Scribd Logo
Upload

Welcome to Scribd!

  • 46 views

    MC 2 Worksheet Week 4

    Uploaded by

    Leah Mariz Roca
    This document discusses proteins and their structure. It begins by asking questions about proteins, such as their abundance and denaturing agents. It then expands on answers about protein solubility and denaturation and renaturation. Finally, it concludes by discussing the four levels of protein structure - primary, secondary, tertiary, and quaternary structure.

    Copyright:

    © All Rights Reserved
    Download as PDF, TXT or read online from Scribd

    MC 2 Worksheet Week 4

    Uploaded by

    Leah Mariz Roca
    46 views3 pages
    This document discusses proteins and their structure. It begins by asking questions about proteins, such as their abundance and denaturing agents. It then expands on answers about protein solubility and denaturation and renaturation. Finally, it concludes by discussing the four levels of protein structure - primary, secondary, tertiary, and quaternary structure.

    Original Title

    MC 2 WORKSHEET WEEK 4

    Copyright

    © © All Rights Reserved

    Available Formats

    PDF, TXT or read online from Scribd

    Did you find this document useful?

    Is this content inappropriate?

    This document discusses proteins and their structure. It begins by asking questions about proteins, such as their abundance and denaturing agents. It then expands on answers about protein solubility and denaturation and renaturation. Finally, it concludes by discussing the four levels of protein structure - primary, secondary, tertiary, and quaternary structure.

    Copyright:

    © All Rights Reserved
    Download as PDF, TXT or read online from Scribd
    Download as pdf or txt
    46 views3 pages

    MC 2 Worksheet Week 4

    Uploaded by

    Leah Mariz Roca
    This document discusses proteins and their structure. It begins by asking questions about proteins, such as their abundance and denaturing agents. It then expands on answers about protein solubility and denaturation and renaturation. Finally, it concludes by discussing the four levels of protein structure - primary, secondary, tertiary, and quaternary structure.

    Copyright:

    © All Rights Reserved
    Download as PDF, TXT or read online from Scribd
    Download as pdf or txt
    You are on page 1of 3

    ST.

    JOHN PAUL II COLLEGE OF DAVAO

    COLLEGE OF NURSING

    Physically Detached Yet Academically Attached

    WEEK 4

    LET’S INITIATE!
    Activity 1. Answer the following questions based on your understanding of
    the topics presented. Write your answers after each question.

    1. What is the most abundant biological macromolecules, occurring in


    all cells?
    Proteins are the most abundant biological macromolecules, occurring in
    all cells.

    2. Give at least 1 chemical agent as denaturing agent of protein?

    Proteins can be denatured by agents such as heat and urea that cause
    unfolding of polypeptide chains without causing hydrolysis of peptide
    bonds.

    3. When proteins are denatured by heat, they form insoluble aggregates


    known as?
    When proteins are denatured by heat, they form insoluble aggregates
    known as coagulum.

    MC 2- WORKSHEET| 1
    ST. JOHN PAUL II COLLEGE OF DAVAO

    COLLEGE OF NURSING

    Physically Detached Yet Academically Attached

    LET’S INQUIRE!
    Activity 1. Expound your answers to the following questions.

    1. Explain the solubility of proteins in water.


    The relationship of proteins with water is complex. The secondary structure of
    proteins depends largely on the interaction of peptide bonds with water through
    hydrogen bonds. Hydrogen bonds are also formed between protein (alpha and beta
    structures) and water. The proteinrich static ball is more soluble than the helical
    structures. At the tertiary structure, water causes the orientation of the chains and
    hydrophilic radicals to the outside of the molecule, while the hydrophobic chains
    and radicals tend to react with each other within the molecule (hydrophobic effect).

    2. Discuss Denaturation and Renaturation.


    Proteins can be denatured by agents such as heat and urea that cause unfolding of
    polypeptide chains without causing hydrolysis of peptide bonds. The denaturing
    agents destroy secondary and tertiary structures, without affecting the primary
    structure.If a denatured protein returns to its native state after the denaturing agent
    is removed, the process is called renaturation.

    LET’S INFER!
    Activity 1. Based on the subject matter presented, in conclusion,
    accomplish the item:

    1. Discuss the Protein Structure.

    The linear sequence of amino acid residues in a polypeptide chain determines the
    three-dimensional configuration of a protein, and the structure of a protein
    determines its function.All proteins contain the elements carbon, hydrogen,oxygen,
    nitrogen and sulfur some of these may also contain phosphorus, iodine, and traces of
    metals like ion, copper, zinc and manganese. MC 2- WORKSHEET| 2
    ST. JOHN PAUL II COLLEGE OF DAVAO

    COLLEGE OF NURSING

    Physically Detached Yet Academically Attached

    A protein may contain 20 different kinds of amino acids. Each amino acid has an
    amine group at one end and an acid group at the other and a distinctive side chain.
    The backbone is the same for all amino acids while the side chain differs from one
    amino acid to the next.

    The structure of proteins can be divided into four levels of organization:


    1. Primary Structure
    2. Secondary Structure
    3. Tertiary Structure
    4. Quaternary Structure

    MC 2- WORKSHEET| 3

    You might also like