Hemoglobin and myoglobin
Вставка
- Опубліковано 19 кві 2015
- This lecture explains about Hemoglobin and myoglobin structural and functional similarities and differences.
Myoglobin and hemoglobin are hemeproteins whose physiological importance is principally regarding their ability to bind molecular oxygen. Myoglobin is a monomeric heme protein found usually in muscle tissues the place it serves as an intracellular storage website for oxygen. Throughout periods of oxygen deprivation oxymyoglobin releases its certain oxygen which is then used for metabolic purposes.
The tertiary constitution of myoglobin is that of a typical water soluble globular protein. Its secondary constitution is amazing in that it contains an extraordinarily high proportion (75%) of α-helical secondary structure. A myoglobin polypeptide is comprised of eight separate correct passed α-helices, targeted A via H, which are connected by quick non helical regions. Amino acid R-agencies packed into the internal of the molecule are predominantly hydrophobic in character whilst those exposed on the surface of the molecule are ordinarily hydrophilic, accordingly making the molecule moderately water soluble.
Every myoglobin molecule comprises one heme prosthetic staff inserted right into a hydrophobic cleft in the protein. Every heme residue comprises one relevant coordinately certain iron atom that is in most cases within the Fe2+, or ferrous, oxidation state. The oxygen carried with the aid of hemeproteins is sure instantly to the ferrous iron atom of the heme prosthetic group. Oxidation of the iron to the Fe3+, ferric, oxidation state renders the molecule incapable of traditional oxygen binding. Hydrophobic interactions between the tetrapyrrole ring and hydrophobic amino acid R groups on the inner of the cleft within the protein strongly stabilize the heme protein conjugate. Furthermore a nitrogen atom from a histidine R crew placed above the airplane of the heme ring is coordinated with the iron atom further stabilizing the interplay between the heme and the protein. In oxymyoglobin the remaining bonding web site on the iron atom (the 6th coordinate role) is occupied with the aid of the oxygen, whose binding is stabilized by using a 2d histidine residue.
Carbon monoxide also binds coordinately to heme iron atoms in a fashion just like that of oxygen, but the binding of carbon monoxide to heme is far improved than that of oxygen. The preferential binding of carbon monoxide to heme iron is largely liable for the asphyxiation that outcome from carbon monoxide poisoning.
Grownup hemoglobin is a [α(2):β(2)] tetrameric hemeprotein discovered in erythrocytes where it's liable for binding oxygen within the lung and transporting the bound oxygen throughout the physique where it is used in cardio metabolic pathways.
For an outline of the special forms of hemoglobin tetramers see the part below on Hemoglobin Genes. Each subunit of a hemoglobin tetramer has a heme prosthetic workforce same to that described for myoglobin. The usual peptide subunits are specific α, β, γ and δ which might be arranged into probably the most most of the time happening functional hemoglobins.
Even though the secondary and tertiary constitution of various hemoglobin subunits are an identical, reflecting huge homology in amino acid composition, the versions in amino acid composition that do exist impart marked differences in hemoglobin's oxygen carrying residences. Furthermore, the quaternary constitution of hemoglobin leads to physiologically most important allosteric interactions between the subunits, a property missing in monomeric myoglobin which is in any other case very similar to the α-subunit of hemoglobin.
Evaluation of the oxygen binding residences of myoglobin and hemoglobin illustrate the allosteric houses of hemoglobin that outcome from its quaternary constitution and differentiate hemoglobin's oxygen binding properties from that of myoglobin. The curve of oxygen binding to hemoglobin is sigmoidal typical of allosteric proteins wherein the substrate, in this case oxygen, is a positive homotropic effector. When oxygen binds to the primary subunit of deoxyhemoglobin it increases the affinity of the remaining subunits for oxygen. As further oxygen is sure to the 2d and 0.33 subunits oxygen binding is further, incrementally, bolstered, in order that on the oxygen anxiety in lung alveoli, hemoglobin is completely saturated with oxygen.
For more information, log on to-
www.shomusbiology.com/
Get Shomu's Biology DVD set here-
www.shomusbiology.com/dvd-store/
Download the study materials here-
shomusbiology.com/bio-material...
I am retired prof of zoology, just by the way I came across your lecture. Well done. You are so young and explaining well. Congratulations god bless you
Hey mam cn u tell me which group is responsible for red color of haemoglobin
Whether it is a globin or hame containing iron
Plz rply me
@@anjusheoranbiosmarterevery6186 The binding of oxygen with the heamgroup is responsible for the red color. This means that de-oxyginated blood (so blood that returns to the heart) will look darker (less bright red), because there's almost no oxygen left in the haemgroups. A haemgroup without O2 will therefore not be responsible for the red color, the *combination* of the haemgroup with the central Fe-ion and O2 bound to it on the other hand will.
