Shared Flashcard Set

Details

Biochemistry
Test 1
75
Biochemistry
Undergraduate 3
08/16/2013

Additional Biochemistry Flashcards

 


 

Cards

Term
When we talk about chemistry we have 2 type of forces we talk about:
Definition
Intermolecular Forces
Intramolecular Forces
Term
Intermolecular forces:
Definition
within a molecule e.g. covalent bond (C-C) usually
very strong bonds. Bond energy for a single bond=356kJ/mol. (C=C) is much
higher than a single bond.
Term
Intramolecular forces:
Definition
between two different molecules. they are forces that
exist between molecules, and they determine the physical properties of solids
and liquids. they keep molecules together.
Term
If there were no intramolecular forces
Definition
there would be no solids or liquids,
everything would be in a gaseous state. (things evaporate)
Term
Types of Intramolecular forces: weak compared to intermolecular forces
Definition
Van Der Waal Forces, Electrostatic Interactions, Hydrophobic effect, Hydrogen Bonds.
Term
Van Der Waal Forces:
Definition
are induced electrical interactions between atoms
or molecules that are close to each other.
It is a weak interaction. Energy associated with it is between 0.4-4.0 kJ/
mol.
Term
Electrostatic interactions:
Definition
A charged group on one molecule can attract
an oppositely charged group on another molecule.
It is a weak interaction
Term
Hydrogen bonds:
Definition
An intramolecular force in which a hydrogen atom
covalently bonded to a nonmetal atom in one molecule is simultaneously
attracted to a nonmetal atom of a neighboring molecule.
It is the most important intramolecular forces that we will come across.
Strongest hydrogen bonds are formed if the nonmetal atoms are small and
highly electronegative.
hydrogen bonds are seen in species containing N, O, and F. (because they
are really small and electronegative.
Term
In water molecule the electronegative
Definition
oxygen atom draws the electron
cloud towards it, as a result there is a partial negative over oxygen and a
partial positive charge around hydrogen atoms
Term
2 terms associated with hydrogen bonds:
Definition
Hydrogen Bond Donor
Hydrogen Bond Acceptor
Term
Hydrogen bond donor
Definition
group that includes both the H and the
electronegative atom to which it is covalently linked.
Term
Hydrogen bond acceptor-
Definition
is the electronegative atom that is linked less
tightly to the hydrogen bond.
Term
weak
Definition
Hydrogen bonds are __ interactions, energy range is from 4-20 KJ/mol
Term
Water
Definition
is the solvent in which most biochemical reactions take place.Properties of water are important for biochemistry, and most arise from its polar nature
Term
Because of the polar nature of water,
Definition
it is an excellent solvent for ionic
substances (because ionic substances are charged and water has both + & -
and will resolve them), non ionic but polar substances (e.g. sugars,alcohol,
amines, and carbonyl containing groups)
Term
Hydrophobic effects-3rd intramolecular force-
Definition
(something that does not like
water)- an intramolecular attraction that is seen in water. The non polar
molecules cannot participate in hydrogen bonding or ionic interactions, so
they do not interact with water molecules. so water molecules surround these molecules, they from a "cage" around it.
If another one comes, the water molecules will dissociate and the non polar
molecules will join together. (how lipids stack up which we will discuss later)
Term
water ionizes because
Definition
oxygen atom strips the electron from one of its
hydrogen atoms.
Term
Ionization of Water Mechanism:
Definition
1) H -- O -- H <--> H+ + OH-
2) the hydrogen ions are immediately hydrated to form hydronium (H3O+)
H+ + H2O <--> H3O+
Term
Dissociation of Water
Definition
at 25 degrees C 1L of water contains 1x10-7 moles of H3O+ and 1x10-7
moles of OH-.
1) H2O <---> H+ + OHequilibrium
constant (K)=
K= [products]/[reactants]=[H+][OH-]/[H2O]=(1x10-7)(1x10-7)/[H2O]
=(1x10-7)(1x10-7)=1x10-14
Kw=[H+][OH-]=1x10-14
Term
Kw=
Definition

[H+][OH-]=10-14

if you know either the [H+] or the [OH-] you can plug in and find the

other.

[H+][10-5]=10-14

[H+]=10-14/10-5

[H+]=10-9M

Term
pH
Definition

is the measure of hydrogen ions in a solution

pH= -log[H+]

e.g. if the [H+] in a solution is 10-9 find pH.

pH=-log(10-9)

pH=9

e.g. if a solution has 10-5M of [OH-], what is the pH?

Kw=[H+][OH-]=10-14

[H+]=10-14/10-5=10-9

Term
Strong electrolytes
Definition

they are substances that completely dissociate when

placed in an aqueous solution. e.g. NaCl, HCl.

