Name: protein mapping with 2d gel electrophoresis
Uploaded: 2023-04-30T06:31:06.000Z
Duration: 7 min 31 s
Channel: JoVE

K12 Standards

new-york-state-science-learning-standards

New York State Science Learning Standards

High School

Physical Science

HS. Structure and Properties of Matter

HS-PS1-10.

Two-Dimensional Gel Electrophoresis

二次元ゲル電気泳動

二次元ゲル電気泳動法 (2DGE) は、生体分子の混合物からの何千もの問題を解決できる手法です。この技法が一緒に結合されている 2 つの明瞭な分離法: 等電集中 (IEF) とナトリウム dodecyl 硫酸ポリアクリルアミドゲル電気泳動 (SDS-PAGE)。これは物理的に彼らの等電点 (電気化学的特性) と、分子量でゲルの 2 つの軸にまたがる化合物を分離します。
このビデオでは手順は、2DGE と複雑なタンパク質溶液の組成を特徴付けるための一般的な手順の主な概念を説明します。病気の発生と進展、治療、次の翻訳後修飾 (PTM) 蛋白質の調査の監視のためのバイオ マーカー検出を含むアプリケーションのセクションでこの技術の 3 つの例のとおりです。
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2 次元、または 2 D、ゲル電気泳動法は単一の混合物からたくさんの蛋白質を分離する 2 つの異なる分離法を用いる。1 つの技術の SDS-PAGE やナトリウム dodecyl 硫酸ポリアクリルアミドゲル電気泳動は完全に複雑な混合物だけを切り離すことはできません。第 2 ゲルの電気泳動に 2 番目メソッド、等電点焦点またはライセート セル可能性がありますすべての蛋白質の解決を可能にする分離は、等電点に基づく、IEF SDS ページのカップルします。このビデオは、2 D の原則のゲルの電気泳動、一般的な手順といくつかの生物医学応用の表示されます。
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<div class="chapter_text" id="script_1">
第 2 ゲルの電気泳動は、最初の次元として IEF で始まります。すべての蛋白質は、等電点または pI、純充満がゼロと呼ばれる pH 値を持ちます。タンパク質は電界に服従する、反対の電荷を持つ電極に向かって移動します。興味のサンプルは、ampholytes、酸性および基本的なグループを含んでいる分子が埋め込まれているストリップ固定化 pH 勾配または IPG に読み込まれます。電界がネット、その電荷を失う彼らの pI を一致する pH 値に到達するまで移行するタンパク質の原因 pH 勾配のストリップに適用されます。
2 番目の次元を実行、する前に埋め込まれた蛋白質は sds のそれらの変化と均一否定的な充電を提供して扱われます。完了すると、IPG ストリップ、ポリアクリルアミド ゲル上に配置されます。適用された電界は大きい蛋白質のゲルを通ってもっとゆっくり移動と陽極に向かって蛋白質を描画します。
蛋白質の混合物は、pI と分子量に従って分離されている、一度汚れを用いてプロテオーム マップを可視化、興味の蛋白質が識別されます。
第 2 ゲルの電気泳動の原理について説明した、代表的な検査法に行きましょう。
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<div class="chapter_text" id="script_2">
