7.3 translation
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Translation is the process by which the genetic code carried by mRNA is used to synthesize proteins. It involves three stages - initiation, elongation, and termination. During initiation, the small ribosomal subunit binds to the mRNA start codon along with initiator tRNA. In elongation, amino acids are added one by one to form the polypeptide chain. Termination occurs when a stop codon enters the ribosomal A site and the protein is released. The primary, secondary, tertiary, and sometimes quaternary structures of proteins are determined by the sequence of amino acids and various bonding interactions.
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INTRODUCTION
HISTORY
MECHANISM OF PROTEIN SYNTHESIS
TRANSCRIPTION
TRANSLATION
TRANSCRIPTION
INITIATION
ELONGATION
TERMINATION
TRANSLATION
AMINOACYLATION OF tRNA
INITIATION OF POLYPEPTIDE CHAIN
ELONGATION
TERMINATION
CONCLUSION
REFERENCES
How cells read the genome from DNA to protein Notes
The document summarizes the process of transcription and translation in cells. It describes:
1) Transcription of DNA to RNA which is catalyzed by RNA polymerase and involves the formation of RNA through the addition of ribonucleotides.
2) Processing of eukaryotic pre-mRNA which involves capping, splicing, and polyadenylation to form mature mRNA.
3) Translation of mRNA to protein which occurs on ribosomes and involves tRNAs carrying amino acids that are linked together through peptide bond formation catalyzed by the ribosome. Accuracy is ensured by induced fit binding and kinetic proofreading.
Prokaryotic translation
It is the process of synthesis of protein by encoding information on mRNA.
Protein synthesis requires mRNA, tRNA, aminoacids, ribosome and enzyme aminoacyl tRNA synthase
TRANSLATION
Messenger RNA carries genetic code from DNA and is translated by the ribosome into proteins. This involves transfer RNA molecules that associate amino acids with their codons. Translation begins with initiation factors recruiting the small ribosomal subunit to the start codon. Elongation then occurs through peptide bond formation catalyzed by the ribosome and translocation of transfer RNAs. Termination occurs when a stop codon is reached. Translation is highly conserved and essential for protein synthesis in all organisms.
Gene expression
Gene expression is the process by which information from a gene is used to produce a functional product like proteins or RNA. It involves two main steps: transcription of DNA into mRNA and translation of mRNA into proteins. Transcription involves unwinding the DNA and synthesizing mRNA complementary to the template strand. Translation uses ribosomes to read the mRNA codon by codon and add the corresponding amino acids to produce a protein according to the genetic code. It occurs through three phases: initiation, elongation, and termination.
Gene expression & protein synthesis
Gene expression involves the transcription of DNA into mRNA and the translation of mRNA into proteins. There are four main stages of protein synthesis: activation, initiation, elongation, and termination. Transcription is regulated by promoters, enhancers, and response elements that control the rate of transcription and influence which genes are expressed. Translation includes quality control mechanisms to ensure accuracy, such as ensuring amino acids are bound to the proper tRNAs and that termination occurs at stop codons. Mutations can occur during DNA replication or transcription and may be caused by mutagens, though cells have repair mechanisms. Recombinant DNA techniques allow genes to be spliced from one organism into a plasmid or virus for protein production in other cells.
Translation .pptx
The process by which a cell makes proteins using the genetic information carried in messenger RNA (mRNA).
Ch14-2translation.pptx
Ribosomes translate mRNA into polypeptides. They consist of two subunits containing rRNA and proteins. tRNAs carry specific amino acids and recognize mRNA codons through complementary base pairing between their anticodons. Translation involves initiation, elongation, and termination. During initiation, the small ribosomal subunit binds the 5' end of mRNA. Elongation adds amino acids to the growing polypeptide chain through peptide bond formation. Termination releases the polypeptide when a stop codon is reached. Accurate protein synthesis depends on specific interactions between mRNA codons, tRNA anticodons, and the ribosomal subunits.
