In comparison of a unstable to stable atom False
by filling of outer shells, the more stable
atom is less abundant.
Phosphate makes 5 covalent bonds, False
predicted from the conventions applied to
O, N, C and H.
The number of covalent bonds for H is True
always 1.
In the valiancy theory, electrons can "count" True
toward filling orbitals for both atoms they
are involved in in making a covalent bond.
The probability of electron distribution in False, more dense toward O
water is even between H and O.
For -CH2-CH3, the C-C bond is polar. False
For -(CH2) 3-NH2, the N-H bonds are both True
polar, with partial + on the H.
A H bond forms between a H and an True
electronegatively charged atom, like O or N
bonded to C.
Two H can form an H bond between False
themselves.
A hydrophobic bond forms between two True
non-polar molecules.
One of the strongest hydrophobic bonds in True
biology are between the fatty acid tails.
In pair of molecules C, there is an interaction False
between the left molecule and the CH2 of
the right molecule.
In D, there is an H bond between the O of False
OH on the left, and the H of the terminal C-
H on the right.
Na+Cl- is more stable and abundant than True
either of the two uncharged atoms.
pH can affect weak bonds by altering the False
charge of nonpolar atoms.
pH can affect weak bonds by altering the True
charge of a carboxyl group (COOH) for
example.
It takes a lot more energy to break a True
covalent bond than a non-covalent weak
bond.
Oil dissolves salt as effectively as water. False
The distance between atoms forming weak FALSE...is reduced by 1/64
bonds is reduced by 1/2 when the distance is
doubled. (Note: We forgot to put 1/r6 is the
righthand diagram.)
HIV #2 does not bind as well as HIV#1. True
,The more weak bonds between two True
molecules, the more often the two bind to
each other.
All other things being equal, A is bound to B True
more than C is bound to D.
Ice has more covalent bonds per molecule FALSE...same number, more weak bonds though!
than water (given their pHs are the same).
pH. At high pH (meaning much larger False
number than pH7), there will be more of the
top molecule than the bottom.
The equilibrium shown in the lower half of True
the diagram will favor the right side because
there are more weak bonds there.
This reaction is a "bomb", as you young folks True
like to say.
A hydride and hydroxyl radical are not False.. less stable!
charged and are thus more stable than H+
and OH- ions.
The Central Dogma has DNA converted to True
RNA converted to protein. Generally
correct!
Synthetic Biology is a field in which an True
organism is made to make something it does
not usually make.
Hemaglobin is a tetramer. When it binds to FALSE,,it does move some!!
Oxygen, the structure does not change
compared to the unbound form.
The Na+K+ ATPase pump uses ATP (not False.. K+ is pumped into the cell. Not a big deal.. I just want you to look carefully at
shown) to "drive" the pumping of Na+ out of diagrams!
the cell, and K+ out of the cell.
ATP synthase is an enzyme that uses a H+ True
gradient to make ATP.
One reason proteins are such great False.. its 20^5, 20 x 20 x 20 x20...which is a number far bigger than 100...
biological molecules is that they can make
many different shapes of surfaces. So, if
there are 5 areas, each being any of 20
different possible structures (different R
groups of amino acids, as we will learn), then
there are about 100 different shapes that can
be made from these 5 areas.
The synthesis reaction involves water being False...water is released by making a peptide bond!
consumed to make a peptide bond.
Any protein has one amino end (or N True
terminus) and one carboxyl end (or C
terminus).
Proteins get degraded, broken down for True
many reasons. One is that the atoms in a
protein may get damaged by oxygen.
, Proteins being degraded involves water True
attacking a peptide bond, in a process
called many things, including hydrolysis. This
is the reaction that the HIV polyprotein
undergoes.
There are three pictures of a protein. They True
are all three hemoglobin. Hemoglobin, the
adult form which is what these are, consists
of 4 molecules, two of an alpha subunit and
two of beta.
Proteins can be fully appreciated just by False
understanding primary, secondary, tertiary
and quaternary structures.
The primary sequence is the sequence of True
amino acids.
The polar amino acids include leucine. False.. this one is non-polar!
An alpha helix is one of the secondary False..H bonds within the helix
structures. It forms from hydrophobic
weakbonds within the helix.
Beta sheets are a second secondary False...NH group to C=O group lll
structure. It forms using hydrogen bonds,
bonding a C-H group to an C=O group, the
hydrogen to oxygen.
This is a part of secondary structure that Dr. True
Ted put in..it has to go somewhere. About
1/3rd of all proteins are "unstructured", the
double asterisks denote such regions in
hemoglobin.
Tertiary structure is formed by You best know intra vs inter!
intermolecular weak bonds.
False...intramolecular weak bonds.
Intermolecular is between two molecules,
intermolecular is within one molecule.
This shows intramolecular weak bonds of False...the disulfide is between to cysteines. :) Alanine is -CH3!
three types. And, a special covalent bond, a
disulfide, that forms between two alanine
amino acids.
O2 has a nonpolar covalent bond. True: O is equal to O
O2 can form a hydrogen bond with water. False..need a polar covalent bond to do so.
If this structure is heated and then cooled, False...hydrophobic does not form bond with hydrophilic...and NH3 group dictates later
the -CH2CH-CH3(2) group in the middle is hydrophilic.
could form a weak bond with the -(CH2)4-
NH3+ group.
Protein complexes have a virtue that they True...the gamma subunit in fetus versus alpha in adult is great example
can be altered by removing and adding
other subunits to achieve a slightly different
activity. Hemoglobin is a good example of
this versatility.