BPK 110 Chapter Notes - Chapter 6: Acidosis, Zymogen, Chymotrypsinogen

50 views3 pages

sapphiresnake846

19 Sep 2012

School

Simon Fraser University

Department

Biomedical Physio & Kines

Course

BPK 110

Professor

Leah Esplen

For unlimited access to Textbook Notes, a Class+ subscription is required.

Document Summary

Wasting: the breaking down of body tissues to use as a protein source. Amino acids are the building blocks of proteins. Indispensable amino acids: the 9 amino acids which the body cannot make. Amino acids (total of 20) builds proteins. Dispensable amino acids: the 11 amino acids which the body can produce. Conditionally indispensable amino acids: amino acids that are normally dispensable, are made indispensable under special circumstances. Form generally consists of 1h, 1cooh, 1nh2, 1unique group. Peptide bond: the bond between two amino acids: releases water during bonding. Dipeptide: two amino acids joined by a peptide bond. Tripeptide: three amino acids joined by a peptide bond. Shape of the protein determines its function. Hydrophilic amino acids: amino acids that are attracted to water. Hydrophobic amino acids: amino acids repelled by water. Disulfide bridge: (sulfur) bond which stabilizes the structure of protein. Denaturing a protein"s shape causes it to lose its function. May be enzymes, hormones, antibodies, fluid balancers, transporters.

Related Questions

Why donât free amino acids have peptide bonds? What is a free amino acid exactly?

Which of the following is true of the number of ATP/GTP required during translation?

A. Translation of a 9 Amino acid protein will require 9 ATP/GTP to initiate.

B. Translation of a 9 Amino acid protein will require 9 ATP/GTP to bring tRNAs with amino acids into the ribosome.

C. Translation of a 9 Amino acid protein will require 9 ATP/GTP to form peptide bonds.

D. Translation of a 9 Amino acid protein will require 9 ATP/GTP to translocate.

E. Translation of a 9 Amino acid protein will require 27 ATP/GTP total.

1. A polypeptide chain has a large percentage of acidic and basic amino acids in it. The R groups of these amino acids form ionic interactions, which helps the protein to maintain itâs structure. This particular polypeptide works well under an optimum pH of 7. Ignoring effects of strong acids and bases on peptide bonds, what will happen to the tertiary structure of the protein if you move it stomach acid, which has a pH of 1-2. Why? Be specific regarding what influence the pH will have on the bonds maintaining tertiary structure in the molecule. Include the amino acid charges of the acidic and basic amino acids at the acidic pH, as well as the concept of pK in your answer. Assume that acidic amino acids have a pK of approximately 4.7 and basic amino acids have a pK of approximately 10.

2. Ignoring peptide length (or lack thereof) where would this portion of a polypeptide be most likely to be found: On the inside or on the outside surface of a protein floating around in the cytoplasm? Explain

3. A mutation occurs in the SRC kinase such that the tyrosine on the loop over the active site is changed to aspartic acid. This mutation mimics phosphorylation.
a. knowing what you know about the properties of phosphate groups and aspartic acid, why does aspartic acid mimic phosphorylation?
b. What would be the implication of this mutation on the function of the SRC kinase?

BPK 110 Chapter Notes - Chapter 6: Acidosis, Zymogen, Chymotrypsinogen

Document Summary

Get access

Related Documents

BPK 110 Chapter Notes - Chapter 6: Essential Amino Acid, Nitrogen Balance, Side Chain

BPK 110 Study Guide - Final Guide: Salt, Biotin, Hallucination

LIFESCI 2N03 Chapter Notes - Chapter 4: Aspartic Acid, Asparagine, Protein Digestibility Corrected Amino Acid Score

Related Questions