For those wondering about the answer to the question (around 21:36) regarding the folding of ECM proteins, these proteins fall into the latter category as they have a distinct signal- encoding sequence on one end which results in their translocation to the ER lumen and subsequent folding
P = NP Sudoku analyzing if 2 cell checks as opposed to single cell checks or 3 is actually a lot more efficient with 2 crab pincers for finding pairs and greater in sudoku.
Hello. The module 2 required article "Molecular Chaperone Functions in Protein Folding and Proteostasis" discusses the benefits of Group I chaperonin GroEL on protein folding. It mentions that chaperonin cage accelerates protein folding by limiting the upper limit of space available for intermediates. Is there an intermolecular force between the chaperonin cage and the intermediate in such a system? Although the intermolecular force and the upper limit of space can make the intermediate more stable, thereby increasing the rate, how can you ensure that the protein still forms the most stable structure in thermodynamics in the chaperonin cage under such a limit?
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For those wondering about the answer to the question (around 21:36) regarding the folding of ECM proteins, these proteins fall into the latter category as they have a distinct signal- encoding sequence on one end which results in their translocation to the ER lumen and subsequent folding
Just for clarity, when she says things like "energy landscape" and "high energy" she's is always referring to Gibb's free energy, not just energy.
Dear madam I am IBNEY ALI from India I am seeing all Biochemistry lecture you are very good explaner
P = NP
Sudoku analyzing if 2 cell checks as opposed to single cell checks or 3 is actually a lot more efficient with 2 crab pincers for finding pairs and greater in sudoku.
After it is solved
Hello. The module 2 required article "Molecular Chaperone Functions in Protein Folding and Proteostasis" discusses the benefits of Group I chaperonin GroEL on protein folding. It mentions that chaperonin cage accelerates protein folding by limiting the upper limit of space available for intermediates. Is there an intermolecular force between the chaperonin cage and the intermediate in such a system? Although the intermolecular force and the upper limit of space can make the intermediate more stable, thereby increasing the rate, how can you ensure that the protein still forms the most stable structure in thermodynamics in the chaperonin cage under such a limit?
I hope I pursuing my PhD under your supervision
She has better handwriting using chalk than me using a pen.
using left hand?