BMS02-1005 & 1049 (Amino Acid, Protein & Protein Structure)

Description

BMS02 - Molecules and Cells Flashcards on BMS02-1005 & 1049 (Amino Acid, Protein & Protein Structure), created by Evian Chai on 29/04/2020.
Evian Chai
Flashcards by Evian Chai, updated more than 1 year ago
Evian Chai
Created by Evian Chai about 4 years ago
2
0

Resource summary

Question Answer
What determines the properties of amino acids? The R group
All amino acids (except glycine with H R group) are .... with a ... center They are optical isomers meaning Asymmetrical Chiral carbon they are nonsuperimposable mirror images
What are the four groups attached to the carbon on a Amino Acid? 1. Carboxyl group COOH 2. H group 3. Amino Group NH2 4. R group
The isoelectric point is The pH where the AA carries no charge
How are amino acids joined together? By a condensation reaction between the amino group of one and carboxyl group of another Forms a peptide bond(covalent)
In a polypeptide, amino acids are made at the ... terminus and joined at the ...terminus 1. N (amino) 2. Carboxyl
Functions and examples of proteins 1) ... - Collagen - Keratin 2) ... - Actin - Myosin 3) ... - Trypsin - DNA polymerase 4) ... - Haemoglobin 5) ... - Na+/K+ pump 6) ... - Insulin 7) ... - ACh receptors (nicotinic & muscarinic) 8) .... - Antibodies - Clotting factors 9) ... - Histones 10) .... - Tubulin 1. Structural 2. Movement 3. Enzymes/catalysts 4. Transport 5. Membrane transport 6. Hormones 7. Receptors 8. Defense 9. Gene regulating 10. Chromosome sorting
The primary structure is the 2D Linear sequence of amino acids joined together by peptide bonds
Secondary structure is caused by Alpha helix is caused by bonds between.... Side chains are located... Beta sheet is caused by bonds between.... side chains are located... Hydrogen bonding between peptide bond of C=O and N-H every 4th peptide on the outside adjacent polypeptides above and below plane of each sheet (alternate)
Fibrillar proteins have more...amino acids while hemoglonbins have more... beta sheet for strength/little elasticity Alpha helix
Tertiary structure folding is mainly dependant on .... The shape determines? The three types of bonds are? Hydrophobic portions folding in The function of the active site 1. H bonds 2. Covalent Disulphide bridges 3. Ionic bonds
Quaternary structure is 2+ polypeptides linked together via same forces as tertiary structure
Structure of collagen? Right handed TRIPLE helix Contains modified aa (hydroxylysine etc.)
Scurvy is caused by... This impacts 1. Deficiency in VIT C 2. The stability of the triple helix of collagen
How does oxygenation affect hemoglobin and its R group pKa? Its pKa DECREASES so it becomes a stronger acid
Show full summary Hide full summary

Similar

BMS02-1003 (Lipids & Membranes)
Evian Chai
BMS02-1008 - Movement of Ions and Molecules in the body
Evian Chai
BMS02-1006- pH and buffering
Evian Chai
BMS02-1010 Enzyme Kinetics
Evian Chai
BMS09-1014 - Bone Development and Ossification
Evian Chai
BMS10-1017 - Blood Cells: RBC WBC and platelets
Evian Chai
BMS03-1016 Organisation of the Nervous System)
Evian Chai
BMS11-1039 - Pharmacology of diuretics
Evian Chai
BMS07-1026- Glucose and Glycogen metabolism
Evian Chai
BMS03-1022- A pharmacological perspective of the autonomic nervous system
Evian Chai
BMS14-1062 - Histology of endocrine glands
Evian Chai