kindly refer to the photo attached. thank you! Match the concepts with their definitions or examples.Match each item to a choice:6N HCIelastinlipotropinrhodopsinceruloplasmincarboxypeptidaseperformic acidtertiaryphaseolinsecalineChoices:i a structural proteini a receptor proteini cuts peptide bonds1 an albumini highest level of structure for 1 polypeptide# cuts C-terminal amino acid# a metalloproteini a prolamine! a hormone# cuts disulfide linkages

6N HCl: Cut peptide bonds (Highly concentrated HCl use to digest/hydrolyze protein molecules as it…

Match each item to a choice: 6N HCI elastin lipotropin rhodopsin ceruloplasmin carboxypeptidase performic acid tertiary phaseolin secaline Choices: # a structural protein # a receptor protein # cuts peptide bonds # an albumin # highest level of structure for 1 polypeptide I cuts C-terminal amino acid I a metalloprotein # a prolamine I a hormone # cuts disulfide linkages

Match each item to a choice: 6N HCI elastin lipotropin rhodopsin ceruloplasmin carboxypeptidase performic acid tertiary phaseolin secaline Choices: # a structural protein # a receptor protein # cuts peptide bonds # an albumin # highest level of structure for 1 polypeptide I cuts C-terminal amino acid I a metalloprotein # a prolamine I a hormone # cuts disulfide linkages

Biochemistry

6th Edition

ISBN:9781305577206

Author:Reginald H. Garrett, Charles M. Grisham

Publisher:Reginald H. Garrett, Charles M. Grisham

Chapter31: Completing The Protein Life Cycle: Folding, Processing, And Degradation

Section: Chapter Questions

Problem 3P: Understanding the Relevance of Chaperones in Protein Folding Protein molecules, like all molecules,...

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Give at least 10 functions of protein and describe each function. Cite an example for each function if there are any.
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Understanding the Relevance of Chaperones in Protein Folding Protein molecules, like all molecules, can be characterized in terms of general properties such as size, shape, charge, solubility/hydrophobicity. Consider the influence of each of these general features on the likelihood of whether folding of a particular protein will require chaperone assistance or not. Be specific regarding just Hsp7O chaperones or Hsp7O chaperones and Hsp60 chaperonins.
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Need help The β chains of HbA and HbS were treated with trypsin, and the sequence of the N-terminal tryptic peptides are as given below. Do these peptides separate from each other in an electric field if the pH is 7.0? Explain in detail the reasoning behind your answer and include your calculations for the charge of each peptide in your answer. HbA: Val-His-Leu-Thr-Pro-Glu-Glu-Lys HbS: Val-His-Leu-Thr
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had a response from a peer and this is what they said: You mentioned that aliphatic amino acids play a role in protein folding and stability by forming together in the protein's hydrophobic core. Could you elaborate on how this process works and provide more details on the structural aspects involved in this interaction? I am not too sure how to respond to this. Thank you.
Hydropathy plot analysis of your protein of interest reveals a single, prominent hydrophobic peak. However, you later discover that this protein is soluble and not membrane associated. Explain how the hydropathy plot may have been misleading.
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