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Search results “Determining km of an enzyme produced”

19:44
Views: 74179 Shomu's Biology

07:17
Project Title: Development of e-contents on foundation course on analytical biochemistry and separation techniques Project Investigator: Dr. Charmy Kothari Module: Substrate kinetics of enzyme (determination of Km and VMAX)
Views: 2571 Vidya-mitra

05:24
You need to know the 3 parts of the graph: a) initially linear since many free enzymes available at the lower concentration of substrate. b) rate begins to slow as substrate cannot always find a free enzyme (some are being used by other substrate) c) Saturated -- the enzymes are always in use -- increasing substrate will no longer increase rate. Adding inhibitors will change these graphs -- but this is for another assessment statement.
Views: 99325 Richard Thornley

16:22
Views: 204487 Moof University

03:56
In this video I have explained how to calculate the value of Km and Vmax for an enzyme substarte reaction using Michaelis-Menten equation. Thanks to Amanda Moulton for painstakingly recording this video.
Views: 8951 Dr.Mungli

04:44

07:31
Moof's Medical Biochemistry Video Course: http://moof-university.thinkific.com/courses/medical-biochemistry-for-usmle-step-1-exam For Related Practice Problems with Worked Video Solutions on Enzymes, visit courses.moofuniversity.com. In this video, I discuss how the Lineweaver-Burk (or Double-Reciprocal) Plot works in association with hyperbolic equation and Michaelis-Menton kinetics. Hyperbolas, when it comes to math, are not simple to work with, which is why the hyperbolic equation relating to Michaelis-Menton kinetics is altered to give the Lineweaver Burk equation / Double Reciprocal plot. It basically turns the hyperbolic equation into a linear equation, which is much easier to work with. The graph becomes 1/V plotted versus 1/substrate concentration. The x intercept is equal to -1/Km, and the y intercept is equal to 1/Vmax, which makes it easy to calculate for either when the values for the intercepts are available. The slope of the line is equal to Km/Vmax. For a suggested viewing order of the videos, information on tutoring, personalized video solutions, and an opportunity to support Moof University financially, visit MoofUniversity.com, and follow Moof University on the different social media platforms. Don't forget to LIKE, COMMENT, and SUBSCRIBE: http://www.youtube.com/subscription_center?add_user=MoofUniversity SUPPORT MOOF UNIVERSITY: http://www.moofuniversity.com/support-moof/ BUY A T-SHIRT https://shop.spreadshirt.com/moofuniversity/ INFORMATION ABOUT TUTORING AND PERSONALIZED VIDEO SOLUTIONS: http://www.moofuniversity.com/tutoring/ INSTAGRAM: https://instagram.com/moofuniversity/ FACEBOOK: https://www.facebook.com/pages/Moof-University/1554858934727545 TWITTER: https://twitter.com/moofuniversity
Views: 124668 Moof University

06:27
The enzyme kinetics specially explaining their Km and Vmax is done in three parts. This is part 1, kindly watch other 3 parts to complete this series. Thanks to Amanda Moulton for painstakingly recording this video
Views: 39228 Dr.Mungli

16:07
Views: 72556 AK LECTURES

17:14
Views: 60721 Shomu's Biology

05:37
Moof's Medical Biochemistry Video Course: http://moof-university.thinkific.com/courses/medical-biochemistry-for-usmle-step-1-exam For Related Practice Problems with Worked Video Solutions on Enzymes, visit courses.moofuniversity.com. In this video, I basically do an example problem relating to Michaelis-Menton Kinetics, the Hyperbolic Equation, and the Lineweaver-Burk (Double Reciprocal) Plot. For a suggested viewing order of the videos, information on tutoring, personalized video solutions, and an opportunity to support Moof University financially, visit MoofUniversity.com, and follow Moof University on the different social media platforms. Don't forget to LIKE, COMMENT, and SUBSCRIBE: http://www.youtube.com/subscription_center?add_user=MoofUniversity SUPPORT MOOF UNIVERSITY: http://www.moofuniversity.com/support-moof/ BUY A T-SHIRT https://shop.spreadshirt.com/moofuniversity/ INFORMATION ABOUT TUTORING AND PERSONALIZED VIDEO SOLUTIONS: http://www.moofuniversity.com/tutoring/ INSTAGRAM: https://instagram.com/moofuniversity/ FACEBOOK: https://www.facebook.com/pages/Moof-University/1554858934727545 TWITTER: https://twitter.com/moofuniversity
Views: 81004 Moof University

