Anabolics
Search More Than 6,000,000 Posts
Results 1 to 8 of 8

Thread: ?Cooking Eggs?

  1. #1
    BrownBomber's Avatar
    BrownBomber is offline Member
    Join Date
    Feb 2003
    Posts
    788

    ?Cooking Eggs?

    I really like meringues - quick to make, keep for a long time, taste great and an easy way to get some extra protein.

    Now, I have read all over that cooking eggs ,the typical morning meal of 10 eggwhites, does not affect the protein, so you cook 30 grams of protein worth you get 30 grams. Does anyone know if the process of making meringues (baking for 1 hour at 300 degrees) affects the protein, making it useless?

    Thanks
    BB

  2. #2
    bigsd67's Avatar
    bigsd67 is offline Anabolic Member
    Join Date
    Oct 2002
    Location
    CT
    Posts
    2,186
    well supposedly cooking food in any way somewhat denatures protein, however i wouldnt let it keep you up at night because all of us cook our food and we make progress, so i dont think baking your meringues is gonna kill you.

  3. #3
    cb25's Avatar
    cb25 is offline Banned
    Join Date
    Mar 2003
    Location
    AZ to MA...depends on whe
    Posts
    2,781
    Quote Originally Posted by bigsd67
    well supposedly cooking food in any way somewhat denatures protein, however i wouldnt let it keep you up at night because all of us cook our food and we make progress, so i dont think baking your meringues is gonna kill you.
    cooking protein does denature protein...this really doesn't have *that* big of an effect on our ability to assimilate the protein though...don't worry about it, eat up!

  4. #4
    bigsd67's Avatar
    bigsd67 is offline Anabolic Member
    Join Date
    Oct 2002
    Location
    CT
    Posts
    2,186
    Quote Originally Posted by cb25
    cooking protein does denature protein...this really doesn't have *that* big of an effect on our ability to assimilate the protein though...don't worry about it, eat up!
    basically what i was trying to convey...thanks for clarifying.

  5. #5
    daman1's Avatar
    daman1 is offline Diet Specialist
    Join Date
    Dec 2003
    Location
    beatin it up...
    Posts
    3,200
    As the other guys have said when you denature something you just change its native conformation, not it's ability to be used in the body. The most basic level of protein structure, called the primary structure, is the linear sequence of amino acids. Different sequences of the acids along a chain, however, affect the structure of a protein molecule in different ways. Forces such as hydrogen bonds, disulfide bridges, attractions between positive and negative charges, and hydrophobic ("water-fearing") and hydrophilic ("water-loving") linkages cause a protein molecule to coil or fold into a secondary structure, examples of which are the so-called alpha helix and the beta pleated sheet. When forces cause the molecule to become even more compact, as in globular proteins, a tertiary protein structure is formed. When a protein is made up of more than one polypeptide chain, as in hemoglobin and some enzymes, it is said to have a quaternary structure. Hope that sheds a little light on structure and etc...

  6. #6
    cb25's Avatar
    cb25 is offline Banned
    Join Date
    Mar 2003
    Location
    AZ to MA...depends on whe
    Posts
    2,781
    ahhhhhhhhhhhhhhhh!!!!!!! no more biochemistry!!!!!!!!!!!!!!!

    sorry, just had flashbacks from last semester when i read that...


    Quote Originally Posted by daman1
    As the other guys have said when you denature something you just change its native conformation, not it's ability to be used in the body. The most basic level of protein structure, called the primary structure, is the linear sequence of amino acids. Different sequences of the acids along a chain, however, affect the structure of a protein molecule in different ways. Forces such as hydrogen bonds, disulfide bridges, attractions between positive and negative charges, and hydrophobic ("water-fearing") and hydrophilic ("water-loving") linkages cause a protein molecule to coil or fold into a secondary structure, examples of which are the so-called alpha helix and the beta pleated sheet. When forces cause the molecule to become even more compact, as in globular proteins, a tertiary protein structure is formed. When a protein is made up of more than one polypeptide chain, as in hemoglobin and some enzymes, it is said to have a quaternary structure. Hope that sheds a little light on structure and etc...

  7. #7
    longhornDr's Avatar
    longhornDr is offline Member
    Join Date
    Feb 2003
    Location
    Galveston Texas
    Posts
    528
    All proteins are digested into peptides or individual AA before absorption so it makes no difference if the protein is denatured or not.

  8. #8
    bigsd67's Avatar
    bigsd67 is offline Anabolic Member
    Join Date
    Oct 2002
    Location
    CT
    Posts
    2,186
    well then i pose this question...i've heard from some people that drinking RTD drinks is somewhat useless cuz of the protein in them being pastuerized...now i dont drink them on a regular basis cuz they're pricey, but if im traveling they come in handy so i guess it's ok to drink them and get all the quality protein?

Thread Information

Users Browsing this Thread

There are currently 1 users browsing this thread. (0 members and 1 guests)

Posting Permissions

  • You may not post new threads
  • You may not post replies
  • You may not post attachments
  • You may not edit your posts
  •