Your videos are really helpful! My teachers are good but I don't always understand or remember the concepts right away. Pictures and animations also really help for some reason. It must have been so hard to learn things before we had all this technology
Thank you 😊 I searched this up because my teacher had us play a game to make it more "fun" but I ended up learning nothing now I need to learn it on my own 😐
At 6:33 minutes you said competitive inhibitors are the same shape as the substrate but my teacher said saying that would make you lose the mark as they aren’t the same shape but they are similar, does this matter?
Thank you so much! I love your videos, they tell me everything I need to know in a way that makes it easy to digest and easy to concentrate on. So thank you! :)))
Why does the human body have competing inhibitors? What is their purpose in the body if it stops enzymes from binding to their substrate isn’t that a bad thing?
Could you explain to me the following questions Enzyme X is produced by thermophilic bacteria and hydrolyses many protein including haemoglobin and egg albumin. Enzyme Y is found in the stomach of young mammals where it acts on single soluble protein found in milk ,causing it to coagulate clot 1 a. From description, comment on differences inspecificity of two enzymes b. Enzymes X and Y used for difference commercial purpose.Suggest what this might be in that case. C. Suggest a possible purpose of enzyme Y in mamalian stomach. d. Use information about the two enzymes to suggest the possible difference type of bonding found in type of structure of each. Explain your reasoning.
Hi, I just wanted to ask which practical should we learn for enzymes? I have come across so much different versions for the practical that I am confused and don't know which one to learn
there isn't a particular practical method to learn. It could be any variable effecting any enzyme. You aren't expected to learn a method,more the practical skills and general understanding of variables and use of apparatus.
Hello, All exam boards will have different requirements so I suggest checking your specification closely when you revise. Maybe print out a copy/have an electronic copy that you can tick off the content as you learn to see your progress the level of detail required :D
not exactly. You need to be specific. Only a high temperature can denature Too high or too low ph denatures Non competitive we wouldn't describe as denature. This is just a factor that affects the rate
Miss Estruch thank you so much !! I was also wondering do you have a video where you explain/solve some enzyme-controlled reactions’ graphs , i mean a video specifically about graphs ? I do understand all the factors that can affect an enzyme activity but find some difficulties when describing and explaining those factors in a graph
hi miss your video was so helpful but I have one question, is the amino acid sequence of the competitive inhibitor the same as the substrate or is it completely different?
Your videos are really helpful! My teachers are good but I don't always understand or remember the concepts right away. Pictures and animations also really help for some reason. It must have been so hard to learn things before we had all this technology
ah thank you, so pleased it helped! If definitely makes things easier having diagrams and animations!
you're sooo good. I am so glad my friend recommended your page to me
awww thank you 😊 Hope the videos help
Thank you 😊 I searched this up because my teacher had us play a game to make it more "fun" but I ended up learning nothing now I need to learn it on my own 😐
So glad my video helped! Hopefully you can make notes from it 😊
May god bless you 🙏 this was very helpful for me! Thank you so much! 💜
you're welcome 😊 So glad it helped you
URRRR SOOO PRETYYYYYY N KINDDDDD N AMAZING BEST BIO TEACHER ✨✨✨✨✨
8:48 if induced fit takes place won’t the enzyme be able to bind with the substrate even if it’s shape is slightly changed?
changed a bit too much probably
Love ur videos just have a test right now thanks a lot 😊
Good luck!!!!
And this video is so good!!!!
Thank you!
At 6:33 minutes you said competitive inhibitors are the same shape as the substrate but my teacher said saying that would make you lose the mark as they aren’t the same shape but they are similar, does this matter?
the mark schemes say same/similar. They key marking point is that the inhibitor binds to the active site
cheers
AYYYYYYYYYYYYY AYYYYY AYYYYY AYYYYY AYYYYY cheers
Thank you!
you're welcome 😊
Thank you your video was really helpful
Glad it was helpful!
Miss I have to appear for 9700 biology in 2024, is this the right place?
yupp
Thank you so much! I love your videos, they tell me everything I need to know in a way that makes it easy to digest and easy to concentrate on. So thank you! :)))
You are so welcome! Really glad you like them and find them so helpful.
Why does the human body have competing inhibitors? What is their purpose in the body if it stops enzymes from binding to their substrate isn’t that a bad thing?
it helps to regulate reactions to prevent overheating and wasting resources 😊
Thank you
You're welcome 😊
But wait, if the pH is too low there are many H ions while if it's too high it has many OH ions. You said the other way round!
hello, what minute is that? ill check for the error and correct in description 😊
2:05 miss
Great spot! Thank you for highlighting, I've corrected in the description
@@MissEstruchBiology Thank you for your clear explanation!
super mam you are great
Very nice, thanks!
Glad you like it!
Wow it's so helpful
Thank you, so pleased it helped
doesnt low ph have more H+ ions and higher ph has more OH- ions ?
You're right
What does it mean when the actuve site becomes saturated
it means that all the available enzymes already have substrate bound to their active sites.
Could you explain to me the following questions
Enzyme X is produced by thermophilic bacteria and hydrolyses many protein including haemoglobin and egg albumin.
Enzyme Y is found in the stomach of young mammals where it acts on single soluble protein found in milk ,causing it to coagulate clot
1 a. From description, comment on differences inspecificity of two enzymes
b. Enzymes X and Y used for difference commercial purpose.Suggest what this might be in that case.
C. Suggest a possible purpose of enzyme Y in mamalian stomach.
d. Use information about the two enzymes to suggest the possible difference type of bonding found in type of structure of each. Explain your reasoning.
Hi, I just wanted to ask which practical should we learn for enzymes? I have come across so much different versions for the practical that I am confused and don't know which one to learn
there isn't a particular practical method to learn. It could be any variable effecting any enzyme. You aren't expected to learn a method,more the practical skills and general understanding of variables and use of apparatus.
Do we need to know end-product inhibitors?
What about metabolic pathways? Do we not need to know about that? 😬
Hello,
All exam boards will have different requirements so I suggest checking your specification closely when you revise. Maybe print out a copy/have an electronic copy that you can tick off the content as you learn to see your progress the level of detail required :D
Thank you so much miss
So do we say that temperature, ph values and non competitive inhibitors can all be factors that can denature an enzyme ?
not exactly. You need to be specific.
Only a high temperature can denature
Too high or too low ph denatures
Non competitive we wouldn't describe as denature. This is just a factor that affects the rate
Miss Estruch thank you so much !!
I was also wondering do you have a video where you explain/solve some enzyme-controlled reactions’ graphs , i mean a video specifically about graphs ?
I do understand all the factors that can affect an enzyme activity but find some difficulties when describing and explaining those factors in a graph
Hi, just wanted to know What are the bonds that are broken when temperature increases?
Hello, It would be hydrogen first and then ionic. 😊
@@MissEstruchBiology thank you so much for replying by the way what happens to disulphide and peptide bonds? Do they break or are they too strong?
@@animationbooth_28 nothing would happen to them, they’re covalent so much stronger
hi miss your video was so helpful but I have one question, is the amino acid sequence of the competitive inhibitor the same as the substrate or is it completely different?
Hi, I was just wondering if the graphs for enzyme concentration and substrate concentration are the same?
hey, yes they have the same curve but different axis labels.
@@MissEstruchBiology Thank you 😄
Wait is this for alevel?
yes, this is A-level
2:54
Hi guys
Hello 👋