20:59
Views: 17687 Shomu's Biology

11:09
In this video I work a problem that asks us to determine which enzyme is more efficient. I also explain the conditions in which it is useful to determine the Kcat by using the equation Kcat= Vmax/Km
Views: 7189 FortuneFavorsPrep

13:40
Using Excel to do the Lineweaver-Burk plot
Views: 37891 Mark Temple

05:36

04:32
In this video I have explained how to calculate Km and Vmax of an enzyme in Lineweaver Burk double reciprocal plot. The Lineweaver–Burk plot was widely used to determine important terms in enzyme kinetics, such as Km and Vmax, before the wide availability of powerful computers and non-linear regression software. The y-intercept of such a graph is equivalent to the inverse of Vmax; the x-intercept of the graph represents −1/Km. It also gives a quick, visual impression of the different forms of enzyme inhibition. You Can Subscribe to my Channel for REGULAR UPDATES by clicking on SUBSCRIBE button above! You can follow me on my BLOG by clicking the link below http://drmungli.blogspot.com/ You can follow my Facebook page Biochemistry Made Easy by Dr Prakash Mungli, MD by clicking the link below. Here I post USMLE step-1 style MCQs and you can participate in discussion. https://www.facebook.com/drmungli
Views: 23694 Dr.Mungli

07:32
Discussion of the meaning and graphical determination of the kinetic constants of Km & Vmax

07:32

11:56
Specific activity and turnover number of an enzyme
Views: 10333 Peter Klappa

14:07
Project Name: e-Content for undergraduate students of science in graduate programmes Project Investigator: Dr. Mandira Sikdar Module Name: Enzyme kinetics calculating VMAX and KM
Views: 1315 Vidya-mitra

11:10
Example of Km and Kcat from Educator.com’s Biochemistry class. Want more video tutorials? Our full lesson includes in-depth explanations and even more worked out examples. ►See the entire syllabus at https://www.educator.com/chemistry/biochemistry/hovasapian/?utm_source=YT&utm_medium=SEO&utm_campaign=BIOCHEMYT In this video, we’ll discuss km and kcat. You'll learn about the michaelis-Menten equation, second order rate constant, and enzyme's affinity. Like other instructors such as Khan Academy, Kevin Ahern, Moof University, and Armando Hasudungan? Our Biochemistry instructor is pretty awesome too. Professor Hovasapian carefully goes through how Proteins, Carbohydrates, Nucleic Acids and other biomolecules make life on Earth possible. Combining his triple degrees in Mathematics, Chemistry, and Classics, along with 10+ years of teaching experience, Professor Hovasapian expertly helps students understand difficult biochemical concepts. Raffi also teaches AP Chemistry, Multivariable Calculus, and Linear Algebra on Educator. So what are you waiting for? Join over 100K satisfied high school and college students who have aced their classes and exams with http://www.Educator.com’s videos.
Views: 20019 Educator.com

06:34
A presentation that will show you how to calculate the rate of a reaction from experimental data.
Views: 14560 Paul Scott

06:03
Views: 1464 UTM Chemistry

14:39
In this video I discuss the various types of enzyme inhibition, and their graphs.
Views: 90335 FortuneFavorsPrep

14:07
In this video I do a problem where we determine the Vmax and Km for a normal uninhibited enzyme, and then determine the same the values when it's inhibited. The values are then plotted on a graph, and the type of inhibition is determined from the graph.
Views: 48128 FortuneFavorsPrep

