Name: ligand binding and allosteric effects
Uploaded: 2023-04-30T18:28:41.000Z
Duration: 49 s
Channel: JoVE

K12 Standards

north-carolina-k-12-science-standard-course-of-study

North Carolina K-12 Science Standard Course of Study

9-12

Biology

from-molecules-to-organisms-structures-and-processes

From Molecules to Organisms- Structures and Processes

LS.Bio.1.2

Ligand Binding and Linkage

كثير من البروتينات بها مواقع متعددة حيث يقترن عندها الليجند, بالإضافة إل الموقع المسؤول عن وظيفة البروتينات ربط جزيء لأي من هذه المواقع غالبًا ما ينتج عنه تغييرات تشكُلية تبدّل شكل البروتين. عندما يؤثر هذا التغيير على ربط ليجاند أخر يوصف الموقعين كمتلائمين أو متلازمين إرتباط الموقع المتلازمة يكون منظم بطريقة إيجابيًة أو سلبيًة. في الترابط الإيجابي ربط أحد الليجاند يؤدي الى تغييرات فى التشكٌل بطريقة تجعل موقع آخر أكثر احتمالاًفي الربط بالليجاند الخاص به.في الترابط السلبى،ربط أحد اليجاند يؤدي الى تغيير فى التشّكل وهذا من شأنه أن يمنع أي موقع ربط آخر من الإقتران بالليجند الخاص به. البروتينات التي تحتوي على مواقع ربط متلازم تُسمى بروتينات تفارغية وممكن أن تكون من أنواع مختلفة،مثل الإنزيمات،المستقبلات البروتينات الهيكلية،وبروتينات الحركية على سبيل المثال،اسبارتات

<ol>
	<li>سوبلاتوف ، د. ، وسفيداس ، ف. (2015). دراسة المواقع الوظيفية والخيفية في العائلات البروتينية الفائقة. أكتا ناتوراي ، 7 (4) ، 34-45.</li>
	<li>بيليلي ، أ. وكاري ، ج. (2017). البروتينات ذات مواقع bindin المتعددة. في ربط الترابط القابل للانعكاس (محرران أ. بيليلي وجي كاري). دوي: 10.1002 / 9781119238508.ch4</li>
	<li>هيلمستادت ، ك. ، كرابمان ، إس ، وبروس ، جي إتش (2001). التنظيم الخيفي للنشاط التحفيزي: الإشريكية القولونية أسبارتات ترانسكاربامولاز مقابل الخميرة المشيمية الطفرة. مراجعات علم الأحياء الدقيقة والبيولوجيا الجزيئية: MMBR ، 65 (3) ، 404-421. دوي: 10.1128 / MMBR.65.3.404-421.2001</li>
</ol>

ربط الترابط والربط

<div style="direction: rtl;">

تحتوي البروتينات الألوستيرية على أكثر من موقع ربط للربيطة؛ يؤثر ربط الروابط بأي من هذه المواقع على ربط الروابط بالمواقع الأخرى. عندما يكون البروتين لوستيريًا، تسمى مواقع الارتباط الخاصة به مقترنة أو مرتبطة. في حالة الإنزيمات، يُعرف الموقع الذي يرتبط بالركيزة بالموقع النشط ويعرف الموقع الآخر بالموقع التنظيمي. عندما ترتبط الربيطة بالموقع التنظيمي، يؤدي ذلك إلى تغييرات تكوينية في البروتين يمكن أن تؤثر على الموقع النشط للبروتين.

يمكن أن تتسبب روابط الموقع الملزمة في تنظيم إيجابي أو سلبي لربط الروابط بالمواقع الأخرى. في الحالات التي يفضل فيها كلا الرابطين الارتباط بنفس الشكل للبروتين، فإن الارتباط في موقع واحد يزيد من تقارب الموقع الآخر للرابط الخاص به. ويُعرف هذا بالارتباط الإيجابي. من ناحية أخرى، إذا كانت الربيطات تفضل الارتباط بتشكيلات مختلفة، فإن ربط ربيطة واحدة سيجعل من الصعب على الربيطة الثانية الارتباط بالبروتين. ويعرف هذا بالارتباط السلبي.

</div>

تحتوي البروتينات الخيفية على أكثر من موقع ربط ترابط. يؤثر ارتباط الترابط بأي من هذه المواقع على ارتباط الروابط بالآخر ...

