Lecture 5 Web: pollev.com/ucibio Text: To: 37607 Type in: 169964.

Slides:



Advertisements
Similar presentations
Proteins Review. Learning outcomes (e) Describe the structure of an amino acid and the formation and breakage of a peptide bond. (f) Explain the meaning.
Advertisements

Biology 107 Macromolecules II September 9, Macromolecules II Student Objectives:As a result of this lecture and the assigned reading, you should.
1 September, 2004 Chapter 5 Macromolecular Structure.
The Structure and Functions of Proteins BIO271/CS399 – Bioinformatics.
Protein-a chemical view A chain of amino acids folded in 3D Picture from on-line biology bookon-line biology book Peptide Protein backbone N / C terminal.
Polypeptides – a quick review A protein is a polymer consisting of several amino acids (a polypeptide) Each protein has a unique 3-D shape or Conformation.
Biology 107 Macromolecules II September 8, 2003.
1. Primary Structure: Polypeptide chain Polypeptide chain Amino acid monomers Peptide linkages Figure 3.6 The Four Levels of Protein Structure.
Proteins Structures Primary Structure.
Protein Structure Elements Primary to Quaternary Structure.
Daily Starter  Explain how a peptide bond is formed. (What is the reaction called and how does it happen?)
Proteins: Levels of Protein Structure Conformation of Peptide Group
Housekeeping Your performance on the exam has caused me to re-evaluate how homework will be handled I will now be picking up every problem assigned on.
Diverse Macromolecules. V. proteins are macromolecules that are polymers formed from amino acids monomers A. proteins have great structural diversity.
Protein Secondary Structure Lecture 2/19/2003. Three Dimensional Protein Structures Confirmation: Spatial arrangement of atoms that depend on bonds and.
Proteins. Proteins? What is its How does it How is its How does it How is it Where is it What are its.
Protein “folding” occurs due to the intrinsic chemical/physical properties of the 1° structure “Unstructured” “Disordered” “Denatured” “Unfolded” “Structured”
Objectives E – Recall the different structures of proteins and the test for proteins. C – Describe how a peptide bond is formed. Describe the different.
AP Biology Proteins Multipurpose molecules Proteins Most structurally & functionally diverse group Function: involved in almost everything – enzymes.
D. NUCLEIC ACIDS 1.ARE MADE OF THE ELEMENTS C,H,O,N,P.
Protein Folding & Biospectroscopy F14PFB David Robinson Mark Searle Jon McMaster
AP Biology Proteins Multipurpose molecules.
CS790 – BioinformaticsProtein Structure and Function1 Review of fundamental concepts  Know how electron orbitals and subshells are filled Know why atoms.
AP Biology Proteins AP Biology Proteins Multipurpose molecules.
AP Biology Proteins. AP Biology Proteins  Most structurally & functionally diverse group of biomolecules  Function:  involved in.
Part I : Introduction to Protein Structure A/P Shoba Ranganathan Kong Lesheng National University of Singapore.
Protein Structure (Foundation Block) What are proteins? Four levels of structure (primary, secondary, tertiary, quaternary) Protein folding and stability.
AP Biology Proteins AP Biology Proteins Multipurpose molecules.
Chapter 4.1: Overview of Protein Structure CHEM 7784 Biochemistry Professor Bensley.
BIOLOGICALLY IMPORTANT MACROMOLECULES PROTEINS. A very diverse group of macromolecules characterized by their functions: - Catalysts - Structural Support.
A.P. Biology-Day 52 Take out your organic molecules packet Should high schools perform urine tests for steroids in athletes? How are you doing with memorizing.
Protein- Secondary, Tertiary, and Quaternary Structure.
Protein Structure and Bioinformatics. Chapter 2 What is protein structure? What are proteins made of? What forces determines protein structure? What is.
1 Proteins Proteins are polymers made of monomers called amino acids All proteins are made of 20 different amino acids linked in different orders Proteins.
Protein Structure  The structure of proteins can be described at 4 levels – primary, secondary, tertiary and quaternary.  Primary structure  The sequence.
Proteins pp Proteins Proteins are used for: Amino acids.
Proteins: 3D-Structure Chapter 6 (9 / 17/ 2009)
Physical-chemical properties of proteins; precipitation reactions.
Protein backbone Biochemical view:
Proteins Structure and Function. PROTEINS Proteins are essential to the structures and activities of life...
Levels of Protein Structure. Why is the structure of proteins (and the other organic nutrients) important to learn?
AP Biology Proteins AP Biology Proteins Multipurpose molecules.
Levels of Protein Structure. Why is the structure of proteins (and the other organic nutrients) important to learn?
WARM UP 1/29/16 1. Name the six functional groups. 2. Draw the STRUCTURAL formula for each one.
Structural organization of proteins
Four Levels of Protein Structure
CHM 708: MEDICINAL CHEMISTRY
Protein Structure BL
Chapter 5 Proteins.
Protein Proteins are found throughout living organisms.
Amino Acids and Proteins
Lecture 5 Web: pollev.com/ucibio Text: To: 37607
Proteins.
The Peptide Bond Amino acids are joined together in a condensation reaction that forms an amide known as a peptide bond.
Hierarchical Structure of Proteins
The Peptide Bond Amino acids are joined together in a condensation reaction that forms an amide known as a peptide bond.
. Nonpolar (hydrophobic) Nonpolar (hydrophobic) Amino Acid Side Chains
PROTEINS and ENZYMES!.
Proteins.
The Chemistry of Life Proteins
Diverse Macromolecules
Protein Structure Chapter 14.
PROTEINS.
Proteins.
Daily Science In forming a protein, why is it important that every amino acid has the same structure of a carboxyl group on one side and amino group on.
AMIDES.
Fig 3.13 Reproduced from: Biochemistry by T.A. Brown, ISBN: © Scion Publishing Ltd, 2017.
The Three-Dimensional Structure of Proteins
Protein Structure.
Four Levels of Protein Structure
Presentation transcript:

Lecture 5 Web: pollev.com/ucibio Text: To: Type in:

OK. What does this all have to do with enzymes? Anfinsen’s experiment Took a protein (AP) & forced it to unfold - Protein lost activity Therefore:______________________________ Allowed protein to recover - Over time, activity returned Therefore:______________________________

What does a protein need in order to fold? Protein folding information contained in primary amino acid sequence! OK. But how does amino acid sequence “fold?”

Peptide bond is planar…

…but not bonds on either side!

Rotation of bonds around peptide bond

Peptide backbone rotation

“Folding” proteins Amino acids have different properties Different preferred Psi and Phi angles Bonds can rotate and pivot

Secondary structure 3D structure H-bonds between C=O & N-H C=O & N-H of peptide bonds Close together in primary structure

Folding into secondary structures Bond rotation causes secondary structure  -helix  -sheet Bends, Loops, Disordered

The  -helix: Annotate Different parameters define  -helix

 -Sheet: Annotate

 -Sheets Sheets can be twisted

Bends / Loops Bends or Loops: Important Structured/Unstructured

Tertiary structrue Bring secondary structure elements together Hydrophobic interactions important Unstructured regions important

The  -helix Arrangement of side chains important

Tertiary structure

Tertiary structrue Take picture Upload to Dropbox assignment “Barrel structure”