11:08
Why Km does not change with the enzyme concentration.
Views: 5624 Peter Klappa

03:55
A quick guide for my students on how to use excel to get Km and Vmax
Views: 134498 DrDavidSmith

06:36
Views: 18676 Moof University

09:47
A number of important catalytic constants for enzyme reactions: Km, v max, kcat and kcat/vmax. Each convey different information about an enzyme's activity!
Views: 20391 biochemistry rocks

02:24
Applications and skills: Determination of the maximum rate of reaction (Vmax) and the value of the Michaelis constant (Km) for an enzyme by graphical means, and explanation of its significance.
Views: 10737 Mike Sugiyama Jones

14:43
using a Lineweaver Burk plot to analyse enzyme data This work is licenced under the Creative Commons Attribution-NonCommercial-ShareAlike 3.0 Unported License. To view a copy of this licence, visit http://creativecommons.org/licenses/by-nc-sa/3.0/ or send a letter to Creative Commons, 171 Second Street, Suite 300, San Francisco, California 94105, USA.
Views: 112917 Peter Klappa

06:47
Kinetics of chemical reactions with and without enzyme; variation of the initial rate with substrate concentration. Introduction of the Michaelis Menten equation.
Views: 30978 biochemistry rocks

15:47
Views: 41191 AK LECTURES

15:07
Determining the dissociation constant Ki for a competitive inhibitor
Views: 5536 Peter Klappa

08:40
Views: 28222 AK LECTURES

02:25
Thanks to Amanda Moulton for painstakingly recording this video!
Views: 10807 Dr.Mungli

10:28
Moof's Medical Biochemistry Video Course: http://moof-university.thinkific.com/courses/medical-biochemistry-for-usmle-step-1-exam Questions Answered in This Video: - What are competitive inhibitors, and what is mechanism by which they act? - How do competitive inhibitors affect the values of KM and VMAX? - How do competitively inhibited reactions look on the hyperbolic graph and Lineweaver-Burk plot? Don't forget to LIKE, COMMENT, and SUBSCRIBE: http://www.youtube.com/subscription_center?add_user=MoofUniversity INFORMATION ABOUT TUTORING: http://www.moofuniversity.com/tutoring/ TO SUPPORT MOOF UNIVERSITY WITH A FINANCIAL CONTRIBUTION: http://www.moofuniversity.com/support-moof/ INSTAGRAM: https://instagram.com/moofuniversity/ FACEBOOK: https://www.facebook.com/pages/Moof-University/1554858934727545 TWITTER: https://twitter.com/moofuniversity Video Content Summary: Competitive inhibitors "compete" with substrate for binding the enzyme's active site. Free enzyme will bind either the substrate OR the competitive inhibitor. It cannot bind both at the same time. If the enzyme binds the substrate, the enzyme-substrate complex forms, and the enzyme can convert the substrate into product. If, however, a competitive inhibitor binds the active site, the enzyme-competitive inhibitor complex forms, which cannot proceed towards products, for the simple reason that the competitive inhibitor impedes the ability of the substrate to bind to the enzyme. Since a competitive inhibitor blocks the substrate from binding, the competitive inhibitor essentially lowers the affinity of enzyme for the substrate. Thus increasing the KM. Despite this, VMAX can still be reached with a high enough substrate concentration. If the substrate concentration is sufficiently high, the substrates will out-compete the competitive inhibitor for binding at the active site, thus effectively overcoming the effects of the inhibitor. The effects of a competitive inhibitor on an enzyme-catalyzed reaction are depicted in a variety of ways in the video, and it is shown what happens to the hyperbolic graph and the Lineweaver-Burk plot, otherwise known as the double reciprocal plot.
Views: 12718 Moof University