実験を実行する前に、蛋白質はメディアに可溶化する必要があります。サンプルの可溶化脱水素結合相互作用、タンパク質の電荷、ジスルフィド結合を破るに還元剤の変更を防ぐために非イオン性洗剤を混乱させるためカオトロ ピック剤の組み合わせでタンパク質を集約することによって達成され、バッファーします。遠心分離、および結果として得られるペレット; のコレクションによって、干渉の豊富なタンパク質や他の分子を削除するには、材料を順番に抽出します。エンドヌクレアーゼに実験を妨げる DNA を使用する酵素処理後。
タンパク質を可溶化されている、一度 IPG ストリップがストリップのクリーニング液と洗浄によって調製し、乾燥する逆さまのまま。各ストリップ ストリップ ホルダー番号を割り当てられます。一度準備ができて、細胞のエキスがプラスの末尾に負からゆっくりと、スライド モーションのストリップ上に読み込まれます。電極上に、ゲルのストリップの下に湿気のあぶらとり紙を配置水分補給の目的IPG ストリップし、IEF 楽器の上に並んでいます。高電流を適用し、タンパク質が移行し始めます。
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<div class="chapter_text" id="script_3">
最初の次元が完了した後、SDS ページのゲルは、鋳造装置で用意しています。IPG のストリップは、SDS 含んでいる平衡バッファーにダウン顔を置くことによって扱われます。電気泳動装置、電気泳動バッファーの追加準備します。治療の IPG ストリップは、ピンセット、ゲル板の上に置かれ、agarose シール ソリューションで封を使用して収集されます。電圧源は、電界、最速の移動蛋白質はゲルの底から 1 cm まで保持されますを適用します。
電気泳動の終了後、タンパク質を視覚化する必要があります。従来この Coomassie 青いや銀の硝酸塩との汚損によって実行されます。興味の蛋白質はゲルから転送、西部のしみの分析を行ったことがあります。
2 番目の識別方法には、質量分析法で分析するよりも、それらを消化、ゲルからタンパク質の切除が含まれます。
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<div class="chapter_text" id="script_4">
今では我々 は、手順を確認したところ、第 2 ゲルの電気泳動の使用方法のいくつかを見てみましょう。
この手法の最も一般的な用途の 1 つは病気の開始そして進行に関与する分子の同定です。質量分析とつながれる第 2 ゲルの電気泳動は、健康なものと比較して病変部の特定の蛋白質のアップまたはダウン規制を検出できます。
さらに、第 2 ゲルの電気泳動は、次の潜在的な薬物治療に対する患者の反応の進行に便利です。供試体は、様々 な縦長の治療投与の患者から取られるかもしれない。この方法で西部のしみまたは質量分析と相まって第 2 ゲルの電気泳動することができます炎症; などの否定的な反応に関連付けられているタンパク質を検出または緩和状態で蛋白質の不在。
第 2 ゲルの電気泳動の別の用途は、次の翻訳の mRNA から蛋白質への追加は、タンパク質の構造と機能、翻訳後修飾や PTM の研究です。PTM のさまざまなタンパク質シグナル伝達、遺伝子発現を含む機能を調節するなったり、酸化的損傷があります。第 2 ゲルの電気泳動は、メチル化やアセチル化、pI として分子量の変化を引き起こすことができるなどの変更に敏感です。
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<div class="chapter_text" id="script_5">
第 2 ゲルの電気泳動のゼウスのビデオを見てきただけ。このビデオは、テクニック、典型的な実験、生物医学分野への応用のいくつかの原則を説明します。
見てくれてありがとう!
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Two-dimensional gel electrophoresis (2DGE) is a technique that can resolve thousands of biomolecules from a mixture. This technique involves two distinct ...

