Flashcards
biomolecules
Cards in this deck (23)
- 1define biomoleculesoptically active polyhydroxy derivatives of aldehydes and ketones
- 2classification of carbohydrates on hydrolysismono- cant be hydrolyzed to give simpler units eg- glucose, fructose, ribose
oligo-give 2 mono units eg-sucrose, maltose
poly-large no. of mono eg- starch, cellulose - 3classification of carbohydrates on taste1. sugar- sweet
1.1reducing-reduces tollen and Fehling eg- all mono
1.2 non-reducing not reduce tollen and fehling eg- maltose and lactose - 4glucose preperation1. hydrolysis of sucrose
2. commercially from starh - 5structure of glucose1. linear 6c chain:HI
2.carbonyl grp:hcn/nh2oh
3.aldehyde grp:br2-h20
4.5-oh grps:acetic anhydride
5.1 oh 1 degree:hno3 - 6reaction not explained by open chain structure1. not give schiffs test (has-cho)
2. no H2S addition product formed
3. pentacetate doesn't react with hydroxylamine(absence of free -cho)
4. 2 different crystalline structures alpha beta - 7anomersstructures exactly similar except position of -oh at c1
- 8glucose an dsucrose are soluble in water but cyclohexane and benzene are noth bonding in other h bonding absent weak dipole interations
- 9amino acidsbiomolecules containing amines and acids
- 10classification of amino acids1. relative position of -cooh and -nh2
2. relative no. of nh2+cooh
3. requirement(essential, non-essential) - 11examples essential and non-essentialessential- valine, luecine, isoluecine,lysine
non essential- glycine, alanine, aspartic acid, proline - 12zwitter iondipolar neutral with both positive and negative charge amphoteric
- 13peptide bondsconnect amino acids together, the linkage is an amide formed b/w -cooh and -nh2
- 14protein classification1. fibrous- parallel and held together by hydrogen disulfide bonds. insoluble in water eg- keratin(hair), myosin(muscle)
2. globular- polypeptides coil to give spherical shape. soluble in water. eg- insulin and albumin. - 15primary proteincontains one or more polypeptide chains .each chain has amino acids linked in a specific sequence, anychange in sequence results in a different protein
- 16secondary proteinSHAPE gen 2 alpha helix and beta pleated
DUE TO regular folding of the backbone of polypeptide chain+h bond+peptide bond - 17alpha helix beta-pleated1. twisted into a right-hand helix
2. stretched out max. extension, laid side by side and held together by intermolecular h bond - 18tertiary proteinoverall folding of the polypeptide chain, further folding of the 2 structure
gives 2 major shapes fibrous and globular
FORCES- h-bond, disulfide linkage, vanderwaal, electrostatic - 19subunits quarternary proteinproteins composed of 2 or more polypeptide chains
the spatial arrangement of the subunits with respect to each other - 20denaturationwhen a native protein is subjected to a physical change(temp) or a chemical change(pH) the h bonds are disturbed. globules unfold and helix uncoiled. protein loses its biological activity.
primary structures remain intact 2 and 3 destroyed - 21denaturation example1. the coagulation of egg white on boiling
2. curdling of milk - formation of lactic acid in milk - 22the yield on complete hydrolysis of DNApentose sugar+phophoric acid+nitrogen containg heterocylcic compounds(bases)
- 23isoelectric/ eutectic pointthat pH at which amino acid neither migrates towards cathode nor anode
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- XII Chemistry Flashcards on biomolecules, created by Jiya Chaki on 15/02/2021.
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- Jiya Chaki
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