Study Guides (258,837)
CA (124,996)
UTSG (8,541)
BIO (362)
BIO130H1 (91)

BIO130 Section One Guide (3)

4 Pages
141 Views

Department
Biology
Course Code
BIO130H1
Professor
Kenneth Yip

This preview shows page 1. Sign up to view the full 4 pages of the document.
Chapter 3 Proteins
(pg. 125-152)
-Proteins such as kinesin propel organelles through the cytoplasm, topoisomerase
untangles knotted DNA molecules
The Shape and Structure of Proteins
The Shape of a Protein Is Specified by Its Amino Acid Sequence
-Proteins are long polymers of amino acids linked by peptide bonds, and they are
always written with the N-terminus toward the left
-* special case: two cysteine side chains can form disulfide bonds
Proteins Fold into a Conformation of Lowest Energy
-The final folded structure, or conformation , of any polypeptide chain is generally
the one that minimizes its free energy
-In living cells, special proteins called molecular chaperones often assist in protein
folding
oAlso prevent exposed hydrophobic regions in newly synthesized protein
chains from associating with each other to form protein aggregates
-Proteins are generally between 50-2000 amino acids long
oLarge proteins consist of protein domains which fold mostly independent of
each other
The α Helix and the Sheet are Common Folding Patterns
-α helix was found in the protein α-keratin, abundant in skin, hair, nails, horns
- sheet was found in the protein fibroin, the major constituent of silk
oboth patterns result from hydrogen bonding between N-H and C=O groups in
the polypeptide backbone
- sheets (forming the core of many proteins) can form either (via hydrogen bonds):
1. from neighbouring polypeptide chains running in the same orientation
(parallel)
2. from a polypeptide chain that folds back and forth upon itself (anti-
parallel chains)
-αhelix is made through twisting a single polypeptide chain around to form a rigid
cylinder
oA hydrogen bond is formed every 4th peptide bond (N-H and C=O)
oComplete turn every 3.6 amino acids
oFound in cell membranes (transport proteins, receptors)
www.notesolution.com

Loved by over 2.2 million students

Over 90% improved by at least one letter grade.

Leah — University of Toronto

OneClass has been such a huge help in my studies at UofT especially since I am a transfer student. OneClass is the study buddy I never had before and definitely gives me the extra push to get from a B to an A!

Leah — University of Toronto
Saarim — University of Michigan

Balancing social life With academics can be difficult, that is why I'm so glad that OneClass is out there where I can find the top notes for all of my classes. Now I can be the all-star student I want to be.

Saarim — University of Michigan
Jenna — University of Wisconsin

As a college student living on a college budget, I love how easy it is to earn gift cards just by submitting my notes.

Jenna — University of Wisconsin
Anne — University of California

OneClass has allowed me to catch up with my most difficult course! #lifesaver

Anne — University of California
Description
Chapter 3 Proteins (pg. 125-152) - Proteins such as kinesin propel organelles through the cytoplasm, topoisomerase untangles knotted DNA molecules The Shape and Structure of Proteins The Shape of a Protein Is Specified by Its Amino Acid Sequence - Proteins are long polymers of amino acids linked by peptide bonds, and they are always written with the N-terminus toward the left - * special case: two cysteine side chains can form disulfide bonds Proteins Fold into a Conformation of Lowest Energy - The final folded structure, or conformation, of any polypeptide chain is generally the one that minimizes its free energy - In living cells, special proteins called molecular chaperonesoften assist in protein folding o Also prevent exposed hydrophobic regions in newly synthesized protein chains from associating with each other to form protein aggregates - Proteins are generally between 50-2000 amino acids long o Large proteins consist of protein domains which fold mostly independent of each other The Helix and the Sheet are Common Folding Patterns - helix was found in the protein -keratin, abundant in skin, hair, nails, horns - sheet was found in the protein fibroin, the major constituent of silk o both patterns result from hydrogen bonding between N-H and C=O groups in the polypeptide backbone - sheets (forming the core of many proteins) can form either (via hydrogen bonds): 1. from neighbouring polypeptide chains running in the same orientation (parallel) 2. from a polypeptide chain that folds back and forth upon itself (anti- parallel chains) - helix is made through twisting a single polypeptide chain around to form a rigid cylinder o A hydrogen bond is formed every 4 peptide bond (N-H and C=O) o Complete turn every 3.6 amino acids o Found in cell membranes (transport proteins, receptors) www.notesolution.com
More Less
Unlock Document


Only page 1 are available for preview. Some parts have been intentionally blurred.

Unlock Document
You're Reading a Preview

Unlock to view full version

Unlock Document

Log In


OR

Don't have an account?

Join OneClass

Access over 10 million pages of study
documents for 1.3 million courses.

Sign up

Join to view


OR

By registering, I agree to the Terms and Privacy Policies
Already have an account?
Just a few more details

So we can recommend you notes for your school.

Reset Password

Please enter below the email address you registered with and we will send you a link to reset your password.

Add your courses

Get notes from the top students in your class.


Submit