3) Give three examples of where we find proteins in our bodies. a. b. с. Draw the structural formula for a typical amino acid using the letter R to represent the radical group
Q: A polypeptide is shown below. Please answer the following questions. OH В A C H;N E H D H a. Match…
A: A polypeptide is a long, unbranched chain of amino acids joined by peptide/amide bonds. The peptide…
Q: Draw the following amino acids interactions: 1. H-bond - between -0H of Serine amino acid and C=0…
A: Between an electronegative atom with a lone pair of electrons and a hydrogen atom that is covalently…
Q: Give the difference between a proteins tertiary and quaternary structure.
A: Proteins is polypeptide chain which is formed of combination of multiple amino acid joined together…
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A: Proteins are defined as macromolecules or large biomolecules composed of one or more long chains of…
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A: Introduction Amino acids are a kind of nutrient. Proteins are polymers of nitrogenous chemicals…
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A: Macromolecules are molecules containing large number of atoms, such as carbohydrate, protein, lipid…
Q: As we have seen in Chapter 28, monosaccharides can be drawn in a variety of ways, and in truth,…
A: Monosaccharides are the simplest unit of carbohydrates. They can be divided into trioses, tetroses,…
Q: Adjacent amino acids are linked together by the formation of a peptide bond between which of the…
A: In biological molecules, two main types of bonds are found that is covalent and non-covalent bonds.…
Q: Name and draw the structures of the amino acids that fit the following descriptions:(a) Contains an…
A: An amino acid is an organic molecule that is made up of a basic amino group (−NH2), an acidic…
Q: Which is more likely to be changed by heating a protein, its primary structure or its tertiary…
A: When heating of the protein is done then primary structure of the protein does not get changed or…
Q: proteins, which of the following are the characteristic patterns that arise when hydrogen bonds form…
A: The different levels of protein structures are known as primary, secondary, tertiary, and quaternary…
Q: Which of the following characterize -helix regions of proteins? (A) They all have the same primary…
A: Helix is a protein structure that looks like a moving staircase or a spring. The wire of the spring…
Q: What is the highest structural level of protein structure represented in the following image?…
A: When applied to proteins, the term structure has a far more complicated meaning than when applied to…
Q: 9.3 Identify which of the following are a-amino acids. CH3 | H₂N-C-COOH CH, a. b. H H₂N-C-CH₂-COOH…
A: The proteins are constituted of 20 naturally occurring amino acids. The amino acids are all alpha…
Q: The structure of a peptide is shown below: H. HN NH, NH, What is the pl of this peptide? А. 3.24 О…
A: The isoelectric point of a protein is the pH at which the net charge of the protein is zero. At this…
Q: Which component(s) participate in bonds that form the tertiary structure of a protein? Select all…
A: Proteins are polymers of amino acids. The amino acids are connected by a peptide bond. Primary,…
Q: When we refer to the backbone of a polypeptide, we are referring to the attachment between: Select…
A: The body uses biomolecules for its functioning. Biomolecules like carbohydrate, protein, lipids etc…
Q: Creating tertiary structures of proteins involves the linking of amino acid functional groups with…
A: Proteins are the building blocks of the body. All the life forms consist of proteins in their cell…
Q: Indicate which of the following properties depend only on the chemical nature of its repeating…
A: DNA is the hereditary material found in all organisms. The main function of DNA is to store genetic…
Q: Describe the specific bonding responsible for secondary structure in proteins, including which atoms…
A: The secondary structure of proteins is a three dimensional structure of a local folding .its…
Q: The protein pictured has .. O A) primary structure B) secondary structure C) tertiary structure D)…
A: Proteins are a class of complex nitrogen organic compounds, composed of amino acid residues joined…
Q: The side chains of some amino acids possess functional groups that can form hydrogen bonds in…
A: Amino acids are organic compounds. Amino acids contain amino and carboxylic acid functional groups.…
Q: Show a tertiary structure of ACGGC after a disulfide bond forms.
A: Protein folding is the physical process by which a primary sequence of amino acids or a linear…
Q: The amide linkages of proteins are referred to as________________________.
