Ch.1:Principles of biological structure Flashcards

Question

what are 2 major physiological buffers? what do they each regulate? ph of the cytoplasm is maintained by what?

Answer 1

carbon dioxide-bicarbonate system which manages blood ph and he phosphate system which regulates cytosolic pH buffers: weak acids and bases

Answer 2

The larger the Ka value, the more dissociation of the molecules in solution and thus the stronger the acid.

Answer 3

you want the buffer to work in a region where it is a most risk

Answer 4

blood pH drops below 7.35; monitore [HC03] AND [CO2]

Answer 5

carbon, carboxyl, and amino acid and R group at physiological pH: COOH is deprotonated NH2 is protonated to NH3 L (L= life)

Answer 6

Arg, R | arrrrginine

Answer 7

Asp, D | cleopatra Died with an asp

Answer 8

gln, Q Qutamine (cuteamine)

Answer 9

glu, E Glue-tamic acid

Answer 10

lys, K just remember

Answer 11

Phe, F FFFFenylalanine

Answer 12

Thr, T Just remember

Answer 13

Trp, W phan gang

Answer 14

Tyr, Y Tyyyrosine

Answer 15

alanine, methionine, valine, phe, tyrosine, isoleucine, leucine, tryptophan, WAVY FILM

Answer 16

Aspargine Serine Threonine Quest Histidine Lysine Arginine glutamate aspartate New Set by Tribe Called Quest His Lys Arg Basic Hey Mate, you're an asshole

Answer 17

cysteine- can make sulfide bonds glycine- smalles aa and can affect structure and disrupt helix proline- forms unique folded structure that is rigid and can inhibit folding

Answer 18

can shift from positive charge to uncharged in response to small changes in the pH of the environment. at pH 5.8 it is positively charged on the N and in ph 7.8 it is not charged.

Answer 19

charged (-) , except lysine and arginine will have (+) at physiological pH

Answer 20

acid- donates protons or accepts electrons base-accepts protons, donates electrons

Answer 21

The half-neutralization point, where [HA] = [A¯] and therefore pka=ph

Answer 22

The cationic form (the conjugate acid), because at all solution pH values below the pKa the conjugate acid is in excess

Answer 23

6.1; – at this pH, half of the acid molecules will be dissociated. blood pH is 7.4

Answer 24

made of Ch2/ch3 groups. except methionine has a Sulfur. The others have rings.

Answer 25

Try Trippin with Phenytoin Tyrosine Tryptophan Phenilalanine

Answer 26

basic, acidic, or polar with uncharged R group

Answer 27

Asparagine (N) Serine (S) Threonine (T) Glutamine (Q) New Set by Tribe called Quest

Answer 28

``` the movie shallow HAL has a positive image histidine arginine lysine positive charge at physiological pH ```

Answer 29

hey mate, you're an asshole glutamate aspartate

Answer 30

no because it is charged at ph=5.8 and at 7.8 it is uncharged

Answer 31

At pH >> pKa, the ionizable group will be deprotonated. For carboxylic acids, this means that the group will be negatively charged; amines will be neutral. At pH << pKa, the ionizable group will be protonated. For carboxylic acids, this means that the group will be neutral; amines will be positively charged.

Answer 32

The protonation state of a functional group, such as a side-chain carboxylate or an α-amino group, can be determined by comparing the pKa of the functional group to the pH of the solution. If the pH is below the pKa, the group will be largely protonated; if the pH is above the pKa, the group will be largely deprotonated, and if the pH is near the pKa, the group will exist as a mixture of the two forms.

Answer 33

1) The notion of polarity is REALLY important, particularly when we are talking about the properties of amino acids. The distribution of electrons in the building blocks of proteins can have dramatic effects on how proteins fold, which ultimately determines their function. 2) also important because they allow hydrogen bonds to form.The ability to form hydrogen bonds with water dictates the solubility of a molecule. Those that readily dissolve are refered to as hydrophilic or "water-loving".

Answer 34

, so it can form hydrogen bonds with itself and with hydrophilic molecules including alcohols, amines, esters and peptide groups

Answer 35

Due to the polar nature of the water molecule, it is able to readily form ionic or electrostatic interactions. In essence, the ions are surrounded by a hydration shell of water molecules. The ability of water to interact with charged atoms reduces the ability of these charged species to interact with each other and can weaken the strength of ionic bonds between biomolecules.

Answer 36

We can even see water influencing nucleic acid structure where the double stranded DNA forms an interior surface with hydrogen bonds formed between the bases of the two strands. The interior region of the molecule (where the hydrogen bonds are located) limits access to the aqueous environment and enables stronger hydrogen bonds to form.

Answer 37

For this buffer, carbonic acid (H2CO3) is the proton donor and bicarbonate (HCO3-) is the proton acceptor.

Answer 38

tyrosine, threonine, and serine STY

Answer 39

Correct answer = D. The two cysteine residues can, under oxidizing conditions, form a disulfide bond. Glutamine’s 3-letter abbreviation is Gln. Proline (Pro) contains a secondary amino group. Only one (Arg) of the seven would have a posi- tively charged side chain at pH 7.

Answer 40

A A. The peptide bond has a partial double-bond character. Unlike its compo- nents—the α-amino and α-carboxyl groups—the –NH and –C=O of the peptide bond do not accept or give off protons. The peptide bond is not cleaved by organic solvents or urea, but is labile to strong acids. It is usually in the trans configuration.

Answer 41

if the primary disturbance is respiratory, the secondary compensatory mechanism must be metabolic. • if the primary disturbance is metabolic, the secondary compensatory mechanism must be respiratory.

Ch.1:Principles of biological structure Flashcards

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