09:41
Looking at Vmax, Vmax/Km and Km This work is licenced under the Creative Commons Attribution-NonCommercial-ShareAlike 3.0 Unported License. To view a copy of this licence, visit http://creativecommons.org/licenses/by-nc-sa/3.0/ or send a letter to Creative Commons, 171 Second Street, Suite 300, San Francisco, California 94105, USA.
Views: 34169 Peter Klappa

14:14
Views: 113487 AK LECTURES

09:41
Views: 2172 Catalyst University

10:02
Views: 2090 Gowtham Ganesan

07:56
Views: 21292 Catalyst University

08:10
Enzyme questions part 1 http://biochemjm.wordpress.com/2014/03/07/enzymes-part-1-questions/ Enzyme questions part 2 http://biochemjm.wordpress.com/2014/03/08/enzymes-part-2-questions/ Enzymes part 3 http://biochemjm.wordpress.com/2014/03/09/enzymes-part-3-questions/ Biochem JM blog http://biochemjm.wordpress.com/ Biochem JM YouTube http://www.youtube.com/user/BiochemJM
Views: 2072 BiochemJM

05:08
The Question asked to find Michaelis Menten Constant if graph is plotted against (1/rate) and (1/substrate concentration) and the values of slope and intercepts are given. Question was asked for 4 Marks in DEC 2017 CSIR Exam
Views: 4898 All 'Bout Chemistry

08:14

23:06
Views: 26888 Purdue Biochemistry

13:30
How to calculate the specific activity and turnover of an enzyme
Views: 37808 Peter Klappa

11:33
Views: 266 Catalyst University

09:05
This video screencast was created with Doceri on an iPad. Doceri is free in the iTunes app store. Learn more at http://www.doceri.com
Views: 37802 Stephen Murata

09:02
Moof's Medical Biochemistry Video Course: http://moof-university.thinkific.com/courses/medical-biochemistry-for-usmle-step-1-exam Questions Answered in This Video: - What are noncompetitive inhibitors, and what is mechanism by which they act? - How do noncompetitive inhibitors affect the values of KM and VMAX? - How do noncompetitively inhibited reactions look on the hyperbolic graph and Lineweaver-Burk plot? Don't forget to LIKE, COMMENT, and SUBSCRIBE: http://www.youtube.com/subscription_center?add_user=MoofUniversity INFORMATION ABOUT TUTORING: http://www.moofuniversity.com/tutoring/ TO SUPPORT MOOF UNIVERSITY WITH A FINANCIAL CONTRIBUTION: http://www.moofuniversity.com/support-moof/ INSTAGRAM: https://instagram.com/moofuniversity/ FACEBOOK: https://www.facebook.com/pages/Moof-University/1554858934727545 TWITTER: https://twitter.com/moofuniversity Video Content Summary: Noncompetitive inhibitors, unlike competitive inhibitors, do not bind at the active site. They bind a site elsewhere on the enzyme. Thus, they can bind free enzyme OR the enzyme-substrate complex. So, the enzyme-substrate complex, the enzyme-noncompetitive inhibitor complex, and the enzyme-substrate-noncompetitive inhibitor complex can all potentially form. Of course, as long as the noncompetitive inhibitor is bound, the enzyme will not be able to convert substrate into product. Since a noncompetitive inhibitor binds at a site other than the active site and does not have an impact on whether or not substrate can bind, the affinity of enzyme for substrate is not changed, and the KM value remains unchanged. However, the effect of a noncompetitive inhibitor cannot be overcome by increasing substrate concentration, and as long as there are noncompetitive inhibitors present, there will be a smaller number of functional enzymes, relative to an uninhibited case. Less functional enzymes means lower rate of catalysis and a lower VMAX. The effects of a noncompetitive inhibitor on an enzyme-catalyzed reaction are depicted in a variety of ways in the video, and it is shown what happens to the hyperbolic graph and the Lineweaver-Burk plot, otherwise known as the double reciprocal plot.
Views: 7795 Moof University