BIND  TRANSFORM  RELEASE

Slides:



Advertisements
Similar presentations
The Chemical Nature of Enzyme Catalysis
Advertisements

Review Enzymes are specific to a substrate Based on shape (lock & key) Enzymes are NOT consumed or changed by catalyzed reaction Great for speeding up.
PROTEIN PHYSICS LECTURE 24 PROTEINS AT ACTION: BIND  TRANSFORM  RELEASE.
Catalytic Strategies. Basic Catalytic Principles What is meant by the binding energy as it relates to enzyme substrate interactions? –free energy released.
Hypothetical substrate docking in enzyme’s active site. Substrate is geometrically and electronically compatible with active site. Enzymes are also.
Enzyme Mechanisms.
Biochemistry Lecture 8.
Chymotrypsin Chymotrypsin is one of the serine proteases.
Lecture 13: Mechanism of Chymotrypsin
N SINGLE CHAIN AMPHIPHILES   MICELLE 1.LIPID STRUCTURE: FORM COMPLEX STRUCTURES FROM SIMPLE MOLECULE 1.LIPID STRUCTURE A: INTERMOLECULAR AGGREGATES MICELLE.
Catalytic Mechanism of Chymotrypsin slide 1 Chymotrypsin –Protease: catalyze hydrolysis of proteins in small intestine –Specificity: Peptide bond on carboxyl.
Two Substrate Reactions
Probing Mechanisms of Peptide Bond Formation & Catalysis Using Models Model of Koga Uses molecular recognition by a crown ether to bind a model of the.
Enzyme Mechanisms: Serine Proteases
Chapter 3 PROTEIN FUNCTION. All proteins bind to other molecules Binding is selective.
Allosteric Enzymes Allosteric: Greek allo + steric, other shape Allosteric enzyme: an oligomer whose biological activity is affected by other substances.
Gene Expression and Regulation
Lecture 4 Web: pollev.com/ucibio Text: To: Type in:
Chymotrypsin Lecture Aims: to understand (1) the catalytic strategies used by enzymes and (2) the mechanism of chymotrypsin.
Identifying the Molecule of Inheritance
Catalytic Mechanisms.
Enzymes (If you don’t have the energy, we can help!)
Chapter 6.1 and 6.2: Introduction to Enzymes
Copyright © The McGraw-Hill Companies, Inc. Permission required for reproduction or display. Chapter 5 Lecture Slides.
Chapt. 8 Enzymes as catalysts
Gene Regulation, Part 1 Lecture 15 Fall Metabolic Control in Bacteria Regulate enzymes already present –Feedback Inhibition –Fast response Control.
Control of Gene Expression Year 13 Biology. Exceptions to the usual Protein Synthesis Some viruses contain RNA and no DNA. RNA is therefore replicated.
CHMI E.R. Gauthier, Ph.D. 1 CHMI 2227E Biochemistry I Enzymes: - catalysis.
Section 3 Lesson 2– The Catalytic Cycle. What do enzymes do? Enzymes lower the activation energy E a required for a reaction to occur.
CHMI E.R. Gauthier, Ph.D. 1 CHMI 2227E Biochemistry I Enzymes: - catalysis.
Prokaryotes vs Eukaryotes
Biocatalysts Introduction to Molecular Cell Biology Biocatalysts Dr. Fridoon Jawad Ahmad HEC Foreign Professor King Edward Medical University Visiting.
Enzymes.
1 Amino Acids, Proteins, and Enzymes Enzymes Enzyme Action Factors Affecting Enzyme Action Enzyme Inhibition.
Time to Connect……. Enzyme Activity is amount of enzyme that
Biology 102 Gene Regulation and Expression Part 2.
 “Ability to do work”  Chemical, positional (potential), kinetic (heat), etc. Energy.
GENE EXPRESSION and the LAC OPERON We have about genes inside our DNA that code for proteins. Clearly not all the proteins are needed at the same.
Enzyme Rate Enhancement
CHAPTER 6 Energy, Enzymes, and Metabolism. Energy and Energy Conversions Energy is the capacity to do work Potential energy is the energy of state or.
Enzymes: They do all the work! Enzymes  Proteins  Help chemical reactions happen  reduce activation energy  increase rate of reaction.
PROTEIN PHYSICS LECTURE 1. Globularproteins Fibrous proteins H-bonds (NH:::OC) & hydrophobic forces Membraneproteins.
The Behavior of Proteins: Enzymes, Mechanisms, and Control Feb 16, 2016 CHEM 281.
Higher Human Biology Unit 1 Human Cells KEY AREA 6: Metabolic Pathways.
Enzymes: A Molecular Perspective
Flow of energy through life
Enzymes: the proteins in our body that get the chemical reactions necessary of life done common enzyme found in nearly all living organisms which are exposed.
PROTEIN STRUCTURE AT ACTION: BIND  TRANSFORM  RELEASE
Enzymes-2 – Properties, classification and theories of action lecture NO : 1st MBBs Dr Muhammad Ramzan.
Serine Proteases A large group of enzymes that cleave amide bond
PROTEINS AS DRUG TARGETS:
Chapter 15 Enzymes.
Enzymes Biological Catalysts.
Human Cells Metabolic pathways
Enzyme Catalytic Mechanisms
Chemistry 501 Handout 6 Enzymes Chapter 6
The Nature of the Active Site
CHAPTER 6 Energy, Enzymes, and Metabolism
Introduction & overview
Transcription & Translation.
Serine proteases Named because they use a serine residue to cut peptide bonds Possess a catalytic triad His 57 Asp 102 Ser 195 Use 2 different types of.
Turning Genes On and Off
Serine proteases have a reactive serine
Enzymes Biological Catalysts.
Enzymes-2 – Properties, classification and theories of action lecture NO : 1st MBBs Dr Muhammad Ramzan.
Control of Prokaryotic (Bacterial) Genes Different from Eukaryotes!
Enzyme-Substrate Complex
GENE EXPRESSION / PROTEIN SYNTHESIS
Amino acids are coded by mRNA base sequences.
Enzymes.
Presentation transcript:

BIND  TRANSFORM  RELEASE PROTEIN PHYSICS LECTURE 24 PROTEINS AT ACTION: BIND  TRANSFORM  RELEASE

BIND: repressors - turn - 

Zn- fingers DNA & RNA BINDING Leu-zipper

BIND  TRANSFORM  BIND: Repressors -BINDING-INDUCED DEFORMATION MAKES REPRESSOR ACTIVE, and IT BINDS TO DNA

BIND: Immunoglobulins

Immunoglobulin

BIND  TRANSFORM  RELEASE: ENZYMES chymotrypsin Note small active site

Chymotrypsin catalyses hydrolysis of a peptide Spontaneous hydrolysis: very slow

chymotrypsin

CHAIN CUT-INDUCED DEFORMATION MAKES ENZYME ACTIVE non-active cat. site  active cat. site Chymotripsin Chymotripsinogen

SER-protease: catalysis

CHYMOTRYPSIN ACTIVE SITE with INHIBITOR

Preferential binding of TS: RIGID enzyme Catalytic antibodies ABZYM = AntyBody enZYM Transition state (TS) Preferential binding of TS: RIGID enzyme Antibodies are selected to TS-like molecule