@@stijndebuf1654 cn we say that red color of haemoglobin is due to iron
@@anjusheoranbiosmarterevery6186 yes we can say
When I don't understand my Professors you are the solution to my problems since my undergraduate days
biochemical terminology like cooperativity , allosterity and so on should be take in consideration, information is well compiled. Thanks sir .
First of all I apologize for judging .. i came here coz i thought it wont be beneficial but rather stupid and funny .. but i was wrong and i am sorry ! that was really really really helpful ! I love the way u broke it down ( made it look so easy ) thx again and sorry :D
Thank you very much, that's helped me alot. You make super easy!
Sir give me a lecture about prediction of secondary structure of protein by using neural network and GOR
method
Your classes are very helpful thank you sir
Hello Shomu may I ask is myoglobin found in both cytoplasm and mitochondria?
What is allosteric effect ? Any reply would be greatly appreciated.
what is the position on beta globin chain if RBC Hb E ?
Very clear, thank you.
Sir, please deliver a lecture on multiple drug resistance
Sir plz tell what exactly is the role of iron in hemoglobin and myoglobin except for maintaining the structure.....
iron is at the core of heme and it is what the oxygen binds to
Another really helpful video from you.
You're welcome
Stay blessed and happy,u r sooo honest in teaching
Thank you. Glad you liked my lectures
No doubt sir.please keep it going our nation needs lecturer like you
Special thanks for explanation below n description box
Thanqqq sir for making such videos they r really helpful
Uhh r doing a grt job ...🌼
Glad to hear that you're getting benefit from my lectures
Sir hb par charge konsa hota h please reply me and other wise friends bhi bata sakte h
i lik ur way of teaching ...................thnq sir
Excellent! Sir please........ please.......... give a lecture on oxyheamoglobin dissociation curve
You r gerat sir ...Thank you so much for your valuable vedioes....please make morr vedioes for us ...
+Priyankaliza Sahu will do that. Thank you
thnxx sir .very nice and clear my mind
How many peptide bonds in one molecule of heomoglobin ??
Sir....please make a video on absorption in small intestine
Sir give me a lecture on Binding of oxygen to heme
Thank you sir u helping me a loooooot
You're welcome
Nice explanation sir..... carry on
You're welcome
thank you so much....sir
good lecture
good Sir...
Sir, Why myoglobin has greater affinity towards oxygen than Hemoglobin?
Sir please upload cns topics
Anna rbc calculation cheppu please broo
thanks sir
Is the primary structure of myoglobin and haemoglobin the same?
No
U r too good😊
Thank you so much for appreciating my efforts
Superb👍
Thank you for appreciating my efforts
Superb sir
Thank you
Nice class sir 🔥🔥
Thank you
aap hindi mai bhi bnaya krona
Color of haemoglobin is red due to globin or hame containing iron
Plz rply
Heme containing iron
@@shomusbiologyofficial sir my sir say due to globin
Please briefly explain myoglobin it is not enough plzzzzz
26?
very good lecture!! I am from southern Louisiana and I think his voice is great. are you here learn or be ugly?
Sir me from Kashmir i want talk to you
Answer of qsn is Ribozyme
Sir I clearly doubt free from your expalanation
Glad to hear that you're getting benefit from my lectures
Sir check the spelling of haem?
what is ur age sir
sir hindi me bolte to ziada samjh aata
for hindi, you can shift to our channel
gud but gain confidence sir
Confirmed to reply me
👌👌👌👌
mai smgni k lye bol rhi thi Sir...agr aap ko bura lga ho tuo sry
India k ho k b ye expalin English mai kr rhai hai
Phd hindi me nehi hota
hello sir
Hello
Good but not detailed explanation
Exactly my thought, lacks a bit details here and there for people who came before studying "go back to the book, can't remember right now..etc". Was pretty good at explanation though; simple and easy to understand.
sir plz hindi
you can come at our channel for hindi videos for net preparation.
good good i like it
+Hydes thank you. Glad it helped
myosin
Over....
Hindi me samjhao na
english super
Hindi mai explain karo
I wht Telugu calls
Vo hadephone kyu lgaya hai Bhai. Like a joker🃏
Check the published date. You didn't even know UA-cam then
Why your teach fast pls slow
U can say protein is macromolecule instead of large 😑
good but u should practice in talking English
Could you please speak slower lol?
Hindi me bolne me phat gayi hea kya
I am non native to hindi
Not good method of teaching
How many peptide bonds in one molecule of heomoglobin ??
There are 570 peptide bonds.
what is ur age sir
26?
what is ur age sir
what is ur age sir
what is ur age sir
+Giftpal Singh 26
26?
60