Education

JoVE Core

Cell Biology

بيولوجيا الخلية

Unit 1

الوحدة الأولى

Energy and Catalysis

الطاقة والتحفيز

KEY TERMS AND CONCEPTS

المصطلحات والمفاهيم الأساسية

ligand binding and allosteric effects

Ligand binding and linkage describe how one molecule can affect another when it binds to a protein. In this topic, the focus is on how binding at one site can influence activity at a different site on the same protein.

This idea is important for understanding protein function in high school biology. It helps explain why some proteins respond more strongly after a ligand attaches. The transcript centers on the connection between ligand binding and linkage, which is a key concept in molecular interactions.

The term ligand means a molecule that binds to a protein. Linkage describes the way that this binding is connected to changes elsewhere in the protein. Together, these ideas show how protein behavior can be controlled by molecular binding events.

Ligand Binding and Allosteric Effects

the first law of thermodynamics

Energy Changes in Cells and Matter

The first law of thermodynamics describes how energy changes form in the universe. The total amount of energy stays constant. Energy can move from one place to another or change into a different form, but it cannot be created or destroyed. These energy changes happen in everyday life. A light bulb changes electrical energy into light energy. A gas stove changes chemical energy in natural gas into heat energy. Plants also carry out a major energy transformation when they convert sunlight energy...

the second law of thermodynamics

Entropy and Spontaneous Change

Entropy helps predict whether a process will happen on its own. Entropy is a measure of randomness or disorder in a system. High entropy means high disorder and low energy. A student’s bedroom is a simple example. If no work is done, the room becomes messy over time. That messy state is highly disordered and has high entropy. To make the room clean again, energy must be added as the student puts things away. That organized state has low entropy. Processes that increase the entropy of the...

enthalpy within the cell

Cellular Enthalpy and Energy Changes

Cellular enthalpy describes how heat and energy change during chemical and physical processes. Enthalpy is written as H and is defined as the sum of a system’s internal energy, U, and the product of pressure and volume, PV. It is a state function, which means its value depends on the state of the system, not the path taken. Scientists cannot measure the enthalpy of a single substance directly. They can determine enthalpy changes, or ΔH, for a process instead. For reactions or changes that...

entropy within the cell

Cell Energy Loss and Entropy

Cell energy loss and entropy explain why living things need constant energy input. Cells obtain energy, transform it, and use it to do work, but these transfers are never completely efficient. In each transfer, some energy is lost in a form that cannot be used. In many cases, that lost energy is heat energy.

an introduction to free energy

Gibbs Free Energy and Reaction Work

Gibbs free energy describes the usable energy in a chemical reaction. It helps scientists compare how much energy different reactions release. This measurement is called Gibbs free energy, or G, after Josiah Willard Gibbs. The second law of thermodynamics explains why not all energy stays available for work. Some energy is lost in an unusable form, such as heat, and this loss increases entropy. Gibbs free energy is the energy left after that entropy loss is taken into account. Every chemical...

endergonic and exergonic reactions in the cell

endergonic-and-exergonic-reactions-in-the-cell

Cell Reactions That Release or Store Energy

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the equilibrium binding constant and binding strength

the-equilibrium-binding-constant-and-binding-strength

How Equilibrium Binding Constant Affects Binding

The equilibrium binding constant describes how strongly two molecules bind at equilibrium. It is a useful way to compare binding strength in molecular interactions. This topic focuses on how binding is measured and what the equilibrium binding constant means. A higher value indicates stronger binding, while a lower value indicates weaker binding. Understanding this constant helps explain how tightly molecules stay together under equilibrium conditions. The page also connects the binding...

free energy and equilibrium

Free Energy and Reaction Direction

Free energy and reaction direction are linked in chemical equilibrium. A free energy change, ΔG, shows the driving force for a process. When ΔG is negative, the process is driven forward. When ΔG is positive, the reverse direction is favored. When ΔG is zero, the forward and reverse driving forces are equal, and the system is at equilibrium. The reaction quotient, Q, helps show how close a system is to equilibrium. Q is the numerical value of the mass action expression for the system. It can...

non-equilibrium in the cell

Cells Stay Out of Equilibrium

Cells stay out of chemical equilibrium by constantly using energy and moving materials in and out. Chemical reactions in metabolism are often reversible. They can go in both directions. In one direction, they release energy to the surroundings. In the reverse direction, they absorb energy. The same idea applies to reactions that build and break down cell molecules. Proteins, for example, can be broken into individual amino acids, and amino acids can be used to build proteins again. In a closed...