二次元ゲル電気泳動(2D)は、1つの混合物から数千のタンパク質を分離できる2つの異なる分離方法を利用する技術です。その技術の一つであるSDS-PAGEまたはドデシル硫酸ナトリウムポリアクリルアミドゲル電気泳動は、複雑な混合物を単独で完全に分離することはできません。2Dゲル電気泳動は、SDS-PAGEを等電点に基づいて分離する第2の方法である等電点泳動またはIEFに結合し、細胞溶解物中の潜在的にすべてのタンパク質の分離を可能にします。このビデオでは、2Dゲル電気泳動の原理、一般的な手順、およびその生物医学的応用の一部を紹介します。2Dゲル電気泳動は、IEFを1次元として始まります。すべてのタンパク質には、等電点またはpIと呼ばれるpH値があり、正味電荷はゼロです。タンパク質が電界にさらされると、タンパク質は反対の電荷で電極に向かって移動します。目的のサンプルは、酸性基と塩基性基の両方を含む分子である両性電解質が埋め込まれた固定化pHグラジエント(IPG)ストリップにロードされます。次に、電界がpHグラジエントストリップに印加され、タンパク質がpIに一致するpH値に達するまで移動し、そこで正味電荷を失います。2次元を実行する前に、埋め込まれたタンパク質をSDSで処理し、変性させて均一な負電荷を提供します。完成したら、IPGストリップをポリアクリルアミドゲル上に置きます。印加された電場はタンパク質をアノードに引き寄せ、より大きなタンパク質はゲル内をよりゆっくりと移動します。タンパク質混合物をpIと分子量に従って分離すると、染色剤を使用してプロテオームマップを視覚化し、目的のタンパク質を同定します。さて、2Dゲル電気泳動の原理について説明したので、一般的な実験室の手順を見ていきましょう。実験を行う前に、タンパク質を培地に可溶化する必要があります。サンプルの可溶化は、水素結合相互作用を破壊するカオトロピック剤、タンパク質の電荷の変化を防ぐ非イオン性界面活性剤、ジスルフィド結合を切断する還元剤、およびバッファーを組み合わせてタンパク質を解凝集することによって達成されます。干渉する豊富なタンパク質や他の分子を除去するために、材料を遠心分離によって順次抽出し、得られたペレットを回収します。続いて、実験を妨げる任意のDNAを消費するために使用される酵素であるエンドヌクレアーゼによる治療が行われます。タンパク質が可溶化されたら、ストリップクリーニング溶液ですすぎ、逆さまにして乾燥させてIPGストリップを調製します。その後、各ストリップにはストリップホルダー番号が割り当てられます。準備が整うと、細胞抽出物は、ネガティブエンドからポジティブエンドへのゆっくりとしたスライド運動でストリップにロードされます。水分補給の目的で、湿ったあぶらとり紙を電極の上とゲルストリップの下に置きます。次に、IPGストリップをIEF機器に並べます。高電流が印加され、タンパク質が移動し始めます。1次元目が完成したら、キャスティング装置でSDS-PAGE用ゲルを調製します。IPGストリップは、SDS含有平衡化バッファーに伏せて置くことで処理されます。電気泳動ユニットは、電気泳動バッファーを追加することで準備されます。処理したIPGストリップをピンセットで採取し、ゲルプレートの上に置き、アガロースシール液で密封します。次に、電圧源が電界を印加し、最も速く移動するタンパク質がゲルの底から1cmになるまで電界を保持します。電気泳動の完了後、タンパク質を可視化する必要があります。伝統的に、これはクマシーブルーまたは硝酸銀で染色することによって行われます。目的のタンパク質をゲルから移し、ウェスタンブロット分析で分析できます。2つ目の同定アプローチは、質量分析による分析よりも、ゲルからタンパク質を取り出して消化する方法です。手順を確認したので、2Dゲル電気泳動の用途をいくつか見てみましょう。この手法の最も一般的な用途の1つは、疾患の発症と進行に関与する分子の同定です。2Dゲル電気泳動は、質量分析と組み合わせることで、健康な領域と比較して、疾患領域の特定のタンパク質のアップレギュレーションまたはダウンレギュレーションを検出できます。さらに、2Dゲル電気泳動は、潜在的な治療薬に対する患者の反応の進行を追跡するのに役立ちます。検体は、治療の投与後、さまざまな時点で患者から採取できます。.このように、ウェスタンブロットまたは質量分析と組み合わせた2Dゲル電気泳動は、炎症などの負性応答に関連するタンパク質を検出することができます。または緩和された状態のタンパク質の欠如。2Dゲル電気泳動の別の用途は、翻訳後修飾後のタンパク質の構造と機能の研究、またはmRNAからの翻訳後のタンパク質への付加であるPTMの研究です。PTMは、タンパク質シグナル伝達、遺伝子発現など、さまざまな機能を調節したり、酸化的損傷を引き起こしたりする可能性があります。2Dゲル電気泳動は、メチル化やアセチル化などの修飾に敏感であり、pIや分子量の変化を引き起こす可能性があります。JoVEの2Dゲル電気泳動に関するビデオをご覧になりました。このビデオでは、この技術の原理、典型的な実験手順、および生物医学の分野でのいくつかの応用について説明しました。ご覧いただきありがとうございます!

