Home Site Map Contact Us
Rapid Learning Member Login  
Rapid Learning Blog Rapid Learning on Facebook Rapid Learning on Youtube Rapid Learning on Twitter
 How to Learn in 24 Hours?

 Need Help?
M-F: 9am-5pm(PST):
Toll-Free: (877) RAPID-10
US Direct: (714) 692-2900
Int'l: 001-714-692-2900


24/7 Online Technical Support:
The Rapid Support Center

Secure Online Order:
Buy Now

 

 Got Questions?
Frequently Asked Questions
 Need Proof?
Testimonials by Our Users

Trustlink is a Better Business Bureau Program.
Rapid Learning Center is a fivr-star business.

External TrustLink Reviews




 Member Login:
User ID: 
Password: 
 

 Rapid Learning Courses:

MCAT in 24 Hours (2015-16)

USMLE in 24 Hours (Boards)

Chemistry in 24 Hours

Biology in 24 Hours

Physics in 24 Hours

Mathematics in 24 Hours

Psychology in 24 Hours

SAT in 24 Hours

ACT in 24 Hours

AP in 24 Hours

CLEP in 24 Hours

DAT in 24 Hours (Dental)

OAT in 24 Hours (Optometry)

PCAT in 24 Hours (Pharmacy)

Nursing Entrance Exams

Certification in 24 Hours

eBook - Survival Kits

Audiobooks (MP3)


 Tell-A-Friend:
Have friends taking science and math courses too? Tell them about our rapid learning system.


All about Proteins

Topic Review on "Title":

Amino acids – Building blocks
All amino acids incorporated into proteins by organisms are in the L form. All amino acids have acidic and basic functional groups. All amino acids except glycine have a chiral center. The pka for a functional group is the pH at which acidic or basic groups on 50 % of the molecules in a solution are deprotonated.

3D structures and conformation
Proteins are complex structures. Average protein contains 300 amino acids. Average amino acid contains 8 heavy atoms. Average structure contains 2400 atoms. X ray crystallography and NMR spectroscopy are the techniques which allow getting atomic resolution pictures of proteins.

Protein folding
Protein molecules fold by interacting between atoms within the protein chains and by interacting between the protein and the solvent. The forces involved are van der waals forces, disulphide bonds, hydrogen bonds, electrostatic attraction, and hydrophobic interactions. Defect in primary structure of proteins may arise due to mutations. Sickle cell anemia is a defect in the hemoglobin – a protein found in RBCs. Change in primary sequence decreases protein solubility and protein aggregates. For a protein of n residues, there are 20n possible sequences. It can fold into any pattern which is decided by its function.

Covalent backbone and sequence
Alpha helix is formed by hydrogen bonds. Backbone does not follow any actual bonds. They are used for structural super impositions. Peptide bond has a partial double bond character

Protein functions
Proteins are divided based on their functions. Ex: Collagen, fibrous protein is classified under structural proteins. The globular proteins have a number of biologically important roles. Myoglobulin is present in the muscle and hemoglobin in the RBC. Proteins act as biocatalyst – enzymes. They regulate metabolism too.


Rapid Study Kit for "Title":
Flash Movie Flash Game Flash Card
Core Concept Tutorial Problem Solving Drill Review Cheat Sheet

"Title" Tutorial Summary :

All amino acids incorporated into proteins by organisms are in the L form. All amino acids have acidic and basic functional groups. Average protein contains 300 amino acids. X ray crystallography and NMR spectroscopy allow getting atomic resolution pictures of proteins. Protein molecules fold by interacting between atoms within the protein chains and by interacting between the protein and the solvent. The forces involved are van der waals forces, disulphide bonds, hydrogen bonds, electrostatic attraction, and hydrophobic interactions. Defect in primary structure of proteins may arise due to mutations. Alpha helix is formed by hydrogen bonds. Peptide bond has a partial double bond character. Proteins are divided based on their functions. Ex: Collagen, fibrous protein is classified under structural proteins. The globular proteins have a number of biologically important roles. Myoglobin is present in the muscle and hemoglobin in the RBC. Proteins act as biocatalyst – enzymes. They regulate metabolism too.


Tutorial Features:
  • Classification based on functions and forces involved in the 3D structure.
  • Diagrams describing sickle cell anemia are shown.
  • Diagrams to show the structural role of fibrous proteins.
  • Structures of hemoglobin, membrane proteins and collagen are shown.

"Title" Topic List:

Amino acids – Building blocks

  • Structure
  • Classification
  • Handedness
  • pka

3D structures and conformation

  • Protein structure hierarchical levels
  • Proteins are complex structures
  • Solving protein structures
  • Making a polypeptide

Protein folding

  • Forces involved
  • Vander Waals forces
  • Protein folding
  • Significance of a sequence
  • Sickle cell anemia
  • Sickle cell Hb

Covalent backbone and sequence

  • Side chain nomenclature
  • Backbone
  • Polypeptide backbone
  • Peptide bond
  • Ramachandran’s plot

Protein functions

  • Functional classes
  • Collagen – Fibrous protein
  • Fibrous proteins have a structural role
  • Membrane protein
  • Globular protein
  • Myoglobin and Hemoglobin
  • Hemoglobin
  • Proteins for cell mobility
  • Proteins regulate metabolism
  • Protein as a biocatalyst


See all 24 lessons in college chemistry, including concept tutorials, problem drills and cheat sheets:
Teach Yourself Biochemistry Visually in 24 Hours

© 2016 Rapid Learning Inc. All rights reserved         Disclaimer | Privacy Policy | Affiliates