oxidation and reduction of organic molecules

oxidation-and-reduction-of-organic-molecules

Electron Carriers in Cell Energy Transfer

Cell energy production depends on redox reactions, which are oxidation and reduction reactions that happen together. In oxidation, an electron is removed from an atom in a compound. In reduction, that same electron is added to another compound. Because these reactions usually occur as a pair, they are called redox reactions. When a molecule loses an electron, its potential energy goes down. The electron does not stay free in the cytoplasm. Instead, it moves to a second compound and reduces...

introduction to enzymes

Enzyme Function, Cofactors, and Inhibitors

Enzymes are proteins that speed up biochemical reactions without being used up. Humans have used enzymes since about 7000 BCE, when they fermented sugars to make alcohol without knowing the reaction was enzyme-catalyzed. The word enzyme was coined by Wilhelm Kuhne in 1877. It comes from the Greek words en, meaning “in” or “within,” and zyme, meaning “yeast.” Enzymes work through active sites, which are regions that bind substrates and help convert them into products. Many enzymes also have...

enzymes and activation energy

How Enzymes Lower Reaction Energy

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Graphing Enzyme Kinetics Data

Enzyme kinetics uses graphs to show how fast a biochemical reaction happens. Scientists measure the initial reaction rate, or velocity (Vo), at different substrate concentrations ([S]). They may also run trials with inhibitors or other molecules that change the reaction rate. The results are often plotted as Vo against [S]. For many single-substrate reactions, the data fits the Michaelis-Menten equation. This equation, named after Leonor Michaelis and Maud Menten, helps estimate the maximum...

turnover number and catalytic efficiency

How Fast Enzymes Work in Digestion

Enzymes can work at very different speeds, and their turnover number shows how fast they convert substrate molecules into products. Turnover number is the maximum number of substrate molecules an enzyme can transform per unit time. For most enzymes, this value is between 1 and 1000 molecules per second. Some enzymes are especially fast. Catalase has the highest known turnover number and can convert up to 2.8×10^6 molecules of hydrogen peroxide into water and oxygen each second. Lysozyme has...

catalytically perfect enzymes

Diffusion-Controlled Enzymes and Reaction Speed

Catalytically perfect enzymes are enzymes that speed up biochemical reactions at very high rates. The idea was first proposed by W. J. Albery and J. R. Knowles in 1976. These enzymes have catalytic efficiency values of about 10^8 to 10^9 M^-1 s^-1 and are also called diffusion-controlled enzymes because diffusion of the substrate into the active site is the only rate-limiting step. Examples of catalytically perfect enzymes include triose phosphate isomerase, fumarase, and superoxide dismutase.

introduction to mechanisms of enzyme catalysis

introduction-to-mechanisms-of-enzyme-catalysis

How Enzymes Change Shape to Catalyze

Enzyme catalysis depends on how enzymes bind substrates and how the active site responds during the reaction. Scientists once described this process with a simple lock-and-key model, where the enzyme and substrate fit together in one instant. Research now supports induced fit, a more dynamic model in which binding causes a small change in the enzyme’s shape. That shift helps create an ideal match between the enzyme and the substrate’s transition state, which improves catalysis. The active site...

ligand binding and linkage

Ligand binding and linkage describe how one molecule can affect another when it binds to a protein. In this topic, the focus is on how binding at one site can influence activity at a different site on the same protein. This idea is important for understanding protein function in high school biology. It helps explain why some proteins respond more strongly after a ligand attaches. The transcript centers on the connection between ligand binding and linkage, which is a key concept in molecular...

cooperative allosteric transitions

How Proteins Shift Shape Together

Proteins can change shape in a coordinated way during allosteric transitions. In a cooperative transition, one part of the protein affects another part, so the change spreads through the molecule. These shape changes help proteins switch between different states. The shift can influence how the protein works and how it responds to other molecules. Cooperative allosteric transitions are an important idea in protein function. They explain how a small change at one site can lead to a larger...

ribozymes

Catalytic RNA: Ribozymes in Action

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atp energy storage and release

ATP Powers Cellular Transport and Reactions

ATP powers cellular transport and many reactions by transferring energy through phosphorylation. ATP is a highly unstable molecule. If it is not used quickly, it breaks down into ADP and inorganic phosphate, and the released energy is lost as heat. Cells use ATP through energy coupling. This means the exergonic reaction of ATP hydrolysis is linked to an endergonic reaction so the reaction can move forward. One major example is the sodium-potassium pump, a transmembrane ion pump that is vital...

atp and macromolecule synthesis

ATP in Building Cell Macromolecules

ATP helps cells build biological macromolecules. These organic compounds are mainly made of carbon atoms bonded to hydrogen, oxygen, nitrogen, and small amounts of other elements. The four major classes of biological macromolecules are carbohydrates, lipids, proteins, and nucleic acids. Most macromolecules start as small subunits called monomers. Cells join monomers with covalent bonds to make larger molecules called polymers. This building process needs energy, so cells depend on ATP, the...

coupled reactions

ATP Powers Cellular Work

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key terms and concepts

Learn how ligand binding can change protein activity through linkage, where binding at one site affects another site on the same protein.

