Functional Biology 1330 Ch.3

Amino acid side chains distinguish the different amino acids and can be grouped into 4 general types:

Acidic Basic Uncharged polar Nonpolar

Electrically charged side chains are _____________

Acidic/basic

Proteins are polymers of ___________

Amino Acids

All proteins are made from 20 ______________ building blocks

Amino acid

Which amino acids contain side chains that would be unable to to form hydrogen bonds with water?

Amino acids with nonpolar side chains

What 2 functional groups are bound to the central carbon of every free amino acid monomer?

An amino acid group and a carboxyl group

What 2 functional groups are bound to the central carbon of every free amino acid monomer?

An amino group and a carboxyl group

If the side chain has a positive charge it has taken on a proton and is ____________

Basic

Each amino acid chain has 2 sides: one amino acid and one ____________

Carboxyl

Which part of an amino acid is always acidic?

Carboxyl functional group

One function of protein is _____________ (increases the rate of reaction)

Catalysis

One function of protein is ________________ (e.g. keratin hair)

Cell structure

During protein synthesis, the peptide bond between amino acids is formed by the process of _____________

Condensation

Monomer polymerize through ____________ (dehydration) reactions that release a water molecule

Condensation

________________ bonds in tertiary structures form between sulfur-containing R-groups

Covalent disulfide

One function of protein is ______________ (e.g anitbodies in the immune system)

Defense

In tertiary structure ______________ bonds form between hydrogen atoms and the carbonyl group in the peptide-bonded backbone. As well as between hydrogen and negatively charged atoms in side chains

Hydrogen

Protein's secondary structure uses ____________ bonding

Hydrogen

The secondary structure of proteins results because of ___________ bonding between atoms in the protein's backbone

Hydrogen

The secondary structures of a protein results from _____________ bonds

Hydrogen

Which type of interaction stabilizes the α-helix and the β-pleated sheet structures of proteins?

Hydrogen bonds

What type of bond is directly involved in the formation of an aloha helix?

Hydrogen bonds between amino acid residues

_____________ is the reverse reaction of polymerization that breaks polymers apartm by adding a water molecule

Hydrolysis

Polar R-groups form hydrogen bonds and readily dissolve in water making them_______________

Hydrophillic

In tertiary structures __________________ interaction occur within a protein and increases stability of surrounding water molecules by increasing hydrogen bonding

Hydrophobic

Nonpolar R-groups do not form hydrogen bonds, coalesce in water, and lack charge or highly electronegative atoms capable of forming bonds with water. Therefore nonpolar R-groups are ________________ (hydrophillic/hydrophobic)

Hydrophobic

Suppose you discovered a new amino acid. Its R group contains only hydrogen and carbon atoms. Predict the behavior of amino acid ?

Hydrophobic

Defensive proteins are manufactured by the ___________ system

Immune

_______________ bonds form in tertiary structures between groups that have full and opposing charges

Ionic

Very large polymers made up of many monomers linked together

Macromolecules

What causes mad cow disease and other such spongiform encephalopathies?

Misfolden proteins known as prions

One function of protein is ___________________ (e.g. actin and myosin in muscles)

Movement

Nonpolar side chains are hydrophobic and ____________ in water (no charge)

Non soluble

If the side chain is not negative, positive, or uncharge with with an oxygen atom it is a _________________ amino acid

Nonpolar

Which monomers make up RNA?

Nucleotides

Which of the following does NOT contain a structural protein? a. Spider silk b. Tendons c. Ligaments d. Muscles e. Ovalbumin

Ovalbumin

Which of the following is not attached to the central carbon atom in an amino acid?

Oxygen

A bond that forms between carboxyl and amine group of two amino acids

Peptide

Tertiary structure is NOT directly dependent on _______________ bonds

Peptide

What type of bond joins the monomers in a protein's primary structure?

Peptide

____________ bonds link amino acids together by bonding the carboxyl group of one amino acid to the amino acid group of another

Peptide

A chain of amino acids linked by peptide bonds

Polypeptide

Protein's _____________ structure is its unique sequence of amino acids

Primary

_____________ structure is produced by the unique sequence of amino acids in a protein

Primary

______________ are improperly folded forms of normal proteins

Prions

Macromolecules consisting on amino acid monomers linked through chemical bonds

Protein

Oligopeptides are polypeptides containing fewer than 50 amino acids and polypeptides containing more than 50 amino acids are called ____________

Proteins

Which polymers are composed of amino acids?

Proteins

Many proteins contain several distinct polypeptide subunits that interact to form a single structure. The bonding of two or more distinct polypeptide subunits produces _________ structure.

Quaternary

Amino acids have a central carbon bonded to an amino group, a hydrogen atom, a carboxyl group, and an ______ group

R

How do amino acids differ?

R- side chain (determines properties)

The 20 amino acids differ only in the unique ____________ attached to the central carbon

R-group

No catalysis= no _________

Reaction

In water (pH 7), the amino and carboxyl groups ionize to NH3 and COO-respectively. This helps amino acids stay in a solution and makes them more _____________.

Reactive

Protein's ____________ structure is formed by ____________ bonds between the carbonyl group of one amino acid and the amino group of another

Secondary

The alph-helix is a component of ___________ protein structure

Secondary

Proteins function is dependent on its _________

Shape

Amino acids have a central carbon atom to the following: H, NH2, COOH, and variable side chain (R-group_ H- a hydrogen atom NH2- and amino functional group COOH- a carboxyl functional group A distinctive R-group (referred to as a ___________)

Side chain

One function of protein is _____________ (e.g insulin receptors)

Signaling

Polar side chains are hydrophillic and _____________ in water (partial charge)

Soluble

Protein folding is often __________

Spontaneous

Interactions between R-groups determine protein __________ structure

Tertiary

One function of protein is _____________ (e.g. Na+ K+ exchanges across membranes)

Transport

(True/False) Enzymes in the digestive tracts catalyze hydrolysis reactions

True

A bond forms between the carboxyl functional group of one amino acid and the amino acid functional group of the other amino acid (T/F)

True

A denatured (unfolded) protein is ____(able/unable) to function normally

Unable

If a side chain is uncharged and have an oxygen atom the highly electronegative oxygen will result in a polar covalent bond thus is _________________

Uncharged polar

If the side change has a negative charge it has lost a proton and is ____________

acidic

Proteins call molecular ________________ help proteins fold correctly in cells

chaperones

Hydrogen bonding between sections of the same backbone is possible only when a polypeptide bends in a way that puts C=O and N-H groups closely together, forming: alpha _____________ ___________ sheets

helix Pleated

Interactions between R-groups or between R-groups and the ___________________ give protein its tertiary structure

peptide-bonded backbone

What is an active site?

the location in an enzyme where substrates bond and attach

__________________ interaction in tertiary structures are weak electrical interactions between hydrophobic side chains

van der Waals