Beta pleated sheet || Secondary structure of protein

Sdílet
Vložit
  • čas přidán 14. 03. 2021
  • This video describes the structural features of beta pleated sheet which is one type of secondary structure of protein. The beta sheet, (β-sheet) (also β-pleated sheet) is a common motif of the regular protein secondary structure. Beta sheets consist of beta strands (β-strands) connected laterally by at least two or three backbone hydrogen bonds, forming a generally twisted, pleated sheet. A β-strand is a stretch of polypeptide chain typically 3 to 10 amino acids long with backbone in an extended conformation. The supramolecular association of β-sheets has been implicated in the formation of the fibrils and protein aggregates observed in amyloidosis, notably Alzheimer's disease.

Komentáře • 29

  • @alexlee3511
    @alexlee3511 Před 2 lety +2

    Hi sir, I wanna know the actual arrangement of amino acids in a polypeptide. As I see many of them in online are arranged in a form like all R groups are pointed upward, I think it may make no sense. So I wanna know if all the amino acid should be placed like R group 1 upward, R group 2 downward, R group 3 upward, etc.?

  • @romanperez2814
    @romanperez2814 Před 3 lety +2

    Excellent video Dr!
    Saludos!

  • @advaithar3058
    @advaithar3058 Před 2 lety +1

    dimer formed between 2 beta pleated sheet in called as?

  • @derpydogz0259
    @derpydogz0259 Před 2 lety +3

    If the beta plated sheet is formed out of a characteristic all amino acids have (backbone polarity) then why aren’t all amino acids prone to immediately take the form of a beta sheet?

    • @matthew_quizon
      @matthew_quizon Před rokem +1

      ot all amino acids are prone to immediately form a beta sheet because the final three-dimensional structure of a protein is determined by a combination of factors including the sequence of amino acids, the strength of hydrogen bonds, and the interactions with the surrounding environment. Additionally, the formation of beta sheets depends on the stability of the sheet relative to other possible structures, such as alpha helices or coil regions, and other biophysical forces that can drive protein folding. Thus, while beta sheet formation is a possibility for many amino acids, it is not a guarantee and will depend on the specific conditions present during protein folding.

  • @biologyflavour5512
    @biologyflavour5512 Před 2 lety +1

    Sir you don't have explained about antiparallel beta pleated sheet 😢

  • @medicalbiochemistry_
    @medicalbiochemistry_ Před 3 lety +1

    Good job

  • @oluwatomioredein
    @oluwatomioredein Před 2 lety +2

    @3:15, is the top line supposed to say residues in beta pleated sheets as opposed to alpha helices, please?

  • @ziasatti5316
    @ziasatti5316 Před 2 lety +1

    Very informative lecture
    Love from pakistan❣️

    • @animatedbiologywitharpan
      @animatedbiologywitharpan  Před 2 lety

      Thanks a lot. Please share with your friends. Love ❤ from 🇮🇳 India. Please put your suggestions in the comments. I will try to make videos on that as well.

  • @asiakhatoon954
    @asiakhatoon954 Před 2 lety +2

    Thank you so much this video really helped me.

  • @abhinabsarma482
    @abhinabsarma482 Před měsícem +1

    Sir you didn't said anything about loops and turns as secondary structure, please make videos on this two

  • @David-zi9nr
    @David-zi9nr Před 3 lety +1

    Awesome 👍🏽

  • @sanughosh6540
    @sanughosh6540 Před 5 měsíci +1

    Thanks for the information

    • @animatedbiologywitharpan
      @animatedbiologywitharpan  Před 5 měsíci

      Could you please help me by sharing my contents with your friends group/ college group. I put huge efforts in making these videos but unfortunately not a lot of people are watching this.

  • @nanhelalgupta476
    @nanhelalgupta476 Před 3 lety +1

    🤩🙏

  • @rainbow4130
    @rainbow4130 Před 3 lety +1

    Thank U sir 🙏

  • @drranafatima7875
    @drranafatima7875 Před 2 lety +1

    Wonderful