Translation ( synthesis of proteins )
Translation is the process by which the genetic code carried by mRNA is used to synthesize proteins. It requires ribosomes, tRNA, amino acids, and various enzymes. There are three main steps: initiation begins protein synthesis using initiator tRNA; elongation joins amino acids through peptide bond formation and translocation; and termination releases the complete polypeptide when a stop codon is reached. The newly formed protein then undergoes post-translational modifications to achieve its functional structure and may combine with other proteins. Multiple ribosomes can translate the same mRNA simultaneously as a polysome.
Campbell6e lecture ch12
This document summarizes key aspects of protein synthesis, including translation of mRNA into a polypeptide chain. It discusses the genetic code and how triplet codons specify amino acids. The stages of translation - initiation, elongation, and termination - are described. Post-translational modifications and protein degradation are also covered. Protein synthesis requires various ribosomal and transfer RNA components to translate the genetic message into proteins.
Translation
Translation is the process by which messenger RNA (mRNA) is used to produce proteins. It involves decoding the mRNA to build a polypeptide chain of amino acids. Translation requires several components, including amino acids, ribosomes, mRNA, transfer RNA (tRNA), and protein factors. It occurs through three main stages - initiation, elongation, and termination. Initiation involves assembling the ribosome and first tRNA on the mRNA start codon. Elongation is the process of linking amino acids together via peptide bonds. Termination occurs when a stop codon is reached, releasing the complete protein chain. The new protein may then undergo further processing and modification.
protein synthesis in prokaryotes.pptx
presentation covers basic structure of protein, its synthesis and regulation in prokaryotic organisms
Gene and protein, protein synthesis
INTRODUCTION
DEFINATION
CENTRALDOGMA
TRANSCRIPTION
TRANSCRIPTION IN PROKARYOTES
INITIATION
ELONGIATION
TERMINATION
TRANSLATION
TRANSLATION IN PROKARYOTES
ACTIVATION OF AMINOACID
INITIATION OF POLYPEPTIDE SYNTHESIS
ELONGIATION
TERMINATION
CONCLUSION
REFERANCE
INTRODUCTION
DEFINATION
CENTRALDOGMA
TRANSCRIPTION
TRANSCRIPTION IN PROKARYOTES
INITIATION
ELONGIATION
TERMINATION
TRANSLATION
TRANSLATION IN PROKARYOTES
ACTIVATION OF AMINOACID
INITIATION OF POLYPEPTIDE SYNTHESIS
ELONGIATION
TERMINATION
CONCLUSION
REFERANCE
PROTEIN SYNTHESIS IN EUKARYOTES.pptx
Protein synthesis in eukaryotes involves three main steps - initiation, elongation, and termination. Initiation requires many initiation factors and begins with formation of a preinitiation complex on the 5' end of mRNA. Elongation is cyclic and adds one amino acid at a time to the growing polypeptide chain using elongation factors. Termination occurs when a stop codon is reached and release factors cause dissociation of the ribosome and polypeptide release. Additional processes like post-translational modifications further process the final protein structure and function.
Translation part 1
Translation is the process by which cells make proteins. It involves three key factors: m RNA, t RNA and r RNA. mRNA of eukaryotes is structurally and functionally different from prokaryotic m RNA. the t RNA contains an aminoacid binding site and a codon binding site. The ribosome has three tRNA-binding sites.
• An aminoacyl-tRNA enters the A site.
• Peptidyl-t RNA is bound in the P site.
• Deacylated tRNA exits via the E site.
• An amino acid is added to the polypeptide chain by
transferring the polypeptide from peptidyl-tRNA in the
P site to aminoacyl-tRNA in the A site.
A codon in mRNA is recognized by an aminoacyl-tRNA, which has an anticodon complementary to the codon and carries the amino acid corresponding to the codon.
Recognition of a prokaryotic initiation site involves binding of a sequence at the 3 ' end of rRNA to the Shine-Dalgarno motif, which precedes the AUG (or GUG) codon in the mRNA. Recognition of a eukaryotic mRNA involves binding to the 5 ' cap; the small subunit then migrates to the initiation site by scanning for AUG codons.
