BIOL1006 Lecture Notes - Lecture 3: Egg White, Covalent Bond, Pepsin

30 views2 pages
9 Aug 2016
Lecture 3
Each protein has its own unique sequence of amino acids
and the interactions between these amino acids create a
specify shape.
This shape determines the protein's function, from
digesting protein in the stomach to carrying oxygen in
the blood.
If the protein is subject to changes in temperature, pH,
or exposure to chemicals, the internal interactions
between the protein's amino acids can be altered, which
in turn may alter the shape of the protein.
Although the amino acid sequence does not change, the
protein's shape may change so much that it becomes
dysfunctional, in which case the protein is considered
Pepsin, the enzyme that breaks down protein in the
stomach, only operates at a very low pH. At higher pHs
pepsin's conformation, the way its polypeptide chain is
folded up in three dimensions, begins to change.
The stomach maintains a very low pH to ensure that
pepsin continues to digest protein and does not denature.
Because almost all biochemical reactions require
enzymes, and because almost all enzymes only work
optimally within relatively narrow temperature and pH
ranges, many homeostatic mechanisms regulate
appropriate temperatures and pH so that the enzymes
can maintain the shape of their active site.
find more resources at
find more resources at
Unlock document

This preview shows half of the first page of the document.
Unlock all 2 pages and 3 million more documents.

Already have an account? Log in

Get access

$10 USD/m
Billed $120 USD annually
Homework Help
Class Notes
Textbook Notes
40 Verified Answers
Study Guides
1 Booster Class
$8 USD/m
Billed $96 USD annually
Homework Help
Class Notes
Textbook Notes
30 Verified Answers
Study Guides
1 Booster Class