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When we talk about chemistry we have 2 type of forces we talk about: |
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Intermolecular Forces Intramolecular Forces |
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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. |
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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. |
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If there were no intramolecular forces |
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there would be no solids or liquids, everything would be in a gaseous state. (things evaporate) |
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Types of Intramolecular forces: weak compared to intermolecular forces |
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Van Der Waal Forces, Electrostatic Interactions, Hydrophobic effect, Hydrogen Bonds. |
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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. |
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Electrostatic interactions: |
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A charged group on one molecule can attract an oppositely charged group on another molecule. It is a weak interaction |
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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. |
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In water molecule the electronegative |
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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 |
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2 terms associated with hydrogen bonds: |
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Hydrogen Bond Donor Hydrogen Bond Acceptor |
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group that includes both the H and the electronegative atom to which it is covalently linked. |
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is the electronegative atom that is linked less tightly to the hydrogen bond. |
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Hydrogen bonds are __ interactions, energy range is from 4-20 KJ/mol |
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is the solvent in which most biochemical reactions take place.Properties of water are important for biochemistry, and most arise from its polar nature |
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Because of the polar nature of water, |
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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) |
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Hydrophobic effects-3rd intramolecular force- |
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(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) |
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oxygen atom strips the electron from one of its hydrogen atoms. |
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Ionization of Water Mechanism: |
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1) H -- O -- H <--> H+ + OH- 2) the hydrogen ions are immediately hydrated to form hydronium (H3O+) H+ + H2O <--> H3O+ |
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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 |
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[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 |
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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 |
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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 |
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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) |
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Henderson-Hasselbalch Equation: |
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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.
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an analytical method used to determine the amount of acid in a
solution |
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is plot of the pH of the solution vs the amount of OH- |
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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) |
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Gibbs free energy change tells us: |
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if the rxn will proceed or not.
For the rxn:
^G = ^H -T^S |
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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 |
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e.g. the equilibrium constant at 54.5'C is 0.27, calculate ^G' and answer if this
rxn is spontaneous or not. |
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Definition
^G'= -RT ln keq
^G'= (-8.314)(54.5+273) ln(0.27)
^G'= 3.5KJ/mol |
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What is the effect of concentration on change in free energy? |
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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
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are very versatile macromolecules in living systems and they have
crucial function in essentially all biological processes
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Some of the functions of proteins are: |
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proteins are polymers built of monomer units called |
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proteins can spontaneously fold up into |
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three dimensional structures, and the
function of a protein is dependent on its three dimensional structure. |
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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
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since there are 4 different groups connected to the alpha-carbon |
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amino
acids are chiral and they may exist in L or D isomer
‣ amino acids found in proteins are L-isomes, except few exceptions |
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polar and charged molecule |
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ziwetterions (dipolar ions) |
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what if the above molecule is in pH 1? |
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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
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it is the pH where the net charge is 0 |
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in order to find the isoelectric point |
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‣ consider various charge forms of the molecule
‣ find the isoelectric form
‣ take average of 2 pkas immediately on either side of the isoelectric form |
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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 |
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• serine - Ser-S
• threonine - Thr-T
• tyrosine - Tyr-T
• cystine- Cys-C
• asparagine - Asn- N
• glutamine - Gln - Q |
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• aspartic acid - Asp- D
glutamic acid - Glu- E |
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• lysine - Lys- K
• arginine - Arg - R
• histidine- His- H |
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Polar Uncharged Group
Ser
S |
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Polar Uncharged Group
Thr
T |
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Polar Uncharged Group
Tyr
T |
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Polar Uncharged Group
Cys
C |
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Polar Uncharged Group
Asn
N |
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Polar Uncharged Group
Gln
Q |
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Polar Charged (acidic)
Asp
D |
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Polar charged (acid)
Glu
E |
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Polar Charged (basic)
Lys
K |
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polar charged (basic)
Arg
R |
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polar charged (basic)
His
H |
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Primary Structure of Proteins |
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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 |
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The formation of peptide bond is accompanied by |
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Series of amino acids joint together by the peptide bond form the |
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each amino acid in a polypeptide is also called a __ |
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By convention __ __ is at the beginning (left side) of the chain and the ___ at the end (right side). |
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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 |
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because of this partial double bond characteristic, |
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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 |
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peptides can be classified into: |
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dipeptide- two amino acids joined by peptide bonds oligopeptide- 12-20 amino acids joined by peptide bonds polypeptide- more than 20 ‣ most are here |
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two cysteins can react to form a __ __. covalent bond that is found in proteins, it provides stability to proteins. |
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