Chemistry Final Part 2
2nd semester (1st year)
2nd semester (1st year)
Set of flashcards Details
Flashcards | 72 |
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Language | English |
Category | Chemistry |
Level | University |
Created / Updated | 11.05.2017 / 16.01.2024 |
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Explain how the secondary structures occur in protein:
The peptides of the primary structure folds and align themselves in such manner that certain patterns repeat themselves.
These repeating patterns are secondary structure
What are the different types of secondary structure:
Alfa helix or beta pleated
What bond keeps the helical structure of a protein together:
Hydrogen bonds
Where can the Beta pleated sheet occur in proteins:
When the polypeptide chain runs parallel
Describe how the tertiary structure of proteins form and what bonds holds it together:
Forms when the elements of the secondary structure fold
Non-covalent bonds Disulphide bond, hydrogen bonds and salt bridges
Give an example of a quatenary protein:
Hemoglobin
In what 2 groups can proteins be divided into and how does their structure look like:
Globular proteins and fibrilar protein
GP: Folded into compact structure
FP: In an extended form
Give some examples of globular proteins:
Hemoglobin, immunoglobulin, myoglobin, cytokines
What factor is important in Heparin’s pharmacological effect:
The pharmacological effect depends on the length of heparin chain.
Only heparin molecules containing more than 8 disaccharides units are active.
Inhibition of Xa factor: 8-18 disaccharide units
Inhibition of Xa factor and thrombin: 18-X
What kind of patients does Heparin have a positive effect on:
Post-surgical patients and in treatment of patients with vascular disorders
What is Heparin sulfate:
Heparin sulfate has more variable composition with less sulfate groups and more acetyl group
What is Hyaluronic acid and what makes it different from their GAG’s:
Component of extracellular matrix, vitreous humor of the eye, and synovial fluid. Also present in bacteria . It binds cations: Ca+, K+ and Na+ tightly.
The one GAG not found in the sulfated form.
What is chondritin:
Major component of cartilage and other connective tissue
Chondroitin A (sulfate gr. At C4) and Chondroitin C (C6)
What is dermatan sulfate:
Component of skin
Mainly consist of L-iduric acid 80-90 % and D-glucoronic acid 10-20%
Explain what heteroglycans of glycoproteins are and what molecules belong to this group:
Complex molecules called glycoproteins
Proteoglycans, N-glycoprotein, and O-glycoproteins
Explain what proteoglycans are:
Special class of glycoproteins that have a protein core and a long polysaccharide chain of acidic polysaccharides named glucosaminoglycans
What kind of bonds can be found between the glycans and the proteins?
Glycosidic bond in N or O glycoproteins
In what groups can the sugar part of O-glycoproteins be divided into:
Monosaccharide, disaccharide, triasaccharide or tetrasaccharides
In what groups can heteroglycans be divided into:
Glucosaminoglycans, glycans of glycoproteins, or glycans of glycolipids
Where can GAGs be found in the human body:
Intracellular spaces connective tissue, skin, cartilage and blood vessels.
Together with elastic fibers are embedded in a gel-like extracellular matrix.
Heparin is an exception occurs on the interior of the cells
Write down the properties of GAGs:
Negatively charged and acidic due to presence of either a sulfate group or a carboxylate group.
Solutions of GAGs are called colloids slimy, mucus like consistency due to the high viscosity and elasticity
In what way can gags be linked to other substances? Give example of this:
Glycosidic-bonds: GAGs-Proteins called proteoglycans
Give some examples of GAGs:
Hyaluronic acid, Heparin, Heparan sulfate, Dermatan sulfate, Keratan, and Chondritin A, C
What is Heparin and why is it different from other GAGs?
Not constituent of connective tissue.
Non-structural role
Synthesized and stored in the intracellular granules of mast cells of the arterial walls, lungs, and skin.
What is the function of Heparin:
Body’s natural anticoagulant, and prevents clotting of blood and is released.
Place of collage occurence:
Extracellular matrix of connective tissue. Mostly found in fibrous tissue, such as tendons, ligaments, and skin.
Structure of tropocollagen
Helical structure consisting of three polypeptide chains coiled around each other to form a spiral and stabilized by interchain bonds.
Forces maintaining the three-dimensional structure of collagen
Cross linkage:
Joining 2 or more collagen chains together at the end of polypeptide chain. Interchain linkage: Linking collagen together to make them less elastic and more stable.
Forces maintaining the three-dimensional tertiary structure of globular protein:
Hydrophobic forces, disulphide bonds and salt bridges
Give the normal concentration of glucose in human blood:
80-100 mg/dl
Write a complex structure, which is composed from glycerol, phosphate, choline and 2 molecules of fatty acids. Name chemical bonding between the glycerol and phosphate. Mark hydrophobic and hydrophilic parts:
Lecithin, ester bond, fatty acid hydrophobic (non-polar) Ester-bond
Explain what a glucosaminoglycans (GAG) is and how many dissacharide units makes up the molecule. Also write down its approximate molecular weight:
A GAG is a nagatively charged, large polymer of repeating disaccharide units.
250-25.000 units
20-1000 kDa