Biology Exam 1 Lecture 3 Flashcards
_____ is an excellent “example” protein
Hemoglobin
hemoglobin is a ____ in which each subunit binds a ___ group which then binds an _____
heterotetramer, heme, oxygen
Proteins fold into conformations that represent ___
energy minima
Unfolded proteins are said to be ____
denatured
____ in the cell help proteins fold into their correct conformations
Molecular chaperones
What are the 4 levels of structural organization in proteins?
Primary- linear amino acid sequence
Secondary- folding patterns
Tertiary- 3D organization of secondary structures, Protein domains
Quaternary- organization of protein complexes
A protein’s structure will be determined by its ____.
primary sequence.
Relevant parts of the protein will be the ____ and the side chains or ___ of each specific amino acid.
polypeptide backbone, R-groups
Which of the four types of amino acids is represented by the most members?
Non-polar
Proteins can fold into many possible ____,
however energetics drives them to ___ ____ _____
for each protein. Folding starts _____
conformations, one stable one, co-translationally
_____ bonds serve to generate structure
in proteins. These can occur between R groups or parts of the polypeptide backbone
Weaker, non-covalent
In cells different _____
help to fold and refold proteins
chaperones
_____ interactions will often help to drive interactions placing non-polar groups
near the ____ of the protein’s structure.
water, center
Modifications like N- and
O-linked ____ can
influence structure
glycosylation
In the cytosol, which sequence of amino acid side chains would most likely be found in the interior structure of a globular protein?
uncharged polar – hydrophobic – basic
basic – basic – hydrophobic
nonpolar – nonpolar – nonpolar
acidic – acidic – uncharged polar
They are all equally likely to be on the protein’s outside
nonpolar – nonpolar – nonpolar
____in proteins are part of _____
They are often arrangements of linked regions of alpha helices and beta sheets.
Domains, tertiary structure
______ between domains can
provide a variety of functions
Unstructured regions
what is the favored conformation when all of the R groups locally
are hydrophobic?
alpha helices
A protein’s primary structure is dependent upon _____ bonds that _____.
peptide; link adjacent amino acids
Z-Mapp is a drug treatment used for Ebola – what is it?
A “cocktail” of inhibitory antibodies
____ can form _____ ____ ______, which can
help stabilize protein structures in harsh environments.
Cysteines, covalent disulfide bridges
Antibodies contain many intra- and inter-polypeptide _____ that help maintain their conformations
disulfide bridges
Two other extracellular proteins containing many disulfide
bridges
collagen and elastin
Non-protein components of proteins -
retinal (rhodopsin), heme (hemoglobin)
A common theme in cells is ___ ____of subunits
into a ____ - this is particularly true with regard to
cytoskeletal proteins
dynamic assembly, filament
Weaker, non-covalent bonds also are key to specific _____ binding of proteins. This occurs through the formation
of _____.
ligand, binding sites
Specific membrane compartments such as lysosomes and peroxisomes can be isolated from cell lysates by differential centrifugation? T or F
True