Hydrogen bond
Download
Report
Transcript Hydrogen bond
Chapter 2
Water
- Description of Physical & Chemical Properties of Water-
Noncovalent interactions in biomolecules
1. Hydrogen bonds
2. Ionic Interactions
3. Hydrophobic Interactions
4. van der Waals interactions
Hydrogen Bonding in Water
Hydrogen Bonding in Water
Unusual properties of water
- High melting and boiling point, and heat of vaporization
Hydrogen bond
Weak bond dissociation energy
23 kJ/mol (c.f. O-H : 348 kJ/mol)
Average 3.4 hydrogen bonds /water molecule
4 hydrogen bonds /water molecule
10% covalent and 90% electrostatic
Liquid
Ice
Melting or evaporation at room temperature : DG<0
Increase in enthalpy < increase in entropy
Hydrogen Bonding of Water with
Polar Solutes
Common H bonds in biological systems
Directionality of H bond
Electrostatic Interaction of Water
with Charged Solutes
Water solubility
Hydrophilic : polar, water soluble
Hydrophobic : nonpolar, water insoluble
Dissolving Salt in Water
Hydration and stabilization of ions
DG = DH – TDS
Small positive DH, large positive DS
negative DG
Dissolving Gas in Water
CO2, O2, N2
Poor solubility
Nonpolar
Decrease in entropy by dissolving in water
Facilitating transport in organisms
O2 carrier protein (hemoglobin, myoglobin)
CO2 forms carbonic acid (H2CO3) in water
water soluble bicarbonate (HCO3-)
NH3, H2S
Polar and water soluble
Dissolving Nonpolar Compounds in
Water
Poor solubility
Small gain of enthalpy
Decrease in entropy
Highly ordered water molecules around nonpolar molecule
Hydrophobic interactions
Clustering of nonpolar molecules or regions in water
Amphipathic molecules form micelles
Increase in entropy
Hydrophobic Interactions in Biological
Systems
Many biomolecules are amphipathic
Hydrophobic interactions
Membrane structure (lipid-lipid & lipid-protein)
Stabilization of 3D structure of protein
Increase in entropy by increasing disordered water
One of the driving force for enzyme-substrate
binding
Enzyme-substrate interaction
van der Waals Interactions
van der Waals interactions (London forces)
Weak interatomic interaction between transient
electric dipole
van der Waals radius
The point balancing van der Waals attraction and
repulsion
Weak Interactions in Macromolecular
Structure and Function
Noncovalent interactions in biological system
Hydrogen bonds, Ionic, hydrophobic,
and van der Waals interactions
Weak but strong cumulative effect
Water in Biomolecules
Structural water molecule
Tightly bound to the proteins (not osmotically active)
Biological function
e.g. cytochrome f
Water chain in cyt f
Structural water in hemoglobin
Effect of Solutes on Colligative
Properties of Aqueous Solutions
Colligative (tied together) properties of solvent
Vapor pressure
Boiling point
Melting point
Osmotic pressure
Effect of Solutes on Colligative Properties
Depending on the number of solute particles
Lowering the effective concentration of water
Effect of Solutes on Colligative
Properties of Aqueous Solutions
Osmotic pressure
Pressure generated by diffusion of water from the
region of high water concentration to that of lower
water concentration
van’t Hoff equation
P = icRT
ic: osmolarity
c: solute’s molar concentration
i: van’t Hoff factor
e.g. NaCl: i =2
Osmosis
Movement of water across a semipermeable
membrane by osmotic pressure
Water Movement across Membrane
Plasma membrane
More permeable to water than other
small molecules
Mechanisms to prevent osmotic lysis
Bacteria, plant
Rigid cell wall
Fresh water protists
Contractile vacuole pumping water out of
the cell
Animals
Maintain osmolarity of blood plasma and
interstitial fluid close to that of the cytosol
Albumin in blood plasma
Na+ pump
Inoization of Water
H2O
H+ + OH Immediate hydration of
H+ to form hydronium ion
(H3O+)
High ionic mobility of H+
and OH- than other ions
(Na+, K+, Cl-)
Proton hopping
Faster than diffusion of
individual proton
Fast acid-base reaction in
water
Ionization of Water
Keq for ionization of water at 25oC
Keq =
[H+] [OH-]
[H2O]
[H+] [OH-]
=
55.5M
Kw : ion product of water
Kw = [H+] [OH-] = (55.5M)Keq
= (55.5M)(1.8 X 10-16 M)
= 1.0 X 10-14 M2
pH = -log [H+]
Neutral pH
[H+] = [OH-] = 1.0 X 10-7 M
Ionization of Weak Acids
Ka: Dissociation constant (HA
H+ + A- )
Equilibrium constant for ionization reactions
[H+] [A-]
pKa = -log Ka
Keq =
[HA]
= Ka
Titration Curve
Titration curve of acetic acid
Gradual addition of 0.1M NaOH to
0.1M acetic acid
Kw = [H+][OH-] = 1 X 10-14 M
[H+][Ac-]
Ka =
[HAc]
Removal of [H+] by addition of NaOH
formation of H2O
Dissociation of HAc to keep Ka
At midpoint of titration
[Ac-] = [HAc]
pH = pKa
Titration Curve
Buffers
Aqueous systems that tend to
resist changes in pH when small
amount of acid or base are
added
Consist of a weak base and its
conjugate base
Maximum buffering power
Midpoint of titration curve
Buffering pH zone
~ pKa ± 1
Hendeson-Hasselbalch equation
pH = pKa + log [A-]/[HA]
Buffer System in Cells and Tissues
Keeping pH is biological system
pH 6.9 ~7.4
Important for enzyme activity and
other structure and functions
Weak acids and bases in biological
system
Proteins (weak acids & base functional
groups of a.a)
His :pKa of 6.0
Nucleotides (phosphate of ATP)
Low molecular weight metabolites
Organic acids : vacuoles of plant cells
Ammonia : urine
Important biological buffers
Phosphate system : biological fluid
H2PO4H+ + HPO42- : pKa of 6.86
Bicarbonate system : blood plasma (pH 7.4)
H2CO3
H+ + HCO3 CO2 (gas) CO2 (dissolved) H2CO3
Water as Reactant
Condensation reaction
Elimination of water
Endergonic
Hydrolysis reaction
Addition of water
Exergonic
Hydrolases
Depolymerization of
proteins, carbohydrate,
nucleic acids
Oxidation and reduction