A: Introduction: Proteins are major biomolecules that consist of long chains of amino acids. The…
Q: List down which amino acids are capable of the following interactions in the tertiary structures of…
A: There are 20 standard amino acids are there which make up all the proteins inside the cell. Amino…
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A: Protein is the linear, unbranched polymer of amino acids. Amino acids are joined together by the…
Q: Because of their tendency to avoid water, nonpolar aminoacids play an important role in forming and…
A: Polymers of L-alpha amino acids form the protein.The structural organisation of protein can be…
Q: Which of the following properties of a protein is least likely to be affected by denaturing agents?*…
A: Proteins are the biopolymers that are organised in four levels of structural organisation. Primary…
Q: Compounds X and Y are acidic amino acid and basic amino acid, respectively. While monomers A and B…
A: Proteins are unbranched polymers constructed from 20 standard α-amino acids. They have four levels…
Q: Which of the following characterize -helix regions of proteins? (A) They all have the same primary…
A: Helix is a protein structure that looks like a moving staircase or a spring. The wire of the spring…
Q: Below is the primary structure of a protein. Вс D R H H H || II || E C - N - с — С — N — С — С — N —…
A: Polypeptides are unbranched, linear polymers that are composed of amino acids linked together by…
Q: Explain the meaning of the designations d and l used to specify the configuration of…
A: A chiral molecule is not the same as its mirror image and cannot be superimposed on its mirror…
Q: Given amino acids A and B 5. Draw the structure of amino acid A at pH < pI 6. Draw the structure…
A:
Q: Φ and ψ in the Ramachandran plot (below) are: a) Rotational angles around the bond between the…
A:
Q: Peptide bond formation occurs between which functional groups? SELECT ALL THAT APPLY A. Amino…
A: A protein is a polymeric macromolecule which is formed by linking together of many monomeric units…
Q: Explain how the tertiary structure of a protein is stabilized by various intermolecular forces and…
A: A protein is considered to be a biological macromolecule made up of one or more polypeptide…
Q: What types of interactions are possible between the side chains of the polypeptide shown below?…
A: Proteins are the polymers of amino acid connected to each other by covalent peptide bond.
Q: Draw the amino acids at the following pH's. Include both the backbone and the sidechain of the amino…
A: There are 20 standard amino acids that make up all the proteins inside the cell. The amino acids are…
Q: Which two types of bonding are in the 1ubq (Ubiquitin)? Explain your choices. a) Hydrogen bonding…
A: The two types of bonding present in 1ubq(ubiquitin) is a) covalent bond b) disulphide bond.…
Q: Describe the levels of structure of a protein and tell how they would be affected by: a. Hydrolysis…
A: Proteins are composed of amino acids. They are linked together by peptide linkages. Proteins have…
Q: Protein secondary structure is stabilized by ... a) H-bonds between functional groups on amino…
A: Ans-Protein secondary structure is stabilized by - d) a and c i.e. H-bonds between functional…
Q: Which covalent bond(s) is/are important for the formation of quaternary structure in proteins?…
A: Proteins are big, complex molecules that play a number of important roles in the human body. They…
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A: Immunology is a section of biology that includes the study of molecules, cells, and organs that…
Q: If you heat a protein to break the intramolecular hydrogen bonds, will you maintain the a-helical or…
A: In the polypeptide chain, the primary structure of a protein refers to the amino acid sequence. The…
Q: The structure of a protein that involves alpha elices and beta-pleated sheets is is O A. primary…
A: Question- The structure of a protein that involves alpha elices and beta-pleated sheets is O A…
Q: Key properties of proteins include: O a. A wide range of functional groups and an ability to possess…
A: Proteins are large biomolecules and macromolecules that comprise one or more long chains of amino…
Q: What type of interaction would you expect between the following R groups in the tertiary structure…
A: Sidechains of amino acids in a protein structure interact with each other in many ways. This…
Q: Draw the Fischer projections representing the L forms of the following amino acids at pH higher than…
A: Amino acids contain amino group and carboxyl group along with R side chain. The R side chain defines…
Q: What type of tertiary structure interactions are most likely between the following amino acids? (Use…
A: Amino acids are building blocks of proteins; they include a carboxylic acid group on the alpha…
