7.1 bio Flashcards
four levels of protein structure
Primary- Order of amino acids in chain
Secondary- regular sections of folding can be seen in all peptides
tertiary- Final 3 shape of a single polypeptide
Quandary- more than one polypeptide chain bonded together.
Identify polar, nonpolar, basic, acidic side chains
Polar- all have a polar functional side group (Hydroxyl, )
Nonpolar/ hydrophobic- None of the chains are the same
acidic- have acidic side functional groups
basic- have basic functional side groups.
protein denaturation
conditions that disrupt hydrogen and ionic bonds
Tertiary- interactions
hydrophobic- clumps towards the middle
Acidic and basic- opposites attract
Cysteines- Strong covalent bond (in the middle)
Hydrophillic- Form hydrogen bonds (on the outside)
Enyzmes cut and join the molecules of life, digestive enzymes break food into small nutrient molecules.
fatty acid synthesis- makes fatty acids
Tryptophan synthase- makes amino acid tryptophan
RuBisCo- Makes sugar molecules
Pepsin- breaks proteins
Amylase- Breaks down starch
Hormones
Carry molecular messages through blood
Infrastructure
Support and move cells
Protein/Filamenet
Collagen- Forms molecular cables that strengthen tendon and resilient sheets that support the skin and internal organs
Microtubule- Provide support and provide tracks for motion of kinesin and dytein
Actin- Forms filaments that are important for cell structure and mobility
Myosin- Molecular motor that powers muscle contraction
Channels,pumps, and receptors
Getting back and forth the membrane
transport structures and their function
Calcium pump- Transport calcium ions across the cell membranes
Potassium Channel- Allow potassium ions to pass through the membrane
Acetycholine receptor- Binds to the neurotransmitter Acetycholine and opens as a channel
Epidermal growth factor recpetor- shows the portion outside and inside of the cell and the part that crosses the membrane
Antibodies
Constant battle in the bloodstream
Characteristics of antibodies
Several flexible arms with binding sites at the end of each one-
Since antibodies don’t know in advance what attackers they could fight, it keeps their options open
The binding site is composed of several loops in the protein chain that have very different lengths and amino acid composition- Form the many types of pockets in different antibodies, each of which bind specifically to a different target
Antibodies are very flexible- Allowing the two fab arms to find neighboring sites on a target such as the surface of a virus.
Why and how would the structure and function of a protein change if a hydrophobic amino acid was substituted for a hydrophilic one?
There would be a change in the proteins folding pattern, and it would start forming hydrogen bonds instead of clump towards the middle.
How are the effects and results of protein denaturation different from the effect and results of a mutation?
Denaturation is the condition the protein is in and how it can effect a protein, where mutation can lead the protein to folding and functions in a not correct way.
what type of amino acid side chains tend to clump to the interior of a protein
Nonpolar
sequence of amino acids
Primary