A special initiator tRNA (fMet-tRNAr in prokaryotes or Met-tRNA; in eukaryotes) recognizes the AUG codon, which is used to start all coding sequences.
Small subunits bind to mRNA and then are joined by large subunits to generate an intact ribosome that undertakes translation.
Similar to 7.3 translation (20)
How cells read the genome from DNA to protein Notes
How cells read the genome from DNA to protein Notes
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6.6 hormones, homeostasis, and reproduction
Insulin, glucagon, thyroxine, leptin, melatonin, and reproductive hormones help regulate homeostasis and reproduction. Insulin and glucagon regulate blood glucose levels. Thyroxine regulates metabolism. Leptin regulates appetite. Melatonin regulates circadian rhythms. Reproductive hormones like testosterone and estrogen influence sexual development and control the menstrual cycle through feedback mechanisms. New technologies like IVF involve manipulating hormone levels to induce superovulation and establish pregnancies.
10.3 gene pools and speciation
This document discusses gene pools, speciation, and mechanisms of reproductive isolation. It defines key terms such as allele frequency, gene pool, and types of reproductive isolation like geographical, temporal, and behavioral isolation. Mechanisms of speciation discussed include gradual divergence of isolated populations and abrupt speciation. Examples of natural selection pressures like directional, stabilizing, and disruptive selection are provided, as well as speciation through polyploidy in plants. The document contrasts theories of gradualism and punctuated equilibrium in the rate of speciation. Homework questions are assigned related to defining terms and challenging concepts.
10.2 inherritance
This document discusses inheritance and related concepts. It defines key terms like linked genes, which are genes located on the same chromosome. When genes are linked, they may assort independently during meiosis leading to recombinants. It also discusses polygenic inheritance where multiple genes influence traits, often resulting in continuous variation. The document provides examples of dihybrid crosses using Punnett squares and sex-linked inheritance from Thomas Morgan's experiments with fruit flies. Homework includes defining terms and working exercises on linked genes and dihybrid crosses.
10.1 meiosis
Meiosis involves two rounds of cell division that results in four haploid cells from one original diploid cell. During meiosis I, homologous chromosomes separate and non-sister chromatids may exchange DNA through crossing over. This leads to new combinations of parental alleles in offspring. Meiosis II then separates the sister chromatids, resulting in four unique gametes. Independent assortment of chromosomes during meiosis contributes further to genetic variation between offspring.
3.5 part 2
Gene transfer involves taking a gene from one organism and placing it into another. Examples given are genes from fish that have been inserted into plants to make them resistant to freezing, and Bt corn which contains genes from Bacillus thuringiensis bacteria that produce toxins killing insect pests. Cloning techniques allow for precise copying of genes. Restriction enzymes cut DNA at specific sequences, allowing genes to be removed and inserted into other organisms using DNA ligase. Transgenic plants and animals are created this way, with potential uses including producing crops resistant to pests or dairy animals with higher milk output. Cloning can also be used for therapeutic purposes like stem cell research. There is debate around the ethics of altering organisms' genetic identities
3.5 part 1
The document discusses polymerase chain reaction (PCR) and how it is used to amplify small amounts of DNA, allowing researchers to generate large quantities of identical DNA copies. It explains the basic steps in PCR, including separating DNA strands, adding primers and nucleotides, and repeating the process for multiple cycles to exponentially replicate the target DNA. The document also describes some common applications of PCR like DNA profiling, gene cloning, and detecting genetically modified organisms.
