Molecular Bonds and Forces - Biochemistry

In the double-helix structure of DNA, there are 2 hydrogen bonds between adenine and thymine, and 3 hydrogen bonds between cytosine and guanine. Phosphodiester bonds are covalent bonds between the 5-C sugar and phosphate group of nucleotides (and are much stronger than the hydrogen bonds between complementary bases).

In a solution of water, the outside of a folded protein is going to be in direct contact with water. Therefore, polar or ionic attractions are most favored on the outside of a protein in a solution of water since these can form attractions. The only amino acid listed that can form either polar or ionic attractions is glutamic acid.

Hydrogen bonds are found in primary structure of protein, as well as between the bases in DNA structure. Hydrogen bonds are only found between hydrogens attached to oxygen, nitrogen, or fluorine. They increase the attraction between water molecules, therefore are harder to break in large numbers, causing an increase in boiling point.

An example of strong intermolecular bond is a hydrogen bond. A hydrogen bond occurs between a hydrogen atom on a molecule and an either nitrogen, oxygen, or fluorine atom on an adjacent molecule. The question states that there are bonds between molecule A and molecule B. We can assume that these are hydrogen bonds. This means that molecule A can have hydrogen atom and/or nitrogen, oxygen, or fluorine atoms. Similarly, molecule B can also have hydrogen atom and/or nitrogen, oxygen, or fluorine atoms.

Molecule C doesn’t form hydrogen bonds with either of the other two molecules. This means it cannot have hydrogen and/or nitrogen, oxygen, or fluorine atoms. This is because if molecule C had any of these atoms then it would interact with at least one of the other molecules and form hydrogen bonds (because molecule A and molecule B have these other atoms).

Covalent bonds occur between atoms within (or intra) molecules. This means that covalent bonds are intramolecular bonds. Hydrogen bonds, on the other hand, occur between hydrogen atoms of one molecule and either a nitrogen, an oxygen, or a fluorine atom in another molecule. Since hydrogen bonds occur between molecules, they are classified as intermolecular bonds. There are some situations in which hydrogen bonds may be formed intramolecularly, but these are special cases.

Hydrogen bonds occur between a hydrogen atom in one molecule and either nitrogen, oxygen, or fluorine atom in another molecule. It only involves nitrogen, oxygen, or fluorine atoms because these atoms have high electronegativity. Since they have very high electronegativity, these three atoms can easily attract the electron found in the hydrogen atom and form hydrogen bonds. Chlorine doesn’t have high enough electronegativity to form hydrogen bonds.

An atom's state of matter does not determine whether an atom can form hydrogen bonds. Fluorine, just like chlorine, is a halogen and it can form hydrogen bonds.

Hydrogen bonds can occur between two molecules (intermolecular) and within parts of a single molecule (intramolecular). They are weaker than covalent bonds but are stronger than a Van der Waals interaction, and this strength is determined by a number of factors including bond angle.

For a hydrogen bond to occur, the atom to which the hydrogen is bonded has to have a high relative Pauling electronegativity. Only oxygen, nitrogen, and fluorine, in the upper right corner of the periodic table, have these electronegativities. Neon, argon, and xenon are, of course, inert noble gases, although xenon is sometimes assigned a high electronegativity. This is due, however, to rare bonding events -- certainly not regular hydrogen bonding. Sodium, magnesium and aluminum often form positively charged ions, so they would not tend to attract a hydrogen nucleus.

Hydrogen can form hydrogen bonds with nitrogen, oxygen, and fluorine. A water molecule consists of an oxygen atom bonded to two hydrogen atoms. Each hydrogen atom can form a hydrogen bond with a nitrogen, fluorine, or oxygen atom. Also, the oxygen, which has two lone pairs of electrons, can form two hydrogen bonds with hydrogen atoms. This sums to four hydrogen bonds per water molecule.

Only nitrogen, oxygen, and fluorine can form hydrogen bonds since these three elements are very electronegative. Thus, their partial negative charge (and the presence of a lone pair of electrons) attracts a partially positive hydrogen atom. Carbon, on the other hand, is not very electronegative and thus cannot form hydrogen bonds.

