Equilibrium Phase Analysis
Response to question 5 Part A i) The three phases A, B and C represents the Lag, Extension and the Equilibrium phase. In the Lag phase, the actin filaments start to polymerize. The lag phase is highly unfavourable but once formed, it proceeds rapidly to the next phase. This is the rate limiting step. In this phase, a small unstable actin filament called the ‘nucleus/seed’ is formed. The nucleus is made when one actin monomer (G-actin) interacts with two other monomers and forms a triple monomer attached actin filament. Only when this nucleus is formed, the polymerization can proceeds to the next step. In the Extension phase, the actin monomers are added to the nuclei and the filament (F-actin) increases in the length. The monomers are added …show more content…
In this, as the monomers are added an equal number f monomers are removed. The filament grows rapidly in one end and slowly in the other. This equilibrium concentration of the monomer is called the critical concentration (Cc). Above Cc the G-actin polymerises and below this the F-actin will depolymerise. The rate of addition of the monomers is high at the +ve end compared to the –ve end. So the filament grows at the =ve ends while the monomers are removed at the –ve end, there by maintain the equilibrium. (Lodish, et al., 2000; Young, Lecture …show more content…
The only difference seen is in the growth of the filaments. Under normal condition addition of actin monomers is seen in both the ends while with cytochalasin it is seen only in the – end. ii) The structure of the actin monomer in the free and when attached to the actin filament is different. This conformation change is seen due to the hydrolysis of ATP to ADP. Actin monomer is attached to ATP. When it attaches to the filament, the filament is a slow ATPase and it hydrolyses the ATP to ADP. Two loops in the monomer are involved with ATP. The Ser14 β-hair loop and the His73met containing sensor loop. The Ser14 is attached to the His 73 and the γ-phosphate of the ATP through an H-bond. When hydrolysis takes place, the Ser-14 creates a new H-bond with the β-phosphate and the His73 from the sensor loops is moved to the space emptied by the γ-phosphate. As a result, there is a conformational change of the whole monomer seen and this leads to a decreased stability of the actin filament in the ADP bound state (Dominguez & Holmes,
Unit 4 P4 Research Paper
1903 Words | 8 PagesEach actin molecule has a myosin-binding site where a myosin head can bind during the process of the sliding filament theory. Myosin is a protein that generates the force in a muscle contraction. Tropomyosin is a long strand. It loops around the actin chains in the thin filament. It covers the myosin binding site of the actin and tropomyosin molecules and prevents muscle
G1 Unit 3 Stages Essay
549 Words | 3 Pagesthree phases G1, where the cells grows up to double it’s original size, S phase, where the dan is replicated , and G2 ,where the cells finishes it growing and prepares to go into prophase. Prophase is where the cell’s nuclear membrane dissolves. Chromatin tightly coils and condenses into chromosomes. Spindle fiber begins to appear and then the cell goes on to metaphase. During metaphase, the cell’s spindle fibers attach to the chromosomes and the chromosome aline in the middle of the cell.
Solute To Dye Synthesis Lab Report
940 Words | 4 PagesFiona Young Ha Hoang and Joey Lu 12/11/15 Malik AP Chem 4th Prepare to Dye Introduction Chromatography is the separation of a mixture or substance by putting it in a solute with chromatography paper. Following with this lab, we take 3 colors of food dye (red, yellow, and blue) and test which solvent out of distilled water, acetone, ethanol, and 2-propanal would separate the molecules in the dyes the best.
Anti Cow Serum Lab Report
1027 Words | 5 PagesAs a result, the glycine keeps pushing the protein towards the chloride ion. In other words, the proteins are trapped between glycine and chloride ion. The proteins form a very tight band inside the stacking gel. Once the protein reaches the resolving gel, the pH changes from 6.8 to 8.8 and the pores are smaller. As pH increases, the N-terminal amino groups are deprotonated.
Planarian Worm Lab
557 Words | 3 PagesThe “tail” segment measured initially at six millimeters and showed little signs of movement. Throughout the two week observation period, the “tail” segment did not grow at all and showed very few signs of vitality, but by the second week, a new head had started to form on the “tail” segment. Comparing the results of the experiment to my initial hypothesis, I was incorrect, the “head” segment grew more than the “tail” segment, although not by much. There could have been some error with the measurements because the tail segment did not really move at all and tended to shrink up
Enzyme Lab
901 Words | 4 PagesThe enzymeʼs have an active site that allows only certain substances to bind, they do this by having an enzyme and substrate that fit together perfectly. If the enzyme shape is changed then the binding
Horseradish Peroxidase Lab Report
1090 Words | 5 PagesThe products are released from the enzyme surface to regenerate the enzyme for another reaction cycle. The active site has a unique geometric shape that is complementary to the shape of a substrate molecule, similar to the fit of puzzle pieces.