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protein mapping with 2d gel electrophoresis

Protein mapping with 2D gel electrophoresis separates complex protein mixtures across two steps. The method combines isoelectric focusing, or IEF, with sodium dodecyl sulfate polyacrylamide gel electrophoresis, or SDS-PAGE. Together, these methods can resolve thousands of biomolecules from a single sample by their isoelectric point and molecular weight.

The first dimension is IEF. Each protein has an isoelectric point, or pI, which is the pH where its net charge is zero. Proteins are loaded onto immobilized pH gradient, or IPG, strips that contain ampholytes, which are molecules with both acidic and basic groups. When an electric field is applied, the proteins move until they reach the pH that matches their pI. At that point, they stop moving because they no longer have a net charge.

Before the second dimension, the proteins are treated with SDS. This step denatures the proteins and gives them a uniform negative charge. The IPG strips are then placed on a polyacrylamide gel for SDS-PAGE. When the electric field is applied, proteins move toward the anode, and larger proteins move more slowly through the gel.

A typical lab workflow begins by solubilizing the protein sample. This is done with chaotropic agents, nonionic detergents, reducing agents, and buffers. The sample is then cleaned by sequential centrifugation and pellet collection, and endonuclease is used to remove DNA that could interfere with the experiment. IPG strips are rinsed, dried, numbered, and loaded with the extract in a slow motion from the negative end to the positive end. Damp blotting paper helps with rehydration before the strips are run on the IEF instrument.

After the first run, the SDS-PAGE gel is prepared in a casting apparatus. The IPG strips are placed face down in SDS-containing equilibration buffer, and then positioned on the gel plates with agarose-sealing solution. Electrophoresis continues until the fastest-moving proteins are about 1 cm from the bottom of the gel. The separated proteins are then visualized with stains such as Coomassie blue or silver nitrate. Proteins of interest can also be transferred for Western blot analysis or excised, digested, and identified by mass spectrometry.

2D gel electrophoresis is widely used in biomedicine. It can help identify proteins involved in disease initiation and progression by comparing diseased and healthy samples. It is also useful for tracking how patients respond to a potential therapeutic drug over time. Another application is the study of posttranslational modifications, or PTMs, which are changes made to proteins after translation from mRNA. Methylation and acetylation can shift both pI and molecular weight, making them detectable with this method.

Protein Mapping with 2D Gel Electrophoresis

protein-mapping-with-2d-gel-electrophoresis

dialysis: diffusion based separation

Dialysis for Buffer Exchange in Biochemistry

Dialysis is a common biochemistry technique for buffer exchange and desalting. It separates molecules by diffusion through a semipermeable membrane, which lets small molecules pass while holding larger biomolecules inside the sample. The membrane is the key part of the setup. Its pores create a molecular weight cutoff, so a membrane such as a 10 kDa membrane usually keeps molecules larger than 10 kilodaltons inside. This cutoff is not exact, because membranes have a range of pore sizes.

enzyme assays and kinetics

Measuring Enzyme Reaction Rates

Enzyme reaction rates can be measured with assays that track how substrate or product levels change over time. Enzymes are proteins, or sometimes RNAs, that speed up chemical reactions by lowering the activation energy needed to start them. They act on a specific substrate and help form a product that supports life processes. Enzymatic reactions are often described in three steps. First, the substrate binds to the enzyme active site and forms an enzyme-substrate complex. That complex can fall...

maldi-tof mass spectrometry

How MALDI-TOF Reads Biomolecules

MALDI-TOF mass spectrometry reads biomolecules by using a laser, a matrix, and a time-of-flight analyzer. MALDI, or matrix-assisted laser desorption ionization, helps fragile molecules keep their structure while they are moved into the mass analyzer. The analyzer then separates compounds based on size and charge. In MALDI, the sample is mixed into a matrix, usually an organic compound with aromatic and conjugated double bonds. A laser pulse strikes the spot, and the matrix absorbs most of the...

