Chapter 5 Part II Flashcards
Enzymes
- a catalyst
- accelerates/ speeds up chemical reactions without themselves being consumed
- can be proteins
- “molecular motors” that perform cellular work
1) highly specific
2) accelerate chemical reactions
3) are not consumed in the reactions they catalyze
Protein Structure
structurally complex molecules known, exhibit a specific 3-D structure or conformation, and may consist of one or more polypeptides
Polypeptides
polymers that are constructed from the 20 aa monomers
Amino Acids
organic molecules possessing both carboxyl and amino groups
- differ in their properties due to differing side chains, called “R” groups or functional groups
- building blocks of proteins (monomer)
- about 20 essential aa
4 types of macromolecules
1) Sugar/ Carbohydrates
2) Lipid/ Fats
3) Protein
4) Nucleic Acid
proteins
most diverse (macro)molecule on the face of the planet
dehydration (hydrolysis)
removes a hydroxyl group from the carboxyl end of one aa and a hydrogen from another aa
Peptide bond
-link aa together from a dehydration reaction (O=C-NH)
Protein conformation
- 3D shape or conformation determines how it functions
- i.e. lysozyme: a “clamp” shaped protein that cuts proteins
Four levels of protein structures
- hierarchical
1) Primary Structure
2) Secondary
3) Tertiary
4) Quaternary
What ultimately determine the protein structure?
sequence and type of aa of a polypeptide
Primary Structure
unique sequence of aa in a polypeptide that is determined by the genetic sequence
Secondary Structure
the (local) folding or coiling of the polypeptide into a repeating configuration and is stabilized by intramolecular hydrogen bonding
-extremely versatile and strong
2 types of secondary structures
1) Alpha helix
2) beta pleated sheet
Alpha Helix
- single helical structure
- stabilized by hydrogen bonding between aa in the protein itself
Beta Pleated Sheet
- stabilized through hydrogen bonding
- backbone of the polypeptide
- get layers of protein, like a fabric or mess
- hydrogen bonding in (side to side?) direction (very strong)
i.e. collagen, spider webs
Tertiary Structure
- overall three-dimensional (3D) shape of a polypeptide (probably in an aqueous solution)
- Results from interactions between amino acids R groups, hydrogen bonding, and hydrophobic interactions (associations)
- help 3D (globular) protein/bonding; bonding between and among the aa
Quaternary Structure
- the overall structure that results from the aggregation of two or more polypeptide subunits
- protein formed from 2 distinct polypeptides
- not all proteins have this structure
- i.e. collagen: 3 distinct polypeptides (3 a helix fibers; found in tissues, bone, cartilage, muscle)
- i.e. hemoglobin: 4 distinct polypeptides; major O transport protein
Overview: 4 levels of protein structure
a polypeptide chain of a given aa sequence can spontaneously arrange itself into a 3D shape by the interactions responsible for secondary and tertiary structure
Protein folding may also be determined by the…
protein’s environment
i.e. pH, temperature, the solution
What determines protein conformation (shape)
depends on the physical and chemical conditions of the protein’s environment
Denaturation
when a protein unravels and loses its native conformation
Most proteins probably go through…
several intermediate states on their way to a stable confirmation
Chaperonins
protein molecules that bind unfolded proteins and assist in their proper folding
-has a cap and a hollow cylinder