranded nucleic acids. Single stranded binding proteins prevent premature annealing, to protect the single-stranded DNA from being digested by nucleases, and to remove secondary structure from the DNA to allow other enzymes to function effectively upon it.
3.The amino-acid sequence of a protein determines its conformation. A protein molecule folds spontaneously during or after biosynthesis. While these macromolecules may be regarded as "folding themselves", the process also depends on the solvent (water or lipid bilayer), the concentration of salts, the pH, the temperature, the possible presence of cofactors and of molecular chaperones. Minimizing the number of hydrophobic side-chains exposed to water is an important driving force behind the folding process. Formation of intramolecular hydrogen bonds provides another important contribution to protein stability. The strength of hydrogen bonds depends on their environment, thus H-bonds enveloped in a hydrophobic core contribute more than H-bonds exposed to the aqueous environment to the stability of the native state. Also reference Anfinsen's dogma and Levinthal's paradox.
Hope this could help!
These answers are from several sources:
www.hindawi.com/journals/jna/2012/140601/
education-portal.com/academy/lesson/trna-role-function-synthesis.html
en.wikipedia.org/
education-portal.com/academy/lesson/the-role-of-ribosomes-and-peptide-bonds-in-genetic-translation.html
Henry Shelonzek Thanks Henry... that's going to take me a while to digest! Many thanks for the reply
Many thanks.
Amazing lecture 👍
It's so great video, thank you so much, I appreciate your lectures soooooo much really
Thanks for this. These lectures are very helpful. :)
Aud :3 you're welcome! glad to hear it
This video was helpful a ton, I have now subscribed to this channel.
@5:47 U can find the entire board.. Take a screen shot of it! ;)
I learned that protein enters the nucleolus & joins with rRNA to form a ribosomal subunit which then leaves the nucleus and enters the cytoplasm....
Yes, perhaps I should have cleared that up. The rRNA are assembled in the nucleolus and trimmed there as well. They then bind to their appropriate proteins (which come from the cytoplasm) to form the 40S and 60S subunits. However, the two subunits do not combine inside the nucleolus to form the ribosome. They are transported out of the nucleus at different times and then combine with their appropriate mRNA molecule in the cytoplasm. Sorry for the confusion! I put an annotation to clear that up.
I beg of you to make a video about secondary and tertiary structures of RNA as well as modified nucleotides. PLEASE do
I think you made a slight oversimplification when saying that RNA consists primarily in the linear form. For example, the yeast phenylanyl-tRNA molicule primarily exists in an L-shaped structure that is formed as a result of hydrogen-base pairing. This three dimensional structure of RNA is what gives it many of its unique properties
Can you be specific as to where I said that? Im pretty sure that by linear I meant single-stranded. The three-dimensional structure of RNA does in fact give it its unique properties (i.e. the structure of tRNA gives it the ability to act as a carrier of amino acids)
You did say single stranded multiple times. I misinterpreted what you meant. Thanks for clarifying! Good video otherwise!
Michael Welch No problem! thanks! :)
thank you very much
very helpful and easy to understand keep up the good work
Thanks so much! This was so clear!!
Glad to hear that! You're welcome!
its very helpful.. and easily can remember the function
Thank you so much, this is a great lecture
You're welcome!
You are supper genius 😘😘
U R so Gr8 ... Thanks❤️❤️
This's awesome. thank you so much.
Brown Scott Martin Anthony Hernandez George
Thank you
I love you.
Unfortunately the thymine structure is wrong
Still a great video though
Thanks. It was so clear and helpful:)
sir can you explain differences between uracil and thymine
thymine is drawn incorrectly
Can you make a video on tRNA synthetase?
hmmm.quite good.BTW what does AK stand for?
thanks! AK are the initials of my full name :-)
Question: So the tRNA brings the raw material amino acids to the ribosome factory to make longer chain proteins. Who makes these "raw material" amino acids then?
Old "used" proteins are disassembled + new amino-acids are continuously brought from the outside of the cell - result of the food digestion.
Can u please explain how there are mutations if the body has an enzyme that goes through a process to make sure there is nothing wrong in the gene
well... thymine should not only have one O right?? NH2 in thymine should be O
Thank you Sir
Thanks a lot you are amazing
Well explained ..but why does thymine has amine group yet it should not be there?
it should have Oxygen atom there, right?
yeah
you're awesome!
If rRNA makes ribosomes utilizing proteins that mRNA created with the ribosomes, thjs sounds like a logical fallacy... Which came first? How do you create the ribosome with a protein that required a ribosome to be created?
goodjob. my only comment is that thymine does not have nh2 it is another double bonded oh
thanks soo much. atleast i got the diffrence!
Sir how to synthesis of mRNA and rRNA
Can someone explain to me why rna have uracil instead of thymine?
no
thank you
en.wikipedia.org/wiki/Thymine Just a heads up check ur structers. Keep up the good work though loving the energetic presentation!
thankyouuuu so muchhhh
The Uracil structure isn't correct, but otherwise your lecturing style really helps me out!
Thank you!
upload.wikimedia.org/wikipedia/commons/thumb/9/9e/Uracil_chemical_structure.png/150px-Uracil_chemical_structure.png
Sir I want in vitro fertilisation(IVF) note ..
I enjoy your lecture video's but you move around too much which is really distracting!
Great lecturer, but the way he talks is like a computer... each and every word is pronounced very distinctly :)
Why uracil is present instead of thayamin
according to my biology teacher, uracil requires less energy than thymine and because proteins are constantly being synthesized in large numbers, the body tries to save as much as energy as possible
I love you😍
All of this happen with this accuracy and still don't believe in Allah!
Waw
FWV =10000
h
Thank you sir