3.3 meiosis
Meiosis is a type of cell division that produces haploid gametes from a diploid cell for sexual reproduction. It involves two rounds of division and has four main stages - prophase I, metaphase I, anaphase I, and telophase I make up the first meiotic division while prophase II, metaphase II, anaphase II, and telophase II make up the second. During meiosis I, homologous chromosomes pair up and may exchange genetic material through crossing over. Then the homologous chromosomes separate, reducing the chromosome number by half. Meiosis II then separates the sister chromatids, resulting in four haploid daughter cells. Errors in meiosis can cause non-disjunction and
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The document summarizes the body's primary defenses against infectious disease. The skin and mucous membranes form the first line of defense through physical and chemical barriers. Cuts in the skin are sealed by blood clotting initiated by platelets. Phagocytic white blood cells provide non-specific immunity by ingesting pathogens. Lymphocytes produce specific antibodies in response to antigens that provide long-term immunity. Antibiotics target bacterial rather than viral or eukaryotic cells. Overuse of antibiotics can lead to resistant bacterial strains.
7.1 dna structure and replication
DNA contains the genetic information that is passed from parents to offspring. It is made up of nucleotides joined by phosphodiester bonds to form a double helix structure. DNA replication involves unwinding of the helix by helicase, addition of RNA primers by primase, and synthesis of new DNA strands in the 5' to 3' direction by DNA polymerase. The leading strand is replicated continuously while the lagging strand involves discontinuous synthesis of Okazaki fragments that are later joined by DNA ligase.
6.2 bloodflow
The document describes the structure and function of the blood system, including the three main types of blood vessels (arteries, capillaries, and veins), how blood flows through the circulatory system from the heart to tissues and back again, and some pathologies that can occur like atherosclerosis and heart attacks. The heart functions as a pump to circulate blood through the arteries and veins, with capillaries allowing for exchange of oxygen, nutrients, and waste between the blood and body tissues. Valves in the veins and heart prevent backflow of blood and ensure forward circulation.
6.1 digestion
The document discusses the process of digestion and absorption in the small intestine, including how enzymes break down macromolecules, how villi and microvilli increase absorption surface area, and how different transport methods absorb breakdown products across the intestinal epithelium into capillaries and lacteals. It also provides examples of homework assignments related to the topic, such as producing a diagram of the digestive system and explaining starch digestion and transport to the liver.
2.7 replication, transcription, translation
1. DNA replication is semi-conservative. Helicase unwinds the DNA double helix, DNA polymerase links nucleotides to form new strands using the existing strands as templates.
2. Transcription creates mRNA from DNA templates using RNA polymerase.
3. Translation uses the genetic code to synthesize polypeptides from mRNA. tRNAs with anticodons complementary to mRNA codons carry amino acids which are linked by the ribosome.
2.4 proteins
Proteins are composed of amino acids linked together by peptide bonds to form polypeptides. The amino acid sequence of polypeptides is determined by genes. There are 20 common amino acids that make up proteins, though some organisms have exceptions. Proteins have a variety of functions in living organisms and each person has a unique set of proteins.
2.3 carbohydrates and lipids
This document discusses carbohydrates and lipids. It defines monosaccharides, disaccharides, and polysaccharides. It provides examples of monosaccharides like glucose and examples of disaccharides like sucrose. It discusses cellulose, starch, and glycogen as important polysaccharides. It also defines saturated and unsaturated fatty acids, as well as cis and trans fatty acid isomers. Triglycerides are formed from fatty acids and glycerol. Lipids provide more energy storage than carbohydrates. The document also provides formulas for calculating body mass index.
2.1 molecules to metabolism
The document discusses key concepts in molecular biology and metabolism. It explains that life is based on carbon compounds like carbohydrates, lipids, proteins, and nucleic acids. Metabolism is defined as the set of enzyme-catalyzed reactions in cells and organisms, including both anabolism, the synthesis of complex molecules from simpler ones, and catabolism, the breakdown of complex molecules into simpler ones. Macromolecules are formed from monomers through condensation reactions, and broken down through hydrolysis reactions. Examples of molecular structures are provided for glucose, ribose, a fatty acid, and an amino acid.
