Identify a peptide bond, the N-terminus (amino-terminus) and C- terminus (carboxyl-terminus) of a polypeptide in a series of linked amino acids. Describe the four levels of protein structure (primary, secondary, tertiary, and quaternary), what types of bonding interactions hold each level together, and how a protein’s structure relates to its cellular function. Link the chemical structures of amino acid R groups to the types of interactions they could form in the folded structure of a protein. Hypothesize the likely consequence of environmental conditions on the folded structure. Recognize secondary structure elements when proteins are represented in different ways (e.g. ball-and-stick structures, ribbon diagrams). Define these terms: enzyme, enzyme activity, active site, substrate, enzyme substrate complex, product, denature. Explain with molecular detail how some conditions affect enzyme activity.

Biochemistry
9th Edition
ISBN:9781319114671
Author:Lubert Stryer, Jeremy M. Berg, John L. Tymoczko, Gregory J. Gatto Jr.
Publisher:Lubert Stryer, Jeremy M. Berg, John L. Tymoczko, Gregory J. Gatto Jr.
Chapter1: Biochemistry: An Evolving Science
Section: Chapter Questions
Problem 1P
icon
Related questions
Question

Learning Objectives

  • Identify a peptide bond, the N-terminus (amino-terminus) and C- terminus (carboxyl-terminus) of a polypeptide in a series of linked amino acids.
  • Describe the four levels of protein structure (primary, secondary, tertiary, and quaternary), what types of bonding interactions hold each level together, and how a protein’s structure relates to its cellular function.
  • Link the chemical structures of amino acid R groups to the types of interactions they could form in the folded structure of a protein.
  • Hypothesize the likely consequence of environmental conditions on the folded structure.
  • Recognize secondary structure elements when proteins are represented in different ways (e.g. ball-and-stick structures, ribbon diagrams).
  • Define these terms: enzyme, enzyme activity, active site, substrate, enzyme substrate complex, product, denature.
  • Explain with molecular detail how some conditions affect enzyme activity.
have in common so that you will be able to identify the chemical group for each of
the 20 amino acids if you are shown its structure. Record your rules in a table
similar to the one shown below.
Nonpolar
Polar (uncharged)
COO
COO
COO"
H3N-C-H
HN-C-H
HạN-C -H
H3N -C -H
HaN-C-H
H3N-C-H
H
CH3
CH
バ
CH,OH
H-C-OH
CH2
CH, CH,
CH3
SH
Glycine
Alanine
Valine
Serine
Threonine
Cysteine
COO
COO
COO
HaN-C-H
HN-C-H
HN-C-H
COO
CH2
CH2
H-C-CH3
HN-C-H
CH
CH2
CH,
CH2
CH2
CH; CH3
CH3
CH2
CH3
H2N
Leucine
Methionine
Isoleucine
Coo
COo-
Coo
Asparagine
Glutamine
H3N-C-H
HN-C -H HN-c-H
Basic
CH2
CH2
CH2
COO
CO"
C=CH
HN-C-H
-C-H
-C-H
NH
CH,
CH2
CH2
ÓH
CH2
CH2
C-NH
CH
CH2
CH2
C-NA
Phenylalanine
Tyrosine
Tryptophan
CH2
NH
CO-
*NH3
C3D
NH2
CH,
Lysine
Arginine
Histidine
HC CH2
Acidic
COO
CO0
Proline
HN-C-H
HạN-C-H
CH2
CH2
COO
CH2
CO0
Aspartate
Glutamate
Figure 2. Structures of the 20 natura
mino acids.
Screenshot
Transcribed Image Text:have in common so that you will be able to identify the chemical group for each of the 20 amino acids if you are shown its structure. Record your rules in a table similar to the one shown below. Nonpolar Polar (uncharged) COO COO COO" H3N-C-H HN-C-H HạN-C -H H3N -C -H HaN-C-H H3N-C-H H CH3 CH バ CH,OH H-C-OH CH2 CH, CH, CH3 SH Glycine Alanine Valine Serine Threonine Cysteine COO COO COO HaN-C-H HN-C-H HN-C-H COO CH2 CH2 H-C-CH3 HN-C-H CH CH2 CH, CH2 CH2 CH; CH3 CH3 CH2 CH3 H2N Leucine Methionine Isoleucine Coo COo- Coo Asparagine Glutamine H3N-C-H HN-C -H HN-c-H Basic CH2 CH2 CH2 COO CO" C=CH HN-C-H -C-H -C-H NH CH, CH2 CH2 ÓH CH2 CH2 C-NH CH CH2 CH2 C-NA Phenylalanine Tyrosine Tryptophan CH2 NH CO- *NH3 C3D NH2 CH, Lysine Arginine Histidine HC CH2 Acidic COO CO0 Proline HN-C-H HạN-C-H CH2 CH2 COO CH2 CO0 Aspartate Glutamate Figure 2. Structures of the 20 natura mino acids. Screenshot
Exercise A: Amino Acid Functional Groups
Figure 1 below shows one of the 20 amino acids that make up proteins. Recall that
carbon can form four covalent bonds. Amino acids consist of a central carbon, called
the a-carbon, that is bonded to four different chemical groups.
H
+
CH2
OH
Figure 1. Structure of an amino acid
Answer the below questions in your own document.
• On the amino acid shown in Figure 1, label the a-carbon.
• The a-carbon of each of the 20 amino acids is bonded to one hydrogen
atom, one amino group, one carboxyl group, and one R group (more on
that below). You should recognize the amino and carboxyl groups from our
discussion of functional groups in organic molecules. Circle and label* the
amino group and the carboxyl group in Figure 1.
*Note: our goal in this question, and in similar questions throughout this lab, is for
you to be able to identify specific structures. You can do this circling/labeling in
whatever way is easiest for you. You might want to draw the structures on a piece of
paper, or use a computer program (like Powerpoint, Photoshop, Paint, Preview, etc.)
to draw on these images. Whatever is easiest for you!
• The last bond an a-carbon in an amino acid makes is to an R group.or side-
chain. Circle and label the R group in Figure 1.
The next page of this handout shows the structures of all 20 amino acids (Figure 2).
They are categorized into 4 chemical groups: nonpolar, uncharged polar, acidic, and
basic.
• Using the three groups you identified in Figure 1 as a reference, what is the only
thing that is different about each of the 20 amino acids?
Look at the amino acids in each of the four groups and compare them to the ones in
the other groups. Figure out rules that describe what the members of each group
Screenshot
Transcribed Image Text:Exercise A: Amino Acid Functional Groups Figure 1 below shows one of the 20 amino acids that make up proteins. Recall that carbon can form four covalent bonds. Amino acids consist of a central carbon, called the a-carbon, that is bonded to four different chemical groups. H + CH2 OH Figure 1. Structure of an amino acid Answer the below questions in your own document. • On the amino acid shown in Figure 1, label the a-carbon. • The a-carbon of each of the 20 amino acids is bonded to one hydrogen atom, one amino group, one carboxyl group, and one R group (more on that below). You should recognize the amino and carboxyl groups from our discussion of functional groups in organic molecules. Circle and label* the amino group and the carboxyl group in Figure 1. *Note: our goal in this question, and in similar questions throughout this lab, is for you to be able to identify specific structures. You can do this circling/labeling in whatever way is easiest for you. You might want to draw the structures on a piece of paper, or use a computer program (like Powerpoint, Photoshop, Paint, Preview, etc.) to draw on these images. Whatever is easiest for you! • The last bond an a-carbon in an amino acid makes is to an R group.or side- chain. Circle and label the R group in Figure 1. The next page of this handout shows the structures of all 20 amino acids (Figure 2). They are categorized into 4 chemical groups: nonpolar, uncharged polar, acidic, and basic. • Using the three groups you identified in Figure 1 as a reference, what is the only thing that is different about each of the 20 amino acids? Look at the amino acids in each of the four groups and compare them to the ones in the other groups. Figure out rules that describe what the members of each group Screenshot
Expert Solution
trending now

