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28 Cards in this Set

  • Front
  • Back

structural proteins compose what structures?

cytoskeleton, anchoring proteins, much of extracellular matrix

most common structural proteins (5)

collagen, elastin, keratin, actin, tubulin

common motor proteins

myosin, kinesin, dynein

binding protein purpose

bind specific substrate, either to sequester it in the body or hold its concentration at steady state

cell adhesion molecules (CAMs) purpose

allow cells to bind to other cells or surfaces


CAM, calcium-dependent glycoproteins that hold similar cells together


CAM, two membrane-spanning chains, permit cells to adhere to proteins in the extracellular matrix. some have signaling capabilities


CAM, allows cells to adhere to carbohydrates on the surfaces of other cells, most commonly used in the immune system


used by immune system to target a specific antigen

what region of an antibody is responsible for antigen binding, and what other regions are there?

variable region (other region is constant)

structure of an antibody

two identical heavy chains and two identical light chains form a single antibody

held together by disulfide linkages and noncovalent interactions

ion channels

used for regulating ion flow into or out of a cell

ungated ion channels

always open

voltage-gated ion channels

open within a range of membrane potentials

ligand-gated ion channels

open in the presence of specific binding substance, usually hormone or neurotransmitter

enzyme-linked receptors

participate in cell signaling through extracellular ligand binding and initiation of second messenger cascades

G protein-coupled receptors

have membrane-bound protein associated with a trimeric G protein. initiate second messenger systems

pathway of G protein-coupled receptor activation

ligand binding engages G protein

GDP is replaced with GTP

alpha subunit dissociates from the beta and gamma subunits

activated alpha subunit alters activity of adenylate cyclase or phospholipase C

GTP is dephosphorylated by GDP

alpha subunit rebinds to beta and gamma


uses gel matrix to observe migration of proteins in response to an electric field

Native PAGE

electrophoresis style, maintains protein's shape, but results are difficult to compare because the mass-to-charge ratio differs for each protein


electrophoresis style, denatures the proteins and masks the native charge so that comparison of size is more accurate, but the functional protein cannot be recaptured from the gel

isoelectric focusing

electrophoresis style, separates proteins by their isoelectric point (pI). protein migrates toward an electrode until it reaches a region of the gel where pH=pI of protein


separates protein mixtures on the basis of their affinity for a stationary phase or a mobile phase

column chromatography

uses beads of a polar compound, like silica or alumina (stationary phase), with a nonpolar solvent (mobile phase)

ion-exchange chromatography

uses a charged column and a variably saline eluent

size-exclusiong chromatography

relies on porous beads (larger molecules elute first because they are not trapped in the pores)

affinity chromatography

uses a bound receptor or ligand and an eluent with free ligand or a receptor for the protein of interest

Edman degradation

used for amino acid sequencing