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NAME: Gemmarose B. Jamelo SECTION: 20.1E

The document provides instructions for Gemmarose B. Jamelo to read a chapter on proteins in their textbook, watch supplementary videos, and answer 5 questions. The questions cover topics like the classification of amino acids, similarities between amino acid structures, differences between alpha-helices and beta-strands, levels of protein structure, and differences between determining protein structure using X-ray crystallography versus NMR spectroscopy.

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124 views2 pages

NAME: Gemmarose B. Jamelo SECTION: 20.1E

The document provides instructions for Gemmarose B. Jamelo to read a chapter on proteins in their textbook, watch supplementary videos, and answer 5 questions. The questions cover topics like the classification of amino acids, similarities between amino acid structures, differences between alpha-helices and beta-strands, levels of protein structure, and differences between determining protein structure using X-ray crystallography versus NMR spectroscopy.

Uploaded by

qwerty
Copyright
© © All Rights Reserved
We take content rights seriously. If you suspect this is your content, claim it here.
Available Formats
Download as DOCX, PDF, TXT or read online on Scribd
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NAME: Gemmarose B.

Jamelo
SECTION: 20.1E

Instruction: read the chapter on proteins in the textbook provided to you, watch the
supplementary videos, then answer the following questions:

1. Amino acids, the building blocks of proteins are classified into four groups. What are
these groups? Describe each with one to two sentences.

Amino Acids are classified into four groups:


1) Amino Group
- The amino group is distinguished by the fact that a single bond bonds the nitrogen atom
to either the hydrogen or the carbon atom.
2) Carboxyl Group
- A carboxyl group is described as a group that has both a carbonyl and a hydroxyl group
that are both attached to the carbon atom of the molecule. A carbonyl group is a carbon
that has formed a double bond with oxygen.
3) R-Group
- The R group is a side chain that is unique to each amino acid and is responsible for
giving distinct chemical properties to that amino acid.
4) Alpha Carbon Group
- The alpha carbon (also known as Cα) is responsible for the bond formed between the
amino group and the acid carboxyl group, which is how amino acids get their name.
Aside from that, the alpha carbon acts as a point of attachment for the sidechains

2. Paste an image showing the chemical structure of the twenty amino acids. What are the
similarities among all twenty amino acids?
These are the 20 amino acids. They all share a similarity in which they have the same
basic structure, but they only differ in their side chains or the r-group.

3. How are the properties of an α-helix different from a ß-strand? How are they similar?

The main difference between the alpha and beta-helix is the style of hydrogen bonding
they present. The alpha helix offers intramolecular hydrogen bonding, whereas the beta-
helix presents intermolecular hydrogen bonding. What they have in common is that they
are both bonded by hydrogen bonding.

4. What is the difference between primary, secondary, tertiary, and quaternary protein
structure?

1) The primary structure is simply the order/sequence of amino acids in the peptide chain.
2) The secondary structure is how a single protein's main structure allows distinct helices
(mostly alpha helices) and beta sheets by forming links between non-adjacent amino acid
wastes.
3) The tertiary structure is how a single protein's primary and secondary structures
engage with one another in ways besides helices and sheets, which form bonds between
different non-adjacent amino acid wastes.
4) The quaternary structure is the mechanism by which distinct proteins (different
polypeptide chains that are not covalently bonded) can form complexes by different types
of non-covalent bonds.

5. What are some of the differences between X‐ray crystallography and NMR for
determining protein structure? What can NMR tell us that X‐ray crystallography cannot?

NMR spectroscopy differs from X-ray crystallography in that it uses strong magnetic
fields to analyze the alignment of nuclei in an atom. X-ray crystallography is used to
learn the three-dimensional structure of a crystal, whereas NMR spectroscopy is used to
analyze the alignment of nuclei in an atom.

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