Week 4 Day 1 Molecular Biology Flashcards
Nonpolar Amino Acids pneumonic
Grandma
C
Always
Visits
London
In
May
Por
Tio’s
Party
Glycine (Gly)
Cysteine (Cys)
Alanine (Ala)
Valine (Val)
Leucine (Leu)
Isoleucine (Ile)
Methionine (Met)
Proline (Pro)
Tryptophan (Trp)
Phenylalanine (Phe)
Acidic Amino Acids (polar)
Glutamic Acid (Glu)
Aspartic Acid (Asp)
Basic Amino Acids pneumonic (polar)
Are
Liars
High
Arginine (Arg)
Lysine (Lys)
Histidine (His)
Polar uncharged amino acids pneumonic
Asparagus
Gets
Sweeter
Through
Time
Asparagine (Asn)
Glutamine (Gln)
Serine (Ser)
Threonine (Thr)
Tyrosine (Tyr)
What determines the identity of an amino acid?
it’s side chain
Which amino acid is not chiral?
Glycine, it’s side chain is an H
Which end of the zwitterion is the conjugate base of a weak acid…the carboxylate end or the ammonium-ion-end?
carboxylate-ion-end
Which end of the zwitterion is the conjugate acid of a weak base…the carboxylate end or the ammonium-ion-end?
the ammonium-ion-end
Stated from the book:
The net electrical charge on an AA is a function of pH, and this has both critical and useful implications. At very low pH, an AA is primarily in its fully protonated form (H2A+), and the net charge on an AA is positive. As pH increases, the cationionic form is gradually converted to the zwitterionic for (HA), and the net charge approaches zero. As we continue to increase the pH to strongly basic conditions, the ammonium group surrenders the second proton, converting the amino acid into its fully deprotonated form (A-), and the net charge on an AA is negative.
Primary structure of proteins
linear sequence of amino acids in a peptide chain
Secondary structure of proteins
indicates local spatial arrangement of polypeptide backbone yielding alpha helical or beta pleated sheet structure
Hydrogen bonds between the ‘backbone’ amide -NH- and
-CO-
Tertiary structure
how the alpha helices and beta sheet portions of a polypeptide chain are folded into a compact globular structure
Quanternary structure
indicates the assemply of multiple polypeptide chains into an intact, tetrameric protein
i.e. hemoglobin
Elements of tertiary structure of proteins
- disulfide bonds (covalent bond) - strongest, but we don’t have a lot, they tend to have special/specific uses (think hair)
- hydrogen bonds - weak, easy to break, but we have A LOT
- salt bridges (much like an ionic bond) - stronger than hydrogen bond, less frequent
- hydrophobic interactions
What is the purpose of RNA polymerase?
Binds to the DNA strand to “unzip” or “split up” the double strand of DNA
After the RNA copy is made in the nucleus, what are some modifications we need to do before sending it out to the cytoplasm?
Put a cap on the 5’ end
cut out the introns
finish with a poly A tail
T or F: The process of making an RNA copy from DNA is called trancription.
True
this is called mRNA synthesis
Where does mRNA synthesis occur?
The nucleus
What is the purpose of RNAase
To degrade the mRNA once the mRNA is done making proteins.