tandem mass spectrometry

Tandem Mass Spectrometry for Biomolecule Analysis

Tandem mass spectrometry is used to isolate a biomolecule and break it into smaller pieces so its makeup can be studied. Because biomolecules often have large, complex structures, it can be hard to identify their molecular composition and sequence from a single measurement. By linking mass spectrometers in series, the technique first selects one ion and then analyzes the fragments it produces. The process starts with an ion source that converts the sample into ions. A mass analyzer then...

protein crystallization

Protein Crystals for Structure Analysis

Protein crystals help scientists study protein structure and function. A crystal is a solid lattice made from purified protein molecules. These crystals are useful in structural biology because they reveal details that methods like mass spectrometry and SDS-PAGE cannot show on their own. Protein crystallization is paired with recombinant protein expression and x-ray diffraction to support this work. The process starts with a large amount of very pure protein. Researchers often make that...

chromatography-based biomolecule purification methods

chromatography-based-biomolecule-purification-methods

Protein Purification with SEC and IMAC

Protein purification with size-exclusion chromatography and affinity chromatography helps isolate biomolecules from complex mixtures. These methods are common in biochemistry because purified samples are needed before a biomolecule’s properties and activity can be studied. The video focuses on the principles behind size-exclusion chromatography, affinity chromatography, and immobilized metal affinity chromatography, or IMAC. Size-exclusion chromatography, or SEC, separates molecules by size. A...

two-dimensional gel electrophoresis

Protein mapping with 2D gel electrophoresis separates complex protein mixtures across two steps. The method combines isoelectric focusing, or IEF, with sodium dodecyl sulfate polyacrylamide gel electrophoresis, or SDS-PAGE. Together, these methods can resolve thousands of biomolecules from a single sample by their isoelectric point and molecular weight. The first dimension is IEF. Each protein has an isoelectric point, or pI, which is the pH where its net charge is zero. Proteins are loaded...

metabolic labeling

Tracking Cell Chemistry with Metabolic Labels

Metabolic labeling tracks cell chemistry by using chemical analogs that cells take up and build into biomolecules. These labels help scientists follow biochemical changes and modifications inside cells. The labeled products can then be studied with tools such as SDS-PAGE and NMR to learn more about metabolic pathways. Several labeling strategies are shown here. Isotopic labeling uses analogs that match the natural molecule but contain uncommon isotopes, such as carbon-13 and nitrogen-15 in an...

electrophoretic mobility shift assay (emsa)

electrophoretic-mobility-shift-assay-emsa

Detecting Protein-DNA Binding by EMSA

Electrophoretic mobility shift assay, or EMSA, is a biochemical method used to detect binding between proteins and nucleic acids. It is also called a gel shift assay. The test compares how a labeled nucleic acid moves through a gel before and after it binds a protein. EMSA is used to see whether a specific protein binds to a specific nucleic acid. First, the nucleic acid is labeled to make a probe. The transcript describes radioactive phosphorus-32 as a common label. The probe is then mixed...

photometric protein determination

Measuring Protein Concentration with Absorbance

Measuring protein concentration with absorbance is a key step in many biochemical assays. Photometric methods use the fact that samples with more light-absorbing material transmit less light. Because concentration and absorption are directly related, this makes it possible to measure an unknown sample. The core idea comes from the Beer-Lambert Law. This law states that the concentration of a light-absorbing species is proportional to its absorbance. The video also introduces the Bradford assay...

density gradient ultracentrifugation

Sucrose Gradient Separation in an Ultracentrifuge

Sucrose gradient separation in an ultracentrifuge is a lab method for isolating cell parts and biomolecules. It uses differences in density to make particles sink or rise in a liquid. A high-speed ultracentrifuge speeds up this process so components can be separated without destroying them. The basic idea starts with a suspension, which is particles mixed in a liquid solvent. Particles that are denser than the solvent sediment, while less dense particles float. A rotor inside the...

co-immunoprecipitation and pull-down assays

co-immunoprecipitation-and-pull-down-assays

Protein Interaction Capture Methods in Cells

Co-immunoprecipitation and pull-down assays are laboratory methods used to capture stable protein-protein interactions. Protein-protein interactions help control many biological functions, but many of them have not yet been identified. These assays are related to immunoprecipitation, which isolates a target protein from a mixed sample using an antibody. In co-immunoprecipitation, or CoIP, an antibody binds the target protein, and that protein is already attached to another protein that the...

