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- On average, how many phosphoanhydride bonds (P;-P; bonds) are directly hydrolyzed in thecourse of synthesizing a 200 amino acid protein? Assume that you begin with the mature mRNA,ribosomal subunits, tRNAs, free amino acids, and all necessary factors.Exploring the nuanced landscape of protein dynamics, could you elaborate on noteworthy post-translational modifications (PTMs)? I'm interested in understanding specific examples of PTMs and gaining insights into their functional mechanisms. This inquiry delves into the intricate aspects of protein modulation within a biological context."What is Protein folding? Give at least 3 diseases that results from protein misfolding. Explain each. Can you give me a brief explanation about this question? Not less than 3 sentences.
- You have isolated a new protein called STICKY. You can predict from comparisons with other known proteins that STICKY contains a bHLH domain. Predict the function of STICKY and rationale forthe importance of these domains in STICKY function.you have isolated a new protein called STICKY. you can predict from comparisons with other known proteins that STICKY contains bHLH domain. Predict the function of STICKY and rationale forthe importnce of these domains in sticky function.An intermediate folding stage seen in protein denaturation or renaturation is called : a) domain b) motif c) subunit d) molten globule Proteins which do not renature spontaneously when denaturation conditions are removed may need the assistance of: a) a prosthetic group b) a higher salt concentration c) a lower temperature d) a chaperone protein The information needed for correct protein folding is encoded in: a) the surrounding molecules b) the protein’s amino acid sequence c) the pH of the aqueous medium d) the electrolyte composition of the aqueous solution
- Which factor has NOT been shown to play a role in determining the specificity of protein kinases? a. protein tertiary structure b. protein quaternary structure c. primary sequence at phosphorylation site d. disulfide bonds near the phosphorylation site e. residues near the phosphorylation siteA protein-ligand binding reaction is run. At equilibrium, half the protein is ligand bound, the unboundligand concentration is 0.657 nM. Calculate the koff value for this reaction. Assume the kon value is typical ofprotein-ligand interactions.In the ER lumen nascent polypeptide chains are kept from misfolding or aggregating until an entire domain or polypeptide is completed and can fold properly. true false
- ..You have isolated a new protein called STICKY. You can predict from comparisons with other known proteins thatSTICKY contains a bHLH domain.Predict the function of STICKY and rationale for the importance of these domains in STICKY function.. ..The proteasome is a multi-subunit machine that unfolds and degrades proteins. How is its activity regulated such that it only degrades certain proteins?Given the peptide Val-Ser-Gln-Lys The lateral chain of one of these amino acids can be modified by N-acetylation. Write the semi‐developed form of the lateral chain of this modified amino acid at pH 7 The lateral chain of one of these amino acids can be modified by phosphorylation. Write the semi‐developed form of the lateral chain of this modified amino acid at pH 7.