Uracil is not a base in DNA, so A-U can be ruled out as an answer. Moreover, C-G and A-T are the correct base pairs, so the other combinations can be ruled out as well. C-G requires more energy to break because there are three hydrogen bonds between these bases, while A-T has only two hydrogen bonds holding them together.

Bond strengths are measured in kilojoules/mole. Hydrogen bonds can have a strength of . Ionic bonds can have a strength of . This makes hydrogen bonds much weaker than ionic bonds.

In aqueous solutions, lipid molecules are surrounded by a lattice-like ring of water molecules known as a clathrate shell. This locks up previously free water molecules in this state, which is not entropically favored. Though it is unavoidable that some water molecules will have to be robbed of some of their freedom of motion by forming at least one clathrate shell, the ideal scenario thermodynamically is the one in which the fewest water molecules are stuck in the shell as possible. As a result, lipid bubbles in aqueous solutions tend to go from many to one, as this results in the clathrate shell with the fewest number of water molecules. In the process, many smaller clathrate shells are broken, and many water molecules are freed, thus increasing the entropy of the system.

Proteins will behave similarly to phospholipids in water; the polar groups will form favorable interactions on the surface with water, while the hydrophobic groups will be in the core and away from the water molecules. Usually, amino acids with non-polar residues will be found in the core of proteins. Tryptophan has a nonpolar side chain, and will thus be found in the core of a protein that is in a aqueous environment.

Hydrophobic effects require water to occur. The reason that hydrophobic groups tend to group together is that by doing so, the network of water molecules around them stays intact. There are no other special forces at play between hydrophobic groups. It is precisely the non-polar nature of hydrophobic groups that gives them their character; water molecules are polar. Cell membranes have a phospholipid bilayer with internal hydrophobic regions (the lipid tails), holding together the membrane.

Hydrogen bonds are the strongest of the intermolecular forces. However, that strength is little in comparison the strength of intramolecular forces, such as ionic and covalent bonds. The strongest of the listed forces is covalent bonds, followed by ionic bonds, hydrogen bonds, and then finally London dispersion forces.

Hydrogen bonds are important in biochemistry because of the incredible effect that they have on life due to their relative strength. But remember, this strength is not nearly as as strong as the covalent and ionic bonds, which actually hold atoms within the same molecule together.

Note, hydrogen bonds can be either an intermolecular or an intramolecular force. A hydrogen bond is considered intramolecular if it is occurring between different molecules, and intermolecular if it is occurring within the same molecule.

This is called the hydrophobic effect. Although initially the water molecules arrange themselves in clathrates and become more ordered, their exclusion of the hydrophobic/nonpolar solute is entropically driven and energetically favorable.

In , each bond is polar, as oxygen is much more electronegative than carbon. However, these dipole moments are equal in charge and this molecule is linear with carbon in the middle, so the entire molecule is nonpolar.

In water, oxygen is more electronegative than hydrogen; thus, electrons are pulled toward the oxygen atoms more than towards hydrogen atoms. This gives oxygen a partial negative charge and hydrogen a partial positive charge. The entire molecule is polar since water's molecular geometry is bent.

Methane includes a carbon with a hydrogen attached to each of its four bonds. Electrons are distributed relatively equally across each bond since the electronegativities of hydrogen and carbon are comparable, and the entire molecule is tetrahedral. Thus, neither the individual bonds nor the entire molecule are polar.

In , nitrogen is left with a lone pair of electrons after it bonds with three hydrogen atoms. Because of this lone pair, the molecular geometry is trigonal pyramidal and the entire molecule is polar with the nitrogen atom being slightly negative (high electronegativity) and the hydrogen atoms being slightly positive.

While the peptide bond in a polypeptide chain is locked and unable to rotate, the amino nitrogen-alpha carbon bond can rotate. Additionally, the alpha carbon-carboxyl carbon can rotate as well.

However, like in many other molecules, the cis conformation is energetically unfavorable due to steric hindrance. This steric hindrance occurs when the side chains of two residues are right next to each other within the polypeptide. This is unfavorable, and the trans conformation is therefore preferred.