reconstitution of membrane proteins

Membrane Proteins in Liposome Models

Membrane proteins can be moved into liposome models so their function can be studied outside a cell. Reconstitution means restoring an isolated biomolecule to a working form. For membrane proteins, that usually means placing a purified protein into an artificial lipid membrane. Cell membranes are made mainly of phospholipids and membrane proteins. The phospholipids form a bilayer with hydrophilic phosphate heads facing water and hydrophobic fatty acid tails facing inward. Some membrane...

f&#246;rster resonance energy transfer (fret)

FRET as a Molecular Ruler in Cells

Föster resonance energy transfer, or FRET, is a way to study close-range biochemical interactions using light-emitting molecules. A donor fluorophore can pass energy to an acceptor fluorophore when their emission and absorption spectra overlap. This transfer happens only when the pair is very close together, usually within 10 nm. Because FRET depends on distance, it is often called a molecular or spectroscopic ruler. The strength of the signal is measured as FRET efficiency, which describes...

surface plasmon resonance (spr)

SPR Biosensors for Tracking Binding Kinetics

Surface plasmon resonance, or SPR, is a way to track biomolecular binding on a label-free biosensor. It is used to measure molecular affinity, kinetics, specificity, and concentration. The method works with a thin metal layer on a prism, where changes in reflected light reveal interactions in real time. SPR sensors use a thin layer of a noble metal on the face of a prism. Light is reflected from the prism-metal interface into a photodetector. At one specific angle, called the surface plasmon...

biochemistry

このコレクションでは、親和性クロマトグラフィーなどの一般的に使用される精製方法や、MALDI-TOFなどの分析方法について紹介します。さらに、共同免疫沈降法や代謝標識法など、生体分子の相互作用や機能を評価する方法も紹介します。

See how 2D gel electrophoresis separates proteins by pI and size, then use staining, Western blot, or mass spectrometry to identify biomarkers and PTMs.

Protein Mapping with 2D Gel Electrophoresis | JoVE K12

HS. Chemical Reactions

HS-PS1-11.

Life Science

Structure and Function

HS-LS1-1.

matter-and-energy-in-organisms-and-ecosystems

Matter and Energy in Organisms and Ecosystems

HS-LS1-6.

Inheritance and Variation of Traits

HS-LS3-1.

Overview

Principles of 2D Gel Electrophoresis

Sample Preparation and Running Isoelectric Focusing

Running SDS-PAGE and Visualization/Analysis

Applications

Summary

Periodic Classification of the Elements

The periodic table arranges atoms based on increasing atomic number so that elements with the same chemical properties recur periodically. When their ...

atomic-radii-and-effective-nuclear-charge

Atomic Radii and Effective Nuclear Charge

The elements in groups of the periodic table exhibit similar chemical behavior. This similarity occurs because the members of a group have the same number ...

Ionic Radii

Ionic radius is the measure used to describe the size of an ion. A cation always has fewer electrons and the same number of protons as the parent atom; it ...

Ionization Energy

The amount of energy required to remove the most loosely bound electron from a gaseous atom in its ground state is called its first ionization energy ...

Electron Affinity

The electron affinity (EA) is the energy change for adding an electron to a gaseous atom to form an anion (negative ion).



This process can be either ...

Electron Orbital Model

Orbitals are the areas outside of the atomic nucleus where electrons are most likely to reside. They are characterized by different energy levels, shapes, ...

The Aufbau Principle and Hund's Rule

To determine the electron configuration for any particular atom, we can build the structures in the order of atomic numbers. Beginning with hydrogen, and ...

Coordination Chemistry Complexes

Source: Laboratory of Dr. Neal Abrams &#8212; SUNY College of Environmental Science and Forestry
Transition metals are found everywhere from vitamin ...

