Draw an. ionized version of an amino acid and label
the major parts(N terminus, C-terminus, alpha-carbon, backbone) of
the molecule.
Specifically describe how an amino acid is affected by
different pH’s (<7, 7, >7).
Which form is most common and why/how is that
important for cell function/survivability?
The carbon to which carboxyl group is attached is called alpha carbon. The amino group is called the N terminus while carboxyl group end is called the C terminus.
The R group( side chain) is different in different amino acids.
When dissolved in water (at ph7/ neutral pH) it exists as zwitter ion as dipolar ion. It has both positive and negative charge. A zwitter ion can act as both acid and base. So, it is a amphoteric molecule. At low pH ( less than 7) the carboxyl group accepts a proton so overall charge become positive due to charge on the amino group. Similarly, at higher pH the amino group loses a proton and become uncharged, this overall charge becomes negative.
Draw an. ionized version of an amino acid and label the major parts(N terminus, C-terminus, alpha-carbon,...
PRELAB ASSIGNMENT 1 Draw the structure of the amino acid son CH-OH Label the alpha carbon acid Sorine (en) which has R MO CHE OH CH2 OH 2. Draw the dipeptide that forms betw the peptide bond. s between serine and alanine The dipeptide sequence is Ser Ala Lace CH NCH H, A - — сH — с CH2 OH 3. How many amino aci arty amino acid residues are in a polypeptide containing 6 peptide bonos How many peptide...
1.) Draw the structure of the amino acid Serine(ser), which has R=-CH2-OH. Label the alpha carbon. 2.) Draw the dipeptide that forms between serine and alanine. The dipeptide sequence is Ser-Ala. Label the peptide bond. 3.) How many amino acids residues are in a polypeptide containing 6 peptide bonds? How many peptide bonds are in a tripeptide 4.) Sketch a alpha-helix and a beta-sheet as best as you can. Label each.
4. In contrast to the alpha amino acids which are ubiquitous in nature, beta amino acids (with an extra carbon in the backbone) are quite rare. They form secondary structures that have very different conformations from traditional proteins. For instance, the compound shown below is the simplest beta amino acid; unusually, it is most stable in a gauche conformation. Draw it and explain why, co, Corn lonic c Hdi athrachan H₂N HT 5. Quebrachitol is a naturally occurring compound found...
a. First, circle the leaving group and label the alpha carbon as a. b. Then, label the adjacent sp3 beta carbons as B. c. Finally, draw in the H's that can get eliminated along with the leaving group in each of these compounds. The first compound has been completed for you. HH می ) و CH3 2. Now, let's perform the elimination to make the Zaitsev (most substituted) product. Draw in the H from before and the curved arrows to...
1 Proteins are long chains of amino acids. There are 4 parts to each amino acid. Which part is responsible for structural variation in proteins? The side chain The carboxylic acid group The amino group The alpha carbon 2. Why is it important to examine the shapes of complex biological molecules and drugs? All of the choices given So scientists can explain biochemical reactions So scientists can design medications So scientists can determine how molecules fit together 3. Determine the...
5. The chemical properties of an amino acid is determined by a. structure of it's group b. it's central carbon molecule c. structure of it's amino group d. hydrogen molecule e. it's carboxyl group 6. Different amino acids are joined by dehydration synthesis to make proteins. How many different amino acids are there? a. 15 b. 30 c. 20 d. 25 e. 40 7. Lipids are composed of a fits b. sugar c. glycerol d. A and C e. A...
How are organisms biologically organized? Describe the anatomy of the eukaryotic cell (animal and plant). Major difference between eukaryotes and prokaryotes. Describe the different types of chemical bonds. How do they affect the organization of biomacromolecules? Differentiate between a peptide bond, a phosphodiester, a phosphoanhydride bond. What are disulfide bridges? Amino-acids participating in this bonding? Describe the function of enzymes. Understand the forces by which substrates bind to enzymes. Distinguish between redox reactions and activated energy carriers. Distinguish between anabolism...
QUESTION 1Which way do the fatty acid tails of a phospholipid face in a cell membrane?a.toward the inside of the cellb.toward the outside of the cellc.both directionsd.They lay parallel to the direction of the membrane.QUESTION 2A readily available source of energy that cells use to drive reactions is stored in the ___________ bond.a.phosphodiesterb.phosphoanhydridec.hydrogend.peptideQUESTION 3Which of the following occurs by bringing nonpolar surfaces together to exclude water?a.hydrogen bondsb.hydrophobic forcesc.Van der Waals attractionsd.electrostatic attractionsQUESTION 4How many bonds are made by a carbon...
____ 1. The diagram below represents serine, a polar, uncharged
amino acid. Which functional group gives serine its
distinct property?
a. H3
b. CH2OH
c. –H
d. COO–
____ 2. The monomers shown below are monomers for which of the
following natural polymers?
a. polysaccharides
b. plastics
c. DNA
d. proteins
____ 3. Which of the following processes illustrates the production
of a protein?
a. specific code for amino acids --> amino acid chain -->
gene --> DNA --> specific...