Ligand Binding and Allosteric Effects | JoVE K12

cell biology

JoVE Core Cell Biology illustrates complex cellular processes in easy-to-understand yet comprehensive animated video lessons. This collection focuses on the essential components and functions of cells, including organelles and membranes, cellular transport, and cell energetics. It is complemented by scientist-in-action videos that demonstrate the application of cell biology in real-world research experiments.

Virginia  Standards of Learning

HIgh School

BIO.2

BIO.2.c

Florida Department of Education

High School

Life Science

SC.912.L.18

SC.912.L.18.4

SC.912.L.18.11

Texas Essential Knowledge and Skills

BIO.11

BIO.11.B

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Macromolecules

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Nucleic Acid Structure

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ATP Energy Storage and Release

ATP and Macromolecule Synthesis

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Construct an explanation to illustrate relationships between structure and function of major macromolecules essential for life.

LS.Bio.1.1

Introduction to Enzymes

The use of enzymes by humans dates to 7000 BCE. Humans first used enzymes to ferment sugars and produce alcohol without knowing that this was an ...

Enzymes and Activation Energy

The activation energy (or free energy of activation), abbreviated as Ea, is the small amount of energy input necessary for all chemical reactions to ...

Introduction to Enzyme Kinetics

Enzyme kinetics studies the rates of biochemical reactions. Scientists monitor the reaction rates for a particular enzymatic reaction at various substrate ...

Turnover Number and Catalytic Efficiency

The turnover number of an enzyme is the maximum number of substrate molecules it can transform per unit time. Turnover numbers for most enzymes range from ...

Catalytically Perfect Enzymes

The theory of catalytically perfect enzymes was first proposed by W.J. Albery and J. R. Knowles in 1976. These enzymes catalyze biochemical reactions at ...

Introduction to Mechanisms of Enzyme Catalysis

For many years, scientists thought that enzyme-substrate binding took place in a simple &#34;lock-and-key&#34; fashion. This model stated that the enzyme ...

Cooperative Allosteric Transitions

Ribozymes

Carry out investigations to illustrate how enzymes act as catalysts for biochemical reactions and how environmental factors affect enzyme activity.

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Prokaryotic Cells

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Cytoplasm

The cytoplasm consists of organelles and a framework of protein scaffolds called the cytoskeleton suspended in an aqueous solution, the cytosol. The ...

The Nucleus

The nucleus is a membrane-bound organelle that acts as a control center in a eukaryotic cell. It contains chromosomal DNA, which controls gene expression ...

Endoplasmic Reticulum

Endoplasmic ReticulumThe endoplasmic reticulum (ER) is an extensive network of membranous sacs and tubules in eukaryotic cells, continuous with the outer ...

Ribosomes

Ribosomes translate genetic information encoded by messenger RNA (mRNA) into proteins. Both prokaryotic and eukaryotic cells have ribosomes. Cells that ...

Golgi Apparatus

As they leave the Endoplasmic Reticulum (ER), properly folded and assembled proteins are selectively packaged into vesicles. These vesicles are ...

Lysosomes

Lysosomes are membrane-enclosed spherical sacs derived from the Golgi apparatus. The most important function of the lysosome is degrading macromolecules ...

Peroxisomes

Peroxisomes and mitochondria are two important oxygen-utilizing organelles in eukaryotic cells. Mitochondria carry out cellular respiration&#x2014;the ...

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Introduction to Actin

Actin is a highly conserved cytoskeletal protein found abundantly in eukaryotic cells. It constitutes 10% weight of the total cellular protein in muscle ...

Cell Structure

Background
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overview-of-myosin-structure-and-function

Overview of Myosin Structure and Function

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ExpandImmediately before the experiment, wash and peel onion bulbs for the class.
Remove the entire brown outer skin and ...

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Use models to explain how the structure of organelles determines its function and supports overall cell processes.

LS.Bio.1.3

Analyze how the relationship between structure and function supports life processes within organisms.

Ligand Binding and Allosteric Effects

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