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Lecture 9

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Total cards: 24•Content version: v4•Public deck•Updated: 8/1/2026

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#1
Front (Question)

What is the structure of an AA?

Back (Answer)

central C attached to Amino group, R group and Acrboxylic acid group

#2
Front (Question)

What % of C,O,N,H,S is in proteins?

Back (Answer)

Carb 50% O 22% N 16% H 7% S little

#3
Front (Question)

What is protein condensation?

Back (Answer)

When 2 AA come together, carboxylic acid and AA from 2 different groups come together and release 1 molecule of water to form a dipeptide

#4
Front (Question)

What is the bond that connects 2 AAs?

Back (Answer)

Peptide bond is the bond between the AA

#5
Front (Question)

What is a hybrid or twitter ion?

Back (Answer)

AA that is ampthoteric -AA can carry +/- charge at the same time on same molecule

#6
Front (Question)

What happens to a twitter ion when pH increases or decreases?

Back (Answer)

Low ph will appear in acid form -net charge + Increase ph go to basic form -net chargee is -1

#7
Front (Question)

What are the characteristics of acid coagulation of casein?

Back (Answer)

Fresh Milk  pH ~ 6.6  “Colloidal Suspension” Net Negative Charge on Casein Add Acid Coagulation (Protein Denaturation) Iso-electric point of casein: PI = 4.6 net charge = 0

#8
Front (Question)

What situation would be desireable/undesireable use of acid coagulation of casein?

Back (Answer)

Desireable if you want yogurt you want coagualtion of casein or in cheese Undesirable curdling of milk in a smoothie

#9
Front (Question)

What are the uncharged R groups of AAs?

Back (Answer)

Serine Threonine Cysteine Glyceine

#10
Front (Question)

What are the negatively charged AAs?

Back (Answer)

Aspartate Glutamate

#11
Front (Question)

What is the one positively charged AA?

Back (Answer)

Lysine

#12
Front (Question)

What are the non polar R groups?

Back (Answer)

Methionine Phenylalanine Alanine Valine

#13
Front (Question)

What are the essential AAS?

Back (Answer)

Valine Leucine Isoleucine Phenylalanine Tryptophan Lysine Arginine Histidine Methionine Threonine

#14
Front (Question)

What are the R groups for Gly, Asp, Set, Lys, Ala, Phe, Cys, Glu?

Back (Answer)

Gly: R= H Asp: R = CH2COOH Ser: R = CH2OH Lys: R = CH2-CH2-CH2-CH2- NH2 Ala: R = CH3 Phe: R = CH2=Benzene ring Cys: R = CH2SH Glu: R = CH2-CH2-COOH

#15
Front (Question)

What is the Pka?

Back (Answer)

PKA: Ph at which you have equal amount of acid and base pH at which [Acid] = [Base]

#16
Front (Question)

What is the isoelectric point?

Back (Answer)

Ph when net charge on protein is 0 PI = PKa1 + PKa2/2

#17
Front (Question)

How can you calculate the pH if you only know the Pka and acid base concentrations?

Back (Answer)

PH = Pka + log [A-]/[HA] HA>H+ + A- HA = ACID A- = BASE

#18
Front (Question)

What is the primary structure of proteins ?

Back (Answer)

AAs joined by peptide bonds

#19
Front (Question)

What are the factors that fact the physical/chemical properties of proteins?

Back (Answer)

Peptide bonds R-groups Type of AA Sequence of AA

#20
Front (Question)

What is the secondary structure of protein ?

Back (Answer)

α-helix Collagen helix Beta Pleated sheet Held together and maintain structure by : • S-S • H-Bond

#21
Front (Question)

What is the tertiary protein structure?

Back (Answer)

Results from folding of 2o structure on itself Maintained by: • H bond • S-S • Ionic Bond

#22
Front (Question)

What is the quaternary structure?

Back (Answer)

Protein consisting of more than one amino acid chain

#23
Front (Question)

What are the 2 kinds of proteins?

Back (Answer)

Globular Protein >Myoglobin *Protein helix is folded back on itself Fibrous Protein > Collagen *Extended polypeptide chain

#24
Front (Question)

What is the nutrition breakdown of egg yolks?

Back (Answer)

(30% Fat, 18% Protein, 50% Water) Lipids Protei: -Lipoprotein (Lipovittellin): Emulsifying property -Non-Lipoprotein (Phosvitin): High in P