Use the periodic table as a model to predict the relative properties of elements based on the patterns of electrons in the outermost energy level of atoms.

HS-PS1-1.

Types of Chemical Bonds

Chemical bonding theories were pioneered by American chemist Gilbert&#xA0;N. Lewis. He developed a model called the Lewis model to explain the type and ...

Lewis Symbols and the Octet Rule

Chemical bonds are complex interactions between two or more atoms or ions, which reduce the potential energy of the molecule. Gilbert N. Lewis developed a ...

Ionic Bonding and Electron Transfer

Ions are atoms or molecules bearing an electrical charge. A cation (a positive ion) forms when a neutral atom loses one or more electrons from its valence ...

The Born-Haber Cycle

Lattice Energy&#xA0;

An ionic compound is stable because of the electrostatic attraction between its positive and negative ions. The lattice energy of a ...

trends-in-lattice-energy-ion-size-and-charge

Trends in Lattice Energy: Ion Size and Charge

An ionic compound is stable because of the electrostatic attraction between its positive and negative ions. The lattice energy of a compound is a measure ...

Covalent Bonding and Lewis Structures

Compared to ionic bonds, which results from the transfer of electrons between metallic and nonmetallic atoms, covalent bonds result from the mutual ...

Electronegativity

Whether a bond is nonpolar or polar covalent is determined by a property of the bonding atoms called electronegativity.&#xA0;

Electronegativity values of ...

bond-polarity-dipole-moment-and-percent-ionic-character

Bond Polarity, Dipole Moment, and Percent Ionic Character

Bond Polarity

The absolute value of the difference in electronegativity (&Delta;EN) of two bonded atoms provides a rough measure of the polarity to be ...

lewis-structures-of-molecular-compounds-and-polyatomic-ions

Lewis Structures of Molecular Compounds and Polyatomic Ions

To draw Lewis structures for complicated molecules and molecular ions, it is helpful to follow a step-by-step procedure as outlined:


	Determine the ...

Resonance

The Lewis structure of a nitrite anion (NO2&minus;) may actually be drawn in two different ways, distinguished by the locations of the N-O and N=O ...

Formal Charges

In some cases, there are seemingly more than one valid Lewis structures for molecules and polyatomic ions. The concept of formal charges can be used to ...

Exceptions to the Octet Rule

Many covalent molecules have central atoms that do not have eight electrons in their Lewis structures. These molecules fall into three categories:


	...

Bonding in Metals

Metallic bonds are formed between two metal atoms. A simplified model to describe metallic bonding has been developed by Paul Dr&#xFC;de called the ...

VSEPR Theory and the Basic Shapes

Overview of VSEPR Theory

Valence shell electron-pair repulsion theory (VSEPR theory) enables us to predict the molecular structure, including approximate ...

vsepr-theory-and-the-effect-of-lone-pairs

VSEPR Theory and the Effect of Lone Pairs

Effect of Lone Pairs of Electrons&nbsp;on Molecule Geometry

It is important to note that electron-pair geometry around a central atom is not the same ...

Predicting Molecular Geometry

VSEPR Theory for Determination of Electron Pair Geometries

The following procedure uses VSEPR theory to determine the electron pair geometries and the ...

Molecular Shape and Polarity

Dipole Moment of a Molecule

Polar covalent bonds connect two atoms with differing electronegativities, leaving one atom with a partial positive charge ...

Valence Bond Theory

Overview of Valence Bond Theory

Valence bond theory describes a covalent bond as the overlap of half-filled atomic orbitals (each containing a single ...

Hybridization of Atomic Orbitals I

The mathematical expression known as the wave function, &#x3C8;, contains information about each orbital and the wavelike properties of electrons in an ...

Hybridization of Atomic Orbitals II

sp3d and sp3d&nbsp;2 Hybridization

To describe the five bonding orbitals in a trigonal bipyramidal arrangement, we must use five of the valence shell ...

Molecular Orbital Theory I

Overview of Molecular Orbital Theory

Molecular orbital theory describes the distribution of electrons in molecules in the same way as the distribution of ...