NaCl <--> Na+ + Cl-

HCl + H+ ---> H3O+ + Cl-

HCl ---> H+ + Cl- (conjugate base)

H2O + H+ ---> H3O+ (conjugate acid)

K=[H3O+][Cl-]/[HCl][H2O]

because water's M is very high

Ka=[H3O+][Cl-]/[HCl]

since HCl dissociates completely, we remove it from the above equation.

Ka=[H3O+][Cl-]

[H3O+]=[HCl] initial

Term
Weak electrolytes
Definition

they are substances which partially dissociate in an

aqueous solution. e.g. acetic acid

since they only partially dissociate, it's much harder for us to determine the

pH.

pH.

CH3COOH + H2O <--> CH3COO- + H3O+

K=[CH3COO-][H3O+]/[CH3COOH][H2O]

we remove [H2O] since it's molarity is very high

Ka=[CH3COO-][H3O+]/[CH3COOH]=1.74x10-5M

(very small number and that it's does not dissociate well)

Term
Henderson-Hasselbalch Equation:
Definition

HA <--> H+ + A- dissociation of a weak acid.

pH = pKa + log [A-]/[HA] (should be MEMORIZED)

using this equation pH of a solution can be calculated, provided pKa, [A-],

[HA] are known.

e.g. calculate pH when 0.01M A- (congugate base) and 0.02M HA (acid)

are in a solution, pKa of the HA (acid) is 4.78

pH= pKa + log [A-]/[HA]

pH= 4.78 + log ( 0.01)/( 0.02)

pH= 4.78 + (-0.3)

pH= 4.48

another scenario, [A-]=0.01, [HA]=0.01

pH= pKa + log [A-]/[HA]

pH= 4.78 + log (0.01)/(0.01)

pH= 4.78

the pH is equal to the pKa when the concentration of the conjugate

base (A-) is equal to the acid (HA) in a solution.

Term
Titration
Definition

an analytical method used to determine the amount of acid in a

solution

Term
titration curve
Definition
is plot of the pH of the solution vs the amount of OH-
Term
Buffers
Definition

they are solutions that tend to resist change. They are made from

weak acid and its conjugate base.

are chosen based on how close to the pKa value is to the desired pH

e.g. pKa of acetic acid is 4.74.

it's good buffer from pH range 3.74-5.74 (+-1)

Term
Gibbs free energy change tells us:
Definition

if the rxn will proceed or not.

For the rxn:

^G = ^H -T^S

Term
Free energy change (^G)
Definition

is related to equilibrium constant for a rxn

A +B <--> C + D

^G = ^G' + RT ln [C][D]/[A][B] - Keq

^G= free energy change

^G'= standard free energy change --> is free energy change under

standard conditions

R= gas constant

T= Temperature in Kelvin

^G''- for biochemical reactions, the standard free energy change at pH 7

is denoted by ^G''

if ^G is negative (-) the rxn is spontaneous (don't need to provide energy

for the rxn to proceed).

if ^G is positive (+) the rxn is non spontaneous (needs energy) if ^G = 0, it rxn is at equilibrium

Term

e.g. the equilibrium constant at 54.5'C is 0.27, calculate ^G' and answer if this

rxn is spontaneous or not.

Definition

^G'= -RT ln keq

^G'= (-8.314)(54.5+273) ln(0.27)

^G'= 3.5KJ/mol

Term
What is the effect of concentration on change in free energy?
Definition

Phosphocreatine + H2O --> creatine + phospate ^G' = 42.8 KJ/mol

what happens if the concentration of reactants and products are 0.001M temp

31 degrees C ?

^G = ^G' + RT ln keq

^G = -42.8 KJ/mol + 8.314 J/mol*K * 301K ln (0.001)

^G= -42.8KJ/mol + (-17.8 KJ/mol

^G= -60.5 KJ/mol

- so it is spontaneous

keq= [creatine][phosphate]/[phosphocreatine]

keq= (0.001)(0.001)/0.001

keq= 0.001

there is a difference of -17 so concentration does play a factor

 

Term
Proteins
Definition

are very versatile macromolecules in living systems and they have

crucial function in essentially all biological processes

 

Term
Some of the functions of proteins are:
Definition

Term
proteins are polymers built of monomer units called
Definition
amino acids
Term
proteins can spontaneously fold up into
Definition

three dimensional structures, and the

function of a protein is dependent on its three dimensional structure.