Slipknotted Proteins Lab Report
873 Words | 4 PagesWang et al performed SMFS on a shallow trefoil knot protein, bovine carbonic anhydrase B, and stretched it to a tightened knot.(110) A figure-eightknotted protein, phytochrome, was stretched by Bornschlogl et al using SMFS based on atomic force microscopy (AFM) as well as SMD simulations.(106) The unfolding force of phytochrome was determined to be ~ 70 pN, which is not as high as many mechanically stable proteins such as I27 domain of human titin (~200 pN). In addition, both their experimental and simulation results revealed that the tightened figure-eight knot contains 17 to 19 amino acid residues as shown in Figure 1.11. Further discussion about the tightening of the knot can be found in chapter
Esophagus Model Of Contraction
723 Words | 3 PagesThese cross bridge attachments form and break several times during a contraction, tension and propel the thin filaments toward the
Laboratory Report on Enzyme Activity
1407 Words | 6 PagesI predicted the sucrase activity with increase the sucrose concentration which is correct! Application 1. Myosin ATPase is an enzyme that is involved in muscle contraction. Athletes do warm-up exercises prior to athletic performance. Explain why warm-up exercises increase myosin-ATPase
B-Galactosidase Lab Report
1764 Words | 8 PagesHowever, all proteins are constructed from the same set of 20 amino acids linked in unbranched polymers. The covalent bond that exists between amino acids is called peptide bond, hence a polymer of amino acids is named polypeptide. A protein is a biological functional molecule made up of one or more polypeptides which is folded and coiled into unique three-dimensional structure. In laboratory, it is important to measure the concentration of proteins for research investigations. Biuret test is adopted to quantify proteins in fluid by using a spectrophotometer.
Essay On Muscle Contraction
1506 Words | 7 PagesDuring ATP hydrolysis the enzyme ATPase uses water to cleave a phosphate from ATP producing ADP and a free phosphate which remains attached to the myosin head. The energy that was released from breaking the chemical bond is used to move the myosin head into position for attachment to the actin molecule. Step two of the contraction cycle is Cross-Bridge formation. During cross bridge formation the myosin head attaches to the revealed myosin-binding site on actin forming a cross bridge between the two protein molecules. Step three of the contraction cycle is the power stroke.
Meat Tenderizer Lab Report
898 Words | 4 PagesHypothesis: If we add pineapple and meat tenderizer to the gelatin, then it will not congeal. Materials needed: Gelatin, Fresh and canned pineapple, Meat tenderizer, Beakers, Cold and boiling water, a timer, 4-5 bowls, 4-5 test tubes and a rack, and a few spoons. STEPS Step 1.
Macromolecules Research Paper
1364 Words | 6 PagesTertiary structure is the "worldwide" collapsing of a solitary polypeptide chain. A noteworthy main impetus in deciding the tertiary structure of globular proteins is the hydrophobic impact. The polypeptide chain overlap such that the side chains of the non-polar amino acids are "covered up" inside the structure and the side chains of the polar buildups are uncovered on the external surface. Hydrogen holding including bunches from both the peptide spine and the side chains are imperative in balancing out tertiary structure. The tertiary structure of a few proteins is balanced out by disulfide bonds between cysteine
More about Equilibrium Phase Analysis
Unit 4 P4 Research Paper
1903 Words | 8 PagesG1 Unit 3 Stages Essay
549 Words | 3 PagesSolute To Dye Synthesis Lab Report
940 Words | 4 PagesAnti Cow Serum Lab Report
1027 Words | 5 PagesPlanarian Worm Lab
557 Words | 3 PagesEnzyme Lab
901 Words | 4 PagesHorseradish Peroxidase Lab Report
1090 Words | 5 PagesSlipknotted Proteins Lab Report
873 Words | 4 PagesNt1310 Unit 1 Lab Report
1125 Words | 5 PagesEsophagus Model Of Contraction
723 Words | 3 PagesLaboratory Report on Enzyme Activity
1407 Words | 6 PagesB-Galactosidase Lab Report
1764 Words | 8 PagesEssay On Muscle Contraction
1506 Words | 7 PagesMeat Tenderizer Lab Report
898 Words | 4 PagesMacromolecules Research Paper
1364 Words | 6 Pages