• Shuffle
    Toggle On
    Toggle Off
  • Alphabetize
    Toggle On
    Toggle Off
  • Front First
    Toggle On
    Toggle Off
  • Both Sides
    Toggle On
    Toggle Off
  • Read
    Toggle On
    Toggle Off
Reading...
Front

Card Range To Study

through

image

Play button

image

Play button

image

Progress

1/96

Click to flip

Use LEFT and RIGHT arrow keys to navigate between flashcards;

Use UP and DOWN arrow keys to flip the card;

H to show hint;

A reads text to speech;

96 Cards in this Set

  • Front
  • Back

What is the range of the number of amino acids a polypeptide can contain?

50 to 2000

What is the mean molecular weight of an amino acid?

110 gm/mol

What mass unit is used for amino acids?

Dalton (Da)

1 dalton = how many gm/mol?

1

What is the protein structural hierarchy?

Primary, secondary, tertiary, quaternary

The ___ (primary/secondary/tertiary/quaternary) structure is the ordered sequence of amino acids in that protein

Primary

A ___ (hydrogen/peptide) bond arises from the carboxyl group of one amino acid and the amino group of another

Peptide

Water is liberated in the formation of peptide bonds in a process called what? Hint: 2 names

Condensation reaction or dehydration process

Is there rotation around peptide bonds?

No

Peptide bonds are ___ (rigid/flexible) and have partial ___ (single/double/triple) bond characteristics

Rigid, double

Why do peptide bonds have partial double bond characteristics?

They have resonance

Peptide bonds are ___ (shorter/longer) than a single bond, but ___ (shorter/longer) than a double bond

Shorter than a single bond, longer than a double bond

How many atoms lie within the same plane in a peptide bond?

6

What are the 6 atoms that lie within the same plane in a peptide bond?

Alpha carbons, carbonyl carbon, oxygen, amide nitrogen, amide hydrogen

Cis and trans configurations in a peptide bond refer to the positions of what carbons?

Alpha carbons

What configuration, cis or trans, is favored in peptide bonds?

Trans

The trans position is favored in peptide bonds because there is ___ (more/less) steric interference between ___ (alpha carbons/R groups)

Less, R groups

What amino acid is an exception to the trans favorability rule and both the trans and cis configuration is seen?

Proline

In the case of proline, cis configurations are seen as relatively ___ (more/equal/less) than trans configurations in terms of steric clash

Equal

The amino acid that is ___ (N/C)-terminal to the proline can be cis or trans configuration

N-terminal

Peptide bonds are rigid and ___ (triangular/planar)

Planar

What must be able to occur for proteins to be able to fold into their 3D shapes?

Rotation

Rotation occurs between the alpha amino nitrogen and the ___ (alpha carbon/alpha carbonyl carbon)

Alpha carbon

Rotation occurs between the alpha carbonyl carbon and the ___ (alpha carbon/alpha carbonyl carbon)

Alpha carbon

Bond angles made between the alpha amino nitrogen and the alpha carbon are called ___ (psy/phi) angles

Phi

Bond angles made between the alpha carbonyl carbon and the alpha carbon are called ___ (psy/phi) angles

Psy

What are the two major secondary structural elements of proteins?

Alpha helices and beta sheets

For an alpha helix, the path is ___ (compact/loose) and winds around a central ___ (peptide bond/axis) of rotation

Compact, axis

Alpha helices are stabilized by ___ (hydrogen/peptide) bonds that are ___ (parallel/perpendicular) to the central axis of rotation

Hydrogen, parallel

Alpha helix hydrogen bonds arise between what 2 groups in the peptide backbone?

Amino groups and carboxyl groups

Alpha helix hydrogen bonds arise between amino acids that are how many residues apart in the peptide chain?

3-4

How many amino acids are there per 360 degree turn in an alpha helix?

3.6

R groups of an alpha helix point ___ (toward/away) from the central axis of rotation, ___ (outward/inward) from the helix

Away, outward

What is the center of an alpha helix filled with?

Atoms of the peptide backbone

___ (Right/Left)-handed alpha helices are the most common type of helices

Right

What amino acid is an alpha helix breaker?

Proline

A series of ___ (charged/uncharged) amino acids is an alpha helix breaker

Charged

Amino acids with ___ (small/large) side chains are helix breakers

Large

Amino acids that branch at the ___ (alpha/beta) carbon are helix breakers

Beta

What are beta sheets made up of?