Term
Amino Acids
Definition

consist of a central carbon atom (alpha carbon) linked to amino

group , a carboxylic group, a R group, and a hydrogen atom

this is the backbone of amino acids, and this is the same for all amino acids,

only the R group changes


Term
since there are 4 different groups connected to the alpha-carbon
Definition

amino

acids are chiral and they may exist in L or D isomer

‣ amino acids found in proteins are L-isomes, except few exceptions

Term
Amino Acid is very
Definition
polar and charged molecule
Term
at pH 7 they exist as
Definition
ziwetterions (dipolar ions)
Term
what if the above molecule is in pH 1?
Definition

the pka tells you that pka=pH when half of the H molecules has

dissociated (chart/graph)

everything will remain the same • except for the COO- because we are

below pH 2.3 the H remains and does not dissociate

pka (2.3) > pH (1)-- H does not dissociate

Term
Isoelectric point
Definition
it is the pH where the net charge is 0
Term
in order to find the isoelectric point
Definition

‣ consider various charge forms of the molecule

‣ find the isoelectric form

‣ take average of 2 pkas immediately on either side of the isoelectric form

Term
hydrophobic group
Definition

9 amino acids

• glycine-Gly-G

• alanine-Ala-A

• valine-Val-V

• leucine-Leu-L

• isoleucine-Ile-I

• methoionine-Met-M

• tryptophan-Trp-W

• phenlyalanine-Phe-F

• proline -Pro-P

Term
Polar uncharged group
Definition

• serine - Ser-S

• threonine - Thr-T

• tyrosine - Tyr-T

• cystine- Cys-C

• asparagine - Asn- N

• glutamine - Gln - Q

Term
Polar charged (acidic)
Definition

• aspartic acid - Asp- D

glutamic acid - Glu- E

Term
Polar charged (basic)
Definition

• lysine - Lys- K

• arginine - Arg - R

• histidine- His- H

Term
Glycine
Definition

Hydrophic group

Gly

G

Term
Alanine
Definition

Hydrophobic group

Ala

A

Term
Valine
Definition

Hydrophobic Group

Val

V

Term
leucine
Definition

Hydrophobic Grouo

Leu

L

Term
Isoleucine
Definition

Hydrophobic Group

Ile 

I

Term

Methoionine

 

Definition

Hydrophobic Group

Met

M

Term
Tryptophan
Definition

Hydrophobic Group

Trp

W

Term
Phenyalanine
Definition

Hydrophobic Group

Phe

F

Term
Proline
Definition

Hydrophobic Group

Pro

P

Term
Serine
Definition

Polar Uncharged Group

Ser

S

Term

Threonine

 

Definition

Polar Uncharged Group

Thr

T

Term
Tyrosine
Definition

Polar Uncharged Group

Tyr

T

Term
Cystine
Definition

Polar Uncharged Group

Cys 

C

Term
asparagine
Definition

Polar Uncharged Group

Asn

N

Term
glutamine
Definition

Polar Uncharged Group

Gln

Q

Term
Aspartic Acid
Definition

Polar Charged (acidic)

Asp

D

Term
Glutamic Acid
Definition

Polar charged (acid)

Glu

E

Term
Lysine
Definition

Polar Charged (basic)

Lys

K

Term
Arginine
Definition

polar charged (basic)

Arg

R

Term
Histidine
Definition

polar charged (basic)

His

H

Term
Primary Structure of Proteins
Definition
amino acids • are linked by peptide bond
to form polypeptide chains. In peptide bond an alpha-carboxyl group of an
amino acid is covalently linked to amino group of another amino acid
Term
The formation of peptide bond is accompanied by
Definition
the loss of water
Term
Series of amino acids joint together by the peptide bond form the
Definition
polypeptide chain
Term
residue
Definition
each amino acid in a polypeptide is also called a __
Term
Amino end carboxyl
Definition
By convention __ __ is at the beginning (left side) of the chain and the ___ at the end (right side).
Term
Peptide bond has
Definition
partial double bond characteristics
drawn as a single bond
the presence of resonance forms in peptide bond
• the bond length of typical C--N is 0.145nm
• the bond length of typical C=N is 0.125nm
• the peptide bond length is 0.133nm
falls between the single and double bond length
Term
because of this partial double bond characteristic,
Definition
another feature of amino acids is restricted at the peptide
bond.
restriction of free rotation around the peptide bond due to its partial
double bond nature
Term
peptides can be classified into:
Definition
dipeptide- two amino acids joined by peptide bonds
oligopeptide- 12-20 amino acids joined by peptide bonds
polypeptide- more than 20
‣ most are here
Term
disulfide bond
Definition
two cysteins can react to form a __ __.
covalent bond that is found in proteins, it provides stability to
proteins.
Supporting users have an ad free experience!