Biochemistry I Lecture 1 for Level II Students

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29 Questions

What percentage of the total marks is allocated to the midterm exam?

5%

What is the minimum number of questions expected in the written exam?

25-30

What is the central dogma according to the classic view?

DNA makes RNA and RNA makes protein

What is the primary purpose of proteins in the body?

To provide structure and function

How many lectures are planned in the Biochemistry I course?

5

What is NOT allowed during the lecture?

Recording

What is the characteristic of the peptide bond that helps to stabilize protein structure?

Partial double-bond character

What type of proteolysis is caused by low pH and/or high temperatures?

Non-specific proteolysis

What is the primary function of trypsin in proteolysis?

Cleaving peptide bonds after a positively charged residue

What is the level of protein structure that refers to local folded structures that form within a polypeptide?

Secondary structure

What type of bond links the alpha carbon atom to the amino group and the carbonyl carbon in a polypeptide?

Single bond

What is the type of interaction that stabilizes the primary structure of a protein?

Covalent bonds

What is the characteristic of the side chains of hydrophobic amino acids?

Nonpolar

What is unique about the amino group of Proline?

It is a secondary amino group

Which type of amino acids have side chains with hydroxyl (OH) groups?

Hydrophilic

What is the general characteristic of the R group of amino acids that determines their classification?

Polarity

What is the characteristic of aromatic hydrophobic amino acids?

They have aromatic side chains

What is the characteristic of acidic amino acids?

They contain a carboxylic acid group

What is the basis of chemical classification of amino acids?

The nature of the R group and its polarity

What is the result of the reaction between the carboxylic group of one amino acid and the amino group of another amino acid?

The formation of a peptide bond

What is the isoelectric point (pI) of an amino acid?

The pH at which the amino acid has a net zero charge

What type of bond is formed between amino acids?

Peptide bond

What determines the pI of an amino acid?

The nature of the side chain

What is the primary force responsible for the tertiary structure of a protein?

Interactions between the R groups of the amino acids

Which type of bond is formed between the SH groups of two cysteine residues?

Disulfide bond

What is the role of disulfide bonds in protein structure?

To maintain tertiary and quaternary structures

What type of interactions are involved in the tertiary structure of a protein?

Ionic interactions, disulfide bonds, hydrophobic interactions, and hydrogen bonding

What is the final three-dimensional form of a protein due to?

The more complicated folding and super-folding of the polypeptide chain in its secondary level

Which of the following bonds is less strong than the peptide bond and is liable to denaturation?

Disulfide bond

This quiz is based on the introductory lecture of Biochemistry I, covering fundamental concepts and principles. It is designed for Level II students in the Faculty of Pharmacy. Test your understanding of the subject with this quiz!

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