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- al - Seattle x S WRLD LIT COMP 10A: Identity Sound+of+Wa x Identity Sound+of+Wa x S Forrar (wrap) y decorar S Scho A districtIms.seattleschools.org/common-assessment-delivery/start/5398502362?action=onresume&submissionld=657119921 Concentration, Osmosis, and Cell Environments HW Quiz Assume that the picture below shows environments on two sides of a selectively permeable membrane. Assume the light blue circles are water molecules. Assume the red circles are glucose molecules. Which side has the higher concentration? left right Which best describes the way that the particles move?16. Your Excel data graph for Serial Dilution lab:** 16a. Include a clear and labeled graph of DF (x axis) versus Absorbance (y axis). See box above for expectations and review video tutorial of this Excel work. Do not graph two of your data points: your blank or your Cuvette #1 (DF=1). 1 Q A Multiple Styles W S X 3 E D $ 4 To C R F % 5 I T V U ^ 6 G Y 7 H U 8 J BN S ( 9 K M XColor: Dark Yellow | Transparency: Turbid Glucose: Trace pH: 6.5 Leukocyte: +1 Ketones: Negative Protein: Trace Protein: Trace Blood: +1 Urobilinogen: Negative 8. 8. 1st field 2nd field 3rd field 4th field
- sis(1) - Saved ansitions Animations add notes C $ 4 101 BIUS ab AY - Aa- - A R F Slide Show Font 16 V f5 % 1. What is the % of glucose and sodium outside the cell? 2. What is the % of glucose and sodium inside the cell? Record Α 3. What is the % of water outside the cell? O Search 5 Search 4. What is the % of water side the cell? 5. Will osmosis occur? 6. The cell is in what type of solution (hypertonic, hypotonic, isotonic)? T G Help Α Α Ξ ΞΞΞ f6 Review View N B Y f7 O & 7 N Paragraph hip U f8 * 4+ H J M fg T 16 MH- K 35% Glucose f12 Find Replace Select- Editing + [ 1.9 88 10 2 -- 5 ? 12 insert Re Dicta Voic 个 ] pauWhy is it not advisable to use adhesive mixture if protein histological investigation are contemplatedTotal Protein Determination Spectroscopy Values CREATE CALIBRATION CURVE? DRAWN CONCENTRATION AND ABSORPTION CURVE
- d/e/1FAIpQLSfTle9UfP15_VUqFI-ACEQd1XBykXv5Lr4dEMQbLJ1d6fCupw/viewform Students subjected three samples of five different molecules to gel electrophoresis as shown in Figure 1 A B C DE +2 3 Wells 4 8. Which of the following statements best explains the pattern seen on the * gel with regard to the size and charge of molecules A and B? 1 point molecules A and B are positively charged, and molecule A is smaller than molecule B. molecules A and B are positively charged, and molecule A is larger than molecule B. molecules A and B are negatively charged, and molecule A is smaller than molecule B. molecules A and B are negatively charged, and molecule A is larger than molecule B. Sign outI. Qualitative Analyses of Proteins Complete the table below. Chemical/reagent used (be specific) Final expected Test Sample Interpretation visible result after the experiment (color change, precipitation, etc.) Egg albumin Gelatin dispersion Biuret test 0.5% urea 0.5% glycine Egg albumin Xanthoproteic test Gelatin dispersion 0.5% lysine 0.5% tryptophan Egg albumin Gelatin dispersion 0.5% glycine 0.5% asparagine Egg albumin Ninhydrin test Millon's test Gelatin dispersion 0.5% tyrosine 0.5% glycineDirection: Read and analyze the following laboratory experiment and answer the following question. PART 3: PLASMOLYSIS Materials: safety goggles, red onion, dropper, slides & cover slips, tweezers/ forceps, compound microscope, iodine, small knife, water, salt (5% and 10% solution) Methodology: 1. With goggles on, carefully cut the onion into wedge shaped pieces using a knife. 2. Use an eye dropper to place a drop of water in the center of a microscope slide. Use the tweezers to peel a thin layer of skin tissue from the thick part of the onion wedge and place it in the center of the microscope slide. 3. 4. 5. Add a drop of water and a drop of iodine over the onion tissue on the slide. Carefully lower a cover glass slip at an angle on the stained tissue to allow air bubbles to escape. 6. Examine the prepared slide under the compound microscope at 100X magnification. 7. Record what the cells look like. 8. Prepare a 5% salt solution by adding 5 grams of salt (measure with balance) per 100…
- Report Sheet: Proteins (page 3) What kind of protein is casein? Name: POST-LABORATORY QUESTIONS: What is the isoelectric point of casein? What is acid in our sour milk? How is it produced? What type of chemical grouping is present in all proteins? How many of these chemical groupings must be present in a molecule to give a positive Biuret test? Give the principle involved and the chemical structure responsible for the positive Biuret Test? Can you distinguish proteins and other amino compounds by the Ninhydrin test? Explain. 30 | BiochemistryThe reults for the macroscopic part: 0.30M glycerin – solution was translucent (could see text behind the test tube) 0.15M NaCl – solution was opaque (could not see text behind the test tube) 0.30M NaCl – solution was opaque (could not see text behind the test tube) 0.15M glucose – solution was translucent (could see text behind the test tube) 0.30M glucose – solution was opaque (could not see text behind the test tube) 0.30M Urea – solution was translucent (could see text behind the test tube) Results for microscopic part: 0.30M glycerin – no cells present 0.15M NaCl – normal sized cells 0.30M NaCl – crenated (shrunken and star-shaped) cells 0.15M glucose – no cells present 0.30M glucose – normal sized cells 0.30M Urea – no cells present Determine the osmolarity (hypoosmotic, isosmotic, or hyperosmotic) and tonicity (hypotonic, isotonic, hypertonic) of the following solutions.In which solutions did the osmolarity NOT match the tonicity? For those solutions, why did the osmolarity…a) mentioned the name of simple laboratory method to roughly estimate the concentration of anunknown protein