VITATI KEY: Positive charge: Purple, Negative Charge: Pink Hydrophilic: Green Hydrophobic: Brown MOSTU. TOUT um b. Now change the second pull down to oil. What changes? וועען a. Set the first pull down to show charge and hydrophobicity and the second pull down as water. Click generate random protein, and then select random mix (last option). Run the simulation (arrow in center of playbar). What do you notice? (ie What type of amino acid are on the outside?) When you run it again, what is the same and what is different? c. Now change the second pull down to vacuum. What changes? What type of interactions remain? d. Now instead of ‘random mix’, click Mostly hydrophobic and toggle between oil and water. What do you notice? e. Lastly click All hydrophilic and toggle between oil and water. What do you notice? 2. What are the monomers (one subunit) of a polypeptide called? ● On the left half of the space below, draw a simple structure of a protein monomer with uncharged functional groups and R to denote the side chain. Circle and label the function groups and alpha carbon. On the right half of the space, draw a similar structure with the two functional groups in their ionized (charged) forms. (At cellular pH both functional groups will be ionized. When we discuss whether this monomer is acidic/basic or polar/nonpolar then we are just referring to the variable side chains.) 3. After synthesis, a bond connects the two amino acids. Many subunits in a polymer make up the primary structure of a polypeptide. In the space below, draw a peptide dimer (2 amino acid connected by a bond, you can just use R for side chain again). Label the two ends of the dimer with N-terminus (to indicate amino group of the first amino acid) and C-terminus (to indicate carboxyl group of the last amino acid).
VITATI KEY: Positive charge: Purple, Negative Charge: Pink Hydrophilic: Green Hydrophobic: Brown MOSTU. TOUT um b. Now change the second pull down to oil. What changes? וועען a. Set the first pull down to show charge and hydrophobicity and the second pull down as water. Click generate random protein, and then select random mix (last option). Run the simulation (arrow in center of playbar). What do you notice? (ie What type of amino acid are on the outside?) When you run it again, what is the same and what is different? c. Now change the second pull down to vacuum. What changes? What type of interactions remain? d. Now instead of ‘random mix’, click Mostly hydrophobic and toggle between oil and water. What do you notice? e. Lastly click All hydrophilic and toggle between oil and water. What do you notice? 2. What are the monomers (one subunit) of a polypeptide called? ● On the left half of the space below, draw a simple structure of a protein monomer with uncharged functional groups and R to denote the side chain. Circle and label the function groups and alpha carbon. On the right half of the space, draw a similar structure with the two functional groups in their ionized (charged) forms. (At cellular pH both functional groups will be ionized. When we discuss whether this monomer is acidic/basic or polar/nonpolar then we are just referring to the variable side chains.) 3. After synthesis, a bond connects the two amino acids. Many subunits in a polymer make up the primary structure of a polypeptide. In the space below, draw a peptide dimer (2 amino acid connected by a bond, you can just use R for side chain again). Label the two ends of the dimer with N-terminus (to indicate amino group of the first amino acid) and C-terminus (to indicate carboxyl group of the last amino acid).
Human Anatomy & Physiology (11th Edition)
11th Edition
ISBN:9780134580999
Author:Elaine N. Marieb, Katja N. Hoehn
Publisher:Elaine N. Marieb, Katja N. Hoehn
Chapter1: The Human Body: An Orientation
Section: Chapter Questions
Problem 1RQ: The correct sequence of levels forming the structural hierarchy is A. (a) organ, organ system,...
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Transcribed Image Text:VITATI
KEY: Positive charge: Purple, Negative Charge: Pink Hydrophilic: Green Hydrophobic: Brown
MOSTU.
TOUT
um
b. Now change the second pull down to oil. What changes?
וועען
a. Set the first pull down to show charge and hydrophobicity and the second pull down as water. Click
generate random protein, and then select random mix (last option). Run the simulation (arrow in center of
playbar). What do you notice? (ie What type of amino acid are on the outside?) When you run it again, what is
the same and what is different?
c. Now change the second pull down to vacuum. What changes? What type of interactions remain?
d. Now instead of ‘random mix’, click Mostly hydrophobic and toggle between oil and water. What do you
notice?
e. Lastly click All hydrophilic and toggle between oil and water. What do you notice?
2. What are the monomers (one subunit) of a polypeptide called?
●
On the left half of the space below, draw a simple structure of a protein monomer with uncharged
functional groups and R to denote the side chain. Circle and label the function groups and alpha carbon.
On the right half of the space, draw a similar structure with the two functional groups in their ionized
(charged) forms. (At cellular pH both functional groups will be ionized. When we discuss whether this
monomer is acidic/basic or polar/nonpolar then we are just referring to the variable side chains.)
3. After
synthesis, a
bond connects the two amino acids.
Many subunits in a polymer make up the primary structure of a polypeptide. In the space below, draw a
peptide dimer (2 amino acid connected by a bond, you can just use R for side chain again). Label the two ends
of the dimer with N-terminus (to indicate amino group of the first amino acid) and C-terminus (to indicate
carboxyl group of the last amino acid).
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