AS Biology - Enzymes topic. Explanation of competitive inhibitor and non-competitive inhibitor and how they affect Vmax and Km when you change the substrate concentration.
Пікірлер: 14
@daniyalalam36219 ай бұрын
WOW! The way you explain the concepts is just amazing. Love the style of your videos- short, concise slow and informative. I was looking everywhere to find some info about this topic as it is quite hard but you explained it in a jiffy. Hope you start making more videos on AS Biology!😃😃😃
@zane9192 жыл бұрын
Really underrated channel. Thanks
@samarashabon1621 Жыл бұрын
I've been so stumped the past hour trying to understand why Vmax is the same whether or not a competitive inhibitor is present and this really helped clarify things for me so much! Thank you !!!!
@amitthakur11547 ай бұрын
amazing explanation tq
@exploringwithmo48253 ай бұрын
Binding of non-competitive inhibitors does not interfere with the binding of the substrate, rather it induces a conformational change that makes the enzym worse at catalysing the reaction, thus rendering the enzym basically useless. Therefore, sence you have less working enzym, your Vmax decreases, but sence the binding of substrate to active site is not altered, the Km stayes the same.
@gudadutoit87362 жыл бұрын
Thanx. Extremely helpful.
@rehanabokhari4482 Жыл бұрын
Very nice explanation Stay blessed
@vishwasd1 Жыл бұрын
Thank you so much mam🙏🙏♥... It really made concepts crisp and easy😊
@hidayatullah8964 Жыл бұрын
Wow really it is amazing mam
@Joklam-vs4gjАй бұрын
What does km stand for
@th33_makamaeАй бұрын
It stands for Michaelis-mentem
@Joklam-vs4gjАй бұрын
What does km stand for
@th33_makamaeАй бұрын
It stands for Michaelis-mentem. You aren't required to know that though