8.3 photosynthesis
The document summarizes photosynthesis, including both the light-dependent and light-independent reactions. It explains that the light-dependent reactions take place in the thylakoid membranes and produce ATP and NADPH through the absorption of light by photosystems. The light-independent reactions take place in the chloroplast stroma and use ATP and NADPH to produce glucose through the Calvin cycle. The structure of the chloroplast is adapted to efficiently carry out these two stages of photosynthesis through the stacking of thylakoids and positioning of the stroma.
2.2 properties of water
This document discusses the properties of water molecules and how those properties allow water to serve important functions. It covers the following key points:
1) Water molecules are polar due to their molecular structure, and they form hydrogen bonds between each other. This explains water's cohesive, adhesive, thermal, and solvent properties.
2) Substances can be either hydrophilic ("water-loving") if they are polar, or hydrophobic ("water-fearing") if they are nonpolar. Polar substances like glucose and phospholipids can dissolve in water due to hydrogen bonding.
3) Water has high specific heat and heat of vaporization, allowing it to effectively absorb and release heat. This contributes to temperature regulation
8.2 cell respiration
The document summarizes cellular respiration. It describes that glycolysis converts glucose to pyruvate and yields a small amount of ATP without oxygen. In aerobic respiration, pyruvate enters the mitochondria and is oxidized to acetyl-CoA. The Krebs cycle further oxidizes acetyl-CoA, producing electron carriers and CO2. The electron transport chain uses protons to power ATP synthase to generate more ATP through chemiosmosis. The structure of the mitochondria is adapted for these functions through cristae that provide surface area for electron transport and an intermembrane space to accumulate protons.
1.4 membrane transport
This document discusses membrane transport, including passive transport mechanisms like diffusion, facilitated diffusion, and osmosis as well as active transport. It defines key terms and concepts related to transport across membranes, like concentration gradients, solute concentrations, hypertonic and hypotonic solutions, and the sodium-potassium pump. Examples of applications and skills involving membrane transport are given, like using osmosis experiments to measure mass and volume accurately and ensuring organ tissues match cytoplasmic osmolarity before medical procedures. Homework assignments review related vocabulary and challenge the reader to apply their understanding.
1.3 membrane structure
The document discusses membrane structure and models of the membrane. It begins by explaining the Davson-Danielli model from 1935 which proposed that the lipid bilayer was covered on both sides by a protein layer. However, this model was later falsified as evidence showed membranes were not always symmetrical. The Singer-Nicolson fluid mosaic model proposed in 1972 stated that proteins are inserted into the phospholipid bilayer in a mosaic pattern. This fluid mosaic model remains the current understanding of membrane structure, composed of a phospholipid bilayer with integral and peripheral proteins, cholesterol, and glycoproteins.
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2:同时对留学生所学专业登记给予评定
3:国家专业人才认证中心颁发入库证书
4:这个认证书并且可以归档倒地方
5:凡事获得留信网入网的信息将会逐步更新到个人身份内，将在公安局网内查询个人身份证信息后，同步读取人才网入库信息
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7.3 translation
- 2. Guidance - Names of the tRNA binding sites are expected, as well as their roles. - Examples of stop and start codons are not required. - Polar and non-polar amino acids are relevant to the bonds formed between R-groups. - Quaternary structure may involve the binding of a prosthetic group to form a conjugated protein Understandings • Initiation of translation involves assembly of the components that carry out the process. • Synthesis of the polypeptide involves a repeated cycle of the events. • Disassembly of the components follows termination of translation. • Free ribosomes synthesize proteins for use primarily in the cell. • Bound ribosomes synthesize proteins primarily for secretion or for use in lysosomes. • Translation can occur immediately after transcription in prokaryotes due to the absence of a nuclear membrane. • The sequence and number of amino acids in the polypeptide is the primary structure. • The secondary structure is the formation of alpha helices and beta pleated sheets stabilized by hydrogen bonding. • The tertiary structure is the further folding of the polypeptide stabilized by interactions between the R- groups. • The quaternary structure exists in proteins with more than one polypeptide chain. Applications/Skills • A: tRNA-activating enzymes illustrate enzyme-substrate specificity and the role of phosphorylation. • S: Identification of polysomes in electron micrographs of prokaryotes and eukaryotes. • S: The use of molecular visualization software to analyze the structure of eukaryotic ribosomes and a tRNA molecule.
