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Chapter 3b/c Learning Objectives

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Section 1

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How can protein structure change?

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6 years ago

Date created

Mar 1, 2020

Cards (19)

Section 1

(19 cards)

How can protein structure change?

Front

-Temp (increase temp, breaks H-bonds) -pH -High concentrations of polar substances -nonpolar substances

Back

What mechanisms do enzymes use to affect a chemical rxn?

Front

-induces strain -mods substrate orientation -adds chemical groups -uses induced fit -uses cofactors

Back

Why would a cell use feedback inhibition?

Front

to prevent a overproduction of a certain substance

Back

4 levels of protein structure

Front

-Primary -Secondary -Tertiary -Quaternary

Back

quaternary structure

Front

-2 or more folded polypeptide chain

Back

How does temperature affect enzyme activity?

Front

-increasing temp, rxn occurs faster

Back

What is the role of an enzyme?

Front

-speed up/catalyze metabolic reactions

Back

How does pH affect enzyme activity?

Front

-adds or releases protons -changes enzyme shape to catalyze a rxn or make it inactive

Back

How are proteins denatured?

Front

-heat -chemicals -this is irreversible

Back

How is protein localization influenced when proteins proteins interact with other proteins or cell components?

Front

-moves protein to proper place to perform its function -may change after a signal/modification is received

Back

feedback inhibition

Front

the end product of a metabolic pathway shuts down the pathway

Back

Structure of amino acid

Front

central carbon, carboxyl group to the right (COOH), amine group to the left (NH2), hydrogen above and R group below

Back

tertiary structure

Front

-3d structure -determined by R-Groups -Can have both folds and a helix in its structure -Formed by covalent bonds or non covalent bonds

Back

competitive vs noncompetitive inhibitors

Front

-competitive: inhibitor binds to active site and blocks it off so substrate can't bind to it -non-competitive: binds to enzyme but not on the active site, and changes the shape of the active site so the substrate can't bind to it

Back

Major functions of proteins

Front

- Enzymes - Defensive proteins - Hormonal and regulatory proteins - Receptor proteins - Storage proteins - Structural proteins - Transport proteins - Genetic regulatory proteins

Back

How to distinguish amino acids?

Front

-Each amino acid has its own R-Group

Back

primary protein structure

Front

-sequence of a chain of amino acids

Back

secondary protein structure

Front

-regular and repeating structural patterns created by hydrogen bonding between backbone atoms in neighboring segments of protein chains -two types -alpha helix -beta sheet

Back

allosteric regulation

Front

-nonsubstrate molecule binds to enzyme other than the active site and mods it -changes shape of the enzyme

Back