Individual beta strands

Beta strands have a directionality that ___ (corresponds to/is opposite to) the direction of the peptide backbone

Corresponds to

Beta strands run from the ___ (amino/carboxyl) group to the ___ (amino/carboxyl) group

Amino group to the carboxyl group

Beta strands run ___ (C/N) to ___ (C/N)

N to C

In beta sheets, adjacent R groups are on the ___ (same/opposite) side of the backbone, and are ___ (above/inward) and ___ (below/outward) strands

Opposite, above, below

In beta sheets, the hydrogen bonds extend between the beta strands from the carbonyl ___ (hydrogen/oxygen) of one strand to the amino ___ (hydrogen/oxygen) of another strand

Carbonyl oxygen, amino hydrogen

Beta sheets are stabilized by ___ (hydrogen/peptide) bonds that are ___ (parallel/perpendicular) to the direction in which the peptide backbone is going

Hydrogen, perpendicular

___ (Parallel/Antiparallel) beta strands have stronger hydrogen bonding between the beta strands

Antiparallel

Antiparallel beta strands have stronger hydrogen bonding between the beta strands because there is greater ___ (circularity/linearity) in these bonds than in parallel strands

Linearity

What is the more stable configuration of beta strands: parallel or antiparallel?

Antiparallel

What type of repetitive secondary structure is located in a place where the peptide backbone is making a sharp turn?

Beta turn

Beta turns allow for compact conformation of what type of proteins?

Globular

Where on a protein are beta turns usually located?

Protein surface

What amino acid is often found in beta turns?

Glycine

What is the start of a beta turn referred to as?

i

What is the end of a beta turn referred to as?

i+3

In beta turns, i corresponds to what terminus?

N

In beta turns, i+3 corresponds to what terminus?

C

In an alpha helix, each right-handed turn is how many amino acids?

3.6

In alpha helices, each main chain N-H (amino group) is hydrogen bonded to the ___ (alpha carbon/oxygen) (carbonyl group) 3-4 amino acids away

Oxygen

On a ramachandran diagram, what quadrant are beta sheets located in?

Upper left

On a ramachandran diagram, what quadrant are alpha helices located in?

Lower left

On a ramachandran diagram, what quadrant are right-handed alpha helices located in?

Lower left

On a ramachandran diagram, what quadrant are left-handed alpha helices located in?

Upper right

On a ramachandran diagram, ___ (light/dark) green represents psy and phi angles that are seen most often

Dark

What are 2 types of non-repetative structures?

Loops and coils

Loops and coils are ___ (more/less) ordered than alpha helices and beta sheets, and ___ (are/are not) random

Less ordered, not random

What is another name for super-secondary structures?

Motifs

Motifs are in between what 2 structures?

Secondary and tertiary

What 3 characteristics do motifs have?

Sequential, recurrent, similar functions

Angiostatin, topoisomerase, and myoglobin are all examples of ___ (primary/secondary/tertiary) structures

Tertiary

The ___ (primary/secondary/tertiary) structure is the overall 3D structure that the peptide chain adopts

Tertiary

What is the name of the unit of organization that makes up the tertiary structure?

Protein domain

True or false: Protein domains are functional units within the protein

True

Motifs are ___ (smaller/bigger) than protein domains

Smaller

What effect is the largest driving force in tertiary and quaternary protein folding?

Hydrophobic effect

With proteins in aqueous solution, hydrophilic amino acid side chains will seek to be ___ (buried within the protein/facing the solution)

Facing the solution

With proteins in aqueous solution, hydrophobic amino acid side chains will seek to be ___ (buried within the protein/facing the solution)

Buried within the protein

With proteins in lipid environment, hydrophobic amino acid side chains will seek to be ___ (buried within the protein/facing out)

Facing out

With proteins in lipid environment, hydrophilic amino acid side chains will seek to be ___ (buried within the protein/facing out)

Buried within the protein

What property of secondary structural elements promotes formation of higher order structures?

Amphipathic property

What effect of water drives the formation of higher order structures?

Entropic

When proteins fold, there is a ___ (increase/decrease) in entropy

Decrease

The amino acids found in a peptide chain in unfolded protein have ___ (more/less) of a chance for randomness in their position than they would in a folded protein

More

As proteins fold and entropy decreases, what also decreases in order to counteract this?

Enthalpy

What are 4 interactions that must be formed to help stabilize proteins?

Hydrogen bonds, hydrophobic interactions, disulfide bonds, and ionic interactions

Disulfide bonds are ___ (covalent/noncovalent) linkages between two S-H groups of two ___ (prolines/cysteines) in ___ (reducing/nonreducing) environments

Covalent, cysteines, non-reducing

What are 2 examples of non-reducing environments that disulfide bonds can form in?

Endoplasmic reticulum, extracellular space

Ionic interactions can form between two ___ (charged/uncharged) R groups and in ___ (acidic/basic) conditions

Charged, acidic

Ionic interactions between R groups and termini are also called what?

Salt bridges

___ (Primary/Secondary/Tertiary/Quaternary) structure is only found in those proteins that are made up of more than one peptide chain

Quaternary

In quaternary structures, each peptide chain folds into what?

A monomer

Quaternary structure is made up of two or more ___ (monomers/dimers/trimers) that come together to make up the whole protein

Monomers

What are the subunits of quaternary structure?

Monomers

True or false: Monomers may be identical or different

True

Subunits (monomers) of quaternary structure add to what 2 characteristics of a protein?

Stability and function

What 3 options may subunits (monomers) have in terms of effect on the activity of other subunits?

May activate, inhibit, or have no effect