Podcast
Questions and Answers
What type of bond is formed between the α-amino and carboxyl groups of amino acids?
What type of bond is formed between the α-amino and carboxyl groups of amino acids?
What is the result of the reaction between Gly and Ala?
What is the result of the reaction between Gly and Ala?
Which type of interaction is characterized by the sharing of electrons?
Which type of interaction is characterized by the sharing of electrons?
What causes denaturation in proteins due to temperature changes?
What causes denaturation in proteins due to temperature changes?
Signup and view all the answers
Which of the following describe the denaturation effect due to pH changes?
Which of the following describe the denaturation effect due to pH changes?
Signup and view all the answers
What is an example of a denaturing agent used in laboratories to study proteins?
What is an example of a denaturing agent used in laboratories to study proteins?
Signup and view all the answers
Which type of interaction occurs at distances of 3-5 Å?
Which type of interaction occurs at distances of 3-5 Å?
Signup and view all the answers
What is the energy range (in kcal/mol) associated with covalent bonds?
What is the energy range (in kcal/mol) associated with covalent bonds?
Signup and view all the answers
Study Notes
Peptide and Peptide Bonds
- Amino acids are covalently linked forming an amide bond between the α-amino and carboxyl groups.
- This bond is called a peptide bond.
- The products formed from amino acid unions are called peptides.
- Linking two amino acids creates a dipeptide (e.g., Gly-Ala).
- This reaction is considered a simple elimination of a water molecule.
Protein Structures and Interactions
-
Table of Protein Interactions
- Type | Mechanism | Energy (kcal/mol) | Interaction Distance (Å) | Interacting groups
- Covalent | Electron sharing | 30-100 | 1-2 | C-C, C-N, C=O, C-S, C-N-C
- Electrostatic/Salt Bridges | Coulombic attraction between opposite charges | 10-20 | 2-3 | -NH3+, -COO-
- Hydrogen Bonds | Shared hydrogen between electronegative atoms | 2-10 | 2-3 | -N-H···O=C-, -N-H···O-H
- Van der Waals | Induced dipole moments in polar groups | 1-3 | 3-5 | Polar groups
Protein Denaturation
- Temperature Changes: Heat is a common denaturing agent used in food processing assisting in protein digestion. It also disables inhibitors.
- pH Changes: A change in pH can lead to significant protein conformation modifications due to ionization changes in charged side chains and affect the amount of stabilizing salt bridges.
- Detergents: Denaturing proteins with detergents, (e.g., SDS), is common in lab settings. Detergents' amphiphilic nature helps with this process.
Studying That Suits You
Use AI to generate personalized quizzes and flashcards to suit your learning preferences.
Description
Explore the fundamental concepts of peptide bonds, amino acid interactions, and protein structures in this biochemistry quiz. Understand the mechanisms and energy associated with various types of protein interactions, crucial for studying biological processes. Test your knowledge on the basics of protein formation and denaturation.