Molecular Orbital Theory II

Molecular Orbital Energy Diagrams

The relative energy levels of atomic and molecular orbitals are typically shown in a molecular orbital diagram. For a ...

Molecular Orbital (MO) Theory

Source: Tamara M. Powers, Department of Chemistry, Texas A&#38;M University
This protocol serves as a guide in the synthesis of two metal complexes ...

Intermolecular vs Intramolecular Forces

Intermolecular forces (IMF) are electrostatic attractions arising from charge-charge interactions between molecules. The strength of the intermolecular ...

Intermolecular Forces

Atoms and molecules interact through bonds (or forces): intramolecular and intermolecular. The forces are electrostatic as they arise from interactions ...

Molecular and Ionic 
Solids

Crystalline solids are divided into four types: molecular, ionic, metallic, and covalent network based on the type of constituent units and their ...

comparing-intermolecular-forces-melting-point-boiling-point

Comparing Intermolecular Forces: Melting Point, Boiling Point, and Miscibility

Intermolecular forces are attractive forces that exist between molecules. They dictate several bulk properties, such as melting points, boiling points, ...

Plan and conduct an investigation to gather evidence to compare the structure of substances at the bulk scale to infer the strength of electrical forces between particles.

HS-PS1-3.

Radioactivity and Nuclear Equations

Nuclear chemistry is the study of reactions that involve changes in nuclear structure. The nucleus of an atom is composed of protons and, except for ...

Types of Radioactivity

The most common types of radioactivity are &#945; decay, &#946; decay, &#947; decay, neutron emission, and electron capture.
Alpha (&#945;) decay is the ...

Nuclear Stability

Protons and neutrons, collectively called nucleons, are packed together tightly in a nucleus. With a radius of about 10&#8722;15 meters, a nucleus is ...

Nuclear Binding Energy

The difference between the calculated and experimentally measured masses is known as the mass defect of the atom. In the case of helium-4, the mass defect ...

Radioactive Decay and Radiometric Dating

Radioactivity is a spontaneous disintegration of an unstable nuclide and is a random process, as all the nuclei in the sample do not decay simultaneously. ...

Nuclear Fission

Many heavier elements with smaller binding energies per nucleon can decompose into more stable elements that have intermediate mass numbers and larger ...

Nuclear Power

Controlled nuclear fission reactions are used to generate electricity. Any nuclear reactor that produces power via the fission of uranium or plutonium by ...

Nuclear Fusion

The process of converting very light nuclei into heavier nuclei is also accompanied by the conversion of mass into large amounts of energy, a process ...

Nuclear Transmutation

Nuclear transmutation is the conversion of one nuclide into another. It can occur by the radioactive decay of a nucleus, or the reaction of a nucleus with ...

Biological Effects of Radiation

All radioactive nuclides emit high-energy particles or electromagnetic waves. When this radiation encounters living cells, it can cause heating, break ...

determining-rate-laws-and-the-order-of-reaction

Determining Rate Laws and the Order of Reaction

Source: Laboratory of Dr. Neal Abrams &#8212; SUNY College of Environmental Science and Forestry
All chemical reactions have a specific rate defining the ...

Develop models to illustrate the changes in the composition of the nucleus of the atom and the energy released during the processes of fission, fusion, and radioactive decay.

HS-PS1-8.

Properties of Transition Metals

Transition metals are defined as those elements that have partially filled d orbitals. As shown in Figure 1, the d-block elements in groups 3&#8211;12 are ...

Coordination Compounds and Nomenclature

In most main group element compounds, the valence electrons of the isolated atoms combine to form chemical bonds that satisfy the octet rule. For ...

Metal-Ligand Bonds

The hemoglobin in the blood, the chlorophyll in green plants, vitamin B-12, and the catalyst used in the manufacture of polyethylene all contain ...

Coordination Number and Geometry

For transition metal complexes, the coordination number determines the geometry around the central metal ion. Table 1 compares coordination numbers to ...

Communicate scientific and technical information about why the particulate-level structure is important in the functioning of designed materials.

HS-PS2-6.

Protein Mapping with 2D Gel Electrophoresis

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