- 3. The Ribosome http://melajr.files.wordpress.com/2012/03/ribosome-subunit.jpg Composed of rRNA and proteins Holds the tRNA carrying the next amino acid to be added to the chain Holds the tRNA carrying the growing chain Site from which tRNA that has lost its amino acid is discharged
- 4. tRNA Adapted from http://classconnection.s3.amazonaws.com/185/flashcards/82185/jpg/6_361320375541451.jpg 5’3’ CUU CGC GUAGCA The amino acid attached is determined by a particular enzyme (20 AA’s 20 enzymes) Activated Amino Acid
- 5. Initiation • Activated amino acid (methionine) attaches to a tRNA with the anticodon UAC • This combines with an mRNA and small ribosomal subunit • Small subunit moves down the mRNA until it reaches the codon AUG • H bonds form between the initiator tRNA and start codon • Large subunit combines with these parts along with initiation factors (proteins) and GTP (similar to ATP)
- 6. Elongation • tRNA’s bring amino acids to the mRNA- ribosomal complex • Elongation factors assist in binding the tRNA’s to the mRNA codons • Initiator tRNA moves to the P site • Ribosomes catalyze the formation of peptide bonds between the amino acids http://www.tokresource.org/tok_classes/biobiobio/biomenu/transcription_translation/translation_1.jpg
- 7. Translocation • Occurs during elongation • Movement of tRNA’s from one site to another • A siteP siteE site • Occurs in the 5’ 3’ direction http://www.tokresource.org/tok_classes/biobiobio/biomenu/transcription_translation/translation_1.jpg
- 8. Termination • Stop codon appears in the A site • A release factor fills the A site and catalyzes hydrolysis of the bond between the tRNA in the P site and the amino acid chain • Polypeptide is released • Ribosomal subunits separate from the mRNA http://thelessonlocker.com/kvhs/biology/translation_termination.jpg
- 10. Video
- 11. Primary Organization • Sequence of amino acids • Determines the next 3 levels • Changing one amino acid can result in a dysfunctional protein http://mykelmedia.com/wp-content/uploads/2010/11/sickle-cell.jpg
- 12. Secondary Organization • Alpha helix or beta pleated sheet • Results from H bonds between the O from a carboxyl group on one amino acid and the H from the amino group of another amino acid • Does NOT involve R groups http://www.abcte.org/files/previews/biology/BioMod%203%5B1%5D.3%20secondary%20structure.jpg
- 13. Tertiary Organization • Three-dimensional configuration as a result of interactions between R-groups • Disulfide bridges: covalent bonds between sulfur atoms • H-bonds • Van der Waals interactions: hydrophobic R-groups forced inward and hydrophilic R-groups interact with water in aqueous solutions • Ionic bonds https://bestofbiochemistry.files.wordpress.com/2013/03/tertiary_structure.jpg
- 14. Quaternary Structure • Two or more polypeptide chains combine to form a single functional protein • Involves all bonds previously mentioned • Can include a non-polypeptide portion (conjugated protein) http://bio3400.nicerweb.com/Locked/media/ch14/14_20-protein_structure-quaternary.jpg
- 15. Fibrous vs Globular Proteins Fibrous Globular - Many polypeptide chains in a long narrow shape - Generally insoluble in water - Ex: Collagen - More three dimensional in shape - Generally water soluble - Ex: Insulin http://www.extremepeptides.com/blog/wp-content/uploads/2013/05/2GF1_Insulin-Like_Growth_Factor_Nmr_Minimum_Average_Structure01.pnghttp://www.prevention.com/sites/prevention.com/files/static/comp-3974997-collagen_0.jpg