Docsity
Docsity

Prepare for your exams
Prepare for your exams

Study with the several resources on Docsity


Earn points to download
Earn points to download

Earn points by helping other students or get them with a premium plan


Guidelines and tips
Guidelines and tips

Protein Structure - Introductory Biology - Lecture Slides, Slides of Biology

These are the important key points of lecture slides of Introductory Biology are: Protein Structure, Primary Structure, Secondary Structure, Tertiary Structure, Quaternary Structure, Amino Acids, Hydrogen, Alpha Helixes, Lower Level Secondary, Disulfide Bridges

Typology: Slides

2012/2013

Uploaded on 01/10/2013

devraaj
devraaj 🇮🇳

4.5

(15)

72 documents

1 / 14

Toggle sidebar

This page cannot be seen from the preview

Don't miss anything!

bg1
Protein Structure
Docsity.com
pf3
pf4
pf5
pf8
pf9
pfa
pfd
pfe

Partial preview of the text

Download Protein Structure - Introductory Biology - Lecture Slides and more Slides Biology in PDF only on Docsity!

Protein Structure

  • Protein structure is represented in a hierarchal scheme comprised of four levels: primary, secondary, tertiary and quaternary
  • Primary structure
  • The linear sequence of amino acids comprising a protein
  • Secondary structure
  • The regular repeating patterns of hydrogen-bonded backbone conformations
  • Tertiary structure
  • The packing of secondary structure elements to form a folded protein - Quaternary structure
  • The relative arrangement of two or more individual polypeptide chains

Overview of Protein Structure

Secondary Structure

  • Are structures formed due to hydrogen bonding between amino acids.
  • The two most common secondary structures are alpha-helixes and pleated sheets.

Tertiary Structure

  • The 3d conformation of a polypetide including the its lower level secondary structures.
  • May involve covalent bonding in the form of disulfide bridges between cysteine amino acid residues.

Quaternary Structure

  • The association of two or more polypeptides in 3d space.

Protein folding

  • Protein folding is very complex, so complex even our most powerful computers are quite up to simulating it…yet.
  • The final conformation is determined by the interaction between the amino acids and their environment.
  • Amino acids can be polar, non-polar, charged, acidic or basic, hydrophobic or hydrophilic. These vary properties contribute to how the protein will fold.

Why is folding so hard to simulated

  • The number of possible conformation increases exponentially as the polypeptide length increases.
  • There are many interactions – with water, other amino acids within the polypeptide, with chaperone proteins that help proteins fold.
  • When computing power increases it will be possible to simulate protein folding properly. This will allow us to design our own proteins.