Trending now

This is a popular solution!

steps

Step by step

Solved in 2 steps

Blurred answer
Knowledge Booster
Nutrition & Digestion
Learn more about
Need a deep-dive on the concept behind this application? Look no further. Learn more about this topic, biochemistry and related others by exploring similar questions and additional content below.
Recommended textbooks for you
Biochemistry
Biochemistry
Biochemistry
ISBN:
9781319114671
Author:
Lubert Stryer, Jeremy M. Berg, John L. Tymoczko, Gregory J. Gatto Jr.
Publisher:
W. H. Freeman
Lehninger Principles of Biochemistry
Lehninger Principles of Biochemistry
Biochemistry
ISBN:
9781464126116
Author:
David L. Nelson, Michael M. Cox
Publisher:
W. H. Freeman
Fundamentals of Biochemistry: Life at the Molecul…
Fundamentals of Biochemistry: Life at the Molecul…
Biochemistry
ISBN:
9781118918401
Author:
Donald Voet, Judith G. Voet, Charlotte W. Pratt
Publisher:
WILEY
Biochemistry
Biochemistry
Biochemistry
ISBN:
9781305961135
Author:
Mary K. Campbell, Shawn O. Farrell, Owen M. McDougal
Publisher:
Cengage Learning
Biochemistry
Biochemistry
Biochemistry
ISBN:
9781305577206
Author:
Reginald H. Garrett, Charles M. Grisham
Publisher:
Cengage Learning
Fundamentals of General, Organic, and Biological …
Fundamentals of General, Organic, and Biological …
Biochemistry
ISBN:
9780134015187
Author:
John E. McMurry, David S. Ballantine, Carl A. Hoeger, Virginia E. Peterson
Publisher:
PEARSON