HOME ORDER PREVIEW REVIEW ABOUT CONTACT

 TOLL-FREE INFO & ORDERING:
M-F: 9am-5pm (PST):
(877) RAPID-10


 24/7 Technical Support:

 Rapid Learning Member Access:

Rapid Learning Member Login
Note: If you are a legacy user of chemistry24 members, please request a new login access to the premium server with your full name and old login email via vip@rapidlearningcenter.com

 Rapid Courses:
Biology in 24 Hours Chemistry in 24 Hours Physics in 24 Hours Mathematics in 24 Hours

 Weekly Biology Tips:
Want to learn all the tips and tricks on biology mastery? Learn from the insiders and gain unfair advantage over your peers. This free newsletter is specifically designed for students who are taking biology. Start having the tips delivered to your inbox weekly, enter your name and email below to subscribe:

 

Your Name  
Email  
 

 Other Related Sites:

 Biology Study Lounge:
These study sheets are for quick review on the subjects. Refer to our rapid courses for comprehensive review.

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 biology, including concept tutorials, problem drills and cheat sheets:
Teach Yourself Biochemistry Visually in 24 Hours

   © 2014 Rapid Learning Center. Privacy | Disclaimer Home | Order | Preview | Review | About | Contact
  Chemistry Survival, Biology Survival, Physics Survival and
Mathematics Survival Publishing are the divisions of Rapid Learning Inc.