B/B Flashcards
cellular Cl- transport
[Cl-] outside cell > [Cl-] inside cell
- to move against the gradient, it requires ATP
- ACTIVE TRANSPORT (ion channel)
The precursor of EGP is translated from a transcript that has had one nontemplated nucleotide added to the open reading frame. This change does not create or eliminate a stop codon. Compared with the protein sGP, which is produced from the unedited transcript, EGP most likely has the same primary:
A) amino-terminal sequence as sGP, but a different primary carboxy-terminal sequence.
- We always read amino acid sequences from N- terminal (amino) to C-Terminal (carboxy).
- C terminal is modified post-translationally not the N.
- A frameshift doesn’t always have to create or eliminate a
- The addition of one nucleotide to the open reading frame of EGP results in a frameshift mutation and an aberrant carboxy-terminal domain
- The frameshift will most likely affect areas after the mutation near the C-terminal but most likely did not affect the areas before the mutation near the N-terminal.
lysosomes
membrane-bound organelles that contain hydrolytic enzymes activated by a low pH. These enzymes are capable of degrading many kinds of biomolecules.
microtubules
cellular structures that originate from centrosomes
Variable region of an antibody
Regions 1 and 3 (“caps” on the chains”) correspond to the variable portion of the light and heavy chains, respectively, of an antibody.
- The variable region of an antibody will enable recognition of a particular antigen, such as HER2, which typically has elevated expression in breast cancer tumors.
Muscle contraction after death
during normal muscle contraction, ATP is required to break the bonds between the actin filament and the myosin head.
After death, no new ATP is generated, so the myosin head cannot be released from the actin filament, resulting in stiffening of muscles
phagocytosis
because when a macrophage ingests foreign material, the material initially becomes trapped in a phagosome. The phagosome then fuses with a lysosome to form a phagolysosome. Inside the phagolysosome, enzymes digest the foreign object.
Where are secretory proteins synthesized?
the rough endoplasmic reticulum
- fold into their tertiary structure there too
Ubiquitination
targets a protein for degradation by a proteasome
transmembrane domains
- cross the phospholipid bilayer
- As a result, these domains are most likely to have a high proportion of hydrophobic residues (non polar)
thiol group
R-S-H
bonds between protein subunits
- reducing agents separate subunits that are linked together by disulfide bonds, which implicate the thiol groups of cysteine residues.
How are posttranslational modification of proteins such as histone acetylation analyzed?
Western blotting (protein)
vasopressin
regulates the fusion of aquaporins with the apical membranes of the collecting duct epithelial cells
Schwann cells
myelin-forming cells in the peripheral nervous system
Osmotic pressure Π relation:
Π = iMRT
where i is the van’t Hoff factor, M is the concentration of solute, R is the gas constant, and T is the temperature.
prion
an abnormally folded protein that induces a normally folded version of the protein to also adopt the abnormal structure, which is often deleterious (infectious)
blood from the small intestine is transported first to the . . .
liver, which regulates nutrient distribution and removes toxins from the blood
endosomes
mediate internalization of viral particles through endocytosis
- endocytosis through the fusion of the viral membrane with the host cell membrane
ectoderm
nervous system, epidermis, dermis, hair, nails, eyes, and ears
mesoderm
muscle, cardiac and skeletal systems, blood, kidney, and spleen
endoderm
glands, lining of the digestive system and respiratory system, liver, pancreas, respiratory system
Motor proteins on microfilaments
move along through interaction with actin
cytotoxic T lymphocytes
target virus-infected cells by recognizing the viral antigen presented on the cell surface