PCB3134 Final Exam (Chapters 1, 3, 4, 6, 7, 8, 9, 10, 12 ) –
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INBDE Orthodontics NBDE II Review - Prosthodontics Perio Study
201 terms 69 terms Teacher 78 terms
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Practice questions for this set
Learn 1/6 Study with Learn
3 Na+ out per 2 K+ in
-uses 1 ATP
Choose an answer
1 Light microscopy (brightfield) 2 Enzymes
3 Cytology 4 Na+/K+ ATPase
Don't know?
Terms in this set (158)
Most common; white light transmitted through specimens. Often
Light microscopy (brightfield)
requires stains.
an electron microscope in which a beam of electrons is
Transmission electron
transmitted through a specimen and focused to produce an
microscopy (TEM)
image.
Scanning electron microscopy Electrons scan the specimen surface, which reveals external
(SEM) features in 3D
Freeze fracture microscopy cells are frozen and a knife is used to crack them open
focuses mainly on cellular structure and emphasizes optical
Cytology
techniques
Biochemistry focuses on cellular structure and function
focuses on information flow and heredity and includes
Genetics
sequencing of the entire genome in numerous organisms
uses centrifugation to separate/isolate different structures and
Subcellular fractionation
macromolecules
, are capable of very high speeds (over 100,000 revolutions per
Ultracentrifuges
minute)
techniques to separate molecules from a solution based on size,
Chromatography
charge, or chemical affinity
uses an electrical field to move proteins, DNA or RNA molecules
Electrophoresis
through a medium based on size/charge
is used to determine the size and composition of individual
Mass Spectrometry
proteins
Enzymes serve as catalysts, increasing the rates of chemical reactions
structural proteins physical support and shape
motility proteins contraction and movement
regulatory proteins control and coordinate cell function
transport proteins move substances into and out of cells
signaling proteins communication between cells
receptor proteins enable cells to respond to chemical stimuli from the environment
defensive proteins protection against disease
storage proteins storage of amino acids
Amino acids are linked together dehydration
stepwise into a linear polymer
by _________ reactions
N- (amino) terminus the end of a polypeptide chain that carries a free a-amino group
The end of a polypeptide chain that carries a free carboxyl
C- (carboxyl) terminus
group (-COOH).
Covalent disulfide bonds form sulfur, cysteine
between the _____ atoms of two
_________ residues
Disulfide bons form through oxidation, reduction
_________ and can be broken
through __________
form in water and between amino acids in a polypeptide chain
hydrogen bonds
via their R groups
ionic bonds form between positively and negatively charged R groups
Weak attractions between molecules or parts of molecules that
Van Der Waals interactions
result from transient local partial charges.
a type of weak chemical interaction caused when molecules that
Hydrophobic interactions
do not mix with water coalesce to exclude water
Primary structure Sequence of amino acids in a protein.
describes local regions of structure that result from hydrogen
Secondary structure bonding between N H and C O groups along the polypeptide
backbone (alpha helix and beta sheets)
B sheet characterized by a maximum of hydrogen bonding
the overall, three-dimensional shape of a polypeptide due to
tertiary structure interactions of the R groups of the amino acids making up the
chain.
The particular shape of a complex, aggregate protein, defined
quaternary structure by the characteristic three-dimensional arrangement of its
constituent subunits, each a polypeptide.
units of secondary structure consist of short stretches of alpha
Motifs
helices and beta sheets
Native conformation the most stable possible 3D structure of a particular polypeptide
Questions With Correct Solutions
Save
Students also studied
INBDE Orthodontics NBDE II Review - Prosthodontics Perio Study
201 terms 69 terms Teacher 78 terms
dong_lee82 Preview melissa_jarvis7 Preview Hunter_Charters
Practice questions for this set
Learn 1/6 Study with Learn
3 Na+ out per 2 K+ in
-uses 1 ATP
Choose an answer
1 Light microscopy (brightfield) 2 Enzymes
3 Cytology 4 Na+/K+ ATPase
Don't know?
Terms in this set (158)
Most common; white light transmitted through specimens. Often
Light microscopy (brightfield)
requires stains.
an electron microscope in which a beam of electrons is
Transmission electron
transmitted through a specimen and focused to produce an
microscopy (TEM)
image.
Scanning electron microscopy Electrons scan the specimen surface, which reveals external
(SEM) features in 3D
Freeze fracture microscopy cells are frozen and a knife is used to crack them open
focuses mainly on cellular structure and emphasizes optical
Cytology
techniques
Biochemistry focuses on cellular structure and function
focuses on information flow and heredity and includes
Genetics
sequencing of the entire genome in numerous organisms
uses centrifugation to separate/isolate different structures and
Subcellular fractionation
macromolecules
, are capable of very high speeds (over 100,000 revolutions per
Ultracentrifuges
minute)
techniques to separate molecules from a solution based on size,
Chromatography
charge, or chemical affinity
uses an electrical field to move proteins, DNA or RNA molecules
Electrophoresis
through a medium based on size/charge
is used to determine the size and composition of individual
Mass Spectrometry
proteins
Enzymes serve as catalysts, increasing the rates of chemical reactions
structural proteins physical support and shape
motility proteins contraction and movement
regulatory proteins control and coordinate cell function
transport proteins move substances into and out of cells
signaling proteins communication between cells
receptor proteins enable cells to respond to chemical stimuli from the environment
defensive proteins protection against disease
storage proteins storage of amino acids
Amino acids are linked together dehydration
stepwise into a linear polymer
by _________ reactions
N- (amino) terminus the end of a polypeptide chain that carries a free a-amino group
The end of a polypeptide chain that carries a free carboxyl
C- (carboxyl) terminus
group (-COOH).
Covalent disulfide bonds form sulfur, cysteine
between the _____ atoms of two
_________ residues
Disulfide bons form through oxidation, reduction
_________ and can be broken
through __________
form in water and between amino acids in a polypeptide chain
hydrogen bonds
via their R groups
ionic bonds form between positively and negatively charged R groups
Weak attractions between molecules or parts of molecules that
Van Der Waals interactions
result from transient local partial charges.
a type of weak chemical interaction caused when molecules that
Hydrophobic interactions
do not mix with water coalesce to exclude water
Primary structure Sequence of amino acids in a protein.
describes local regions of structure that result from hydrogen
Secondary structure bonding between N H and C O groups along the polypeptide
backbone (alpha helix and beta sheets)
B sheet characterized by a maximum of hydrogen bonding
the overall, three-dimensional shape of a polypeptide due to
tertiary structure interactions of the R groups of the amino acids making up the
chain.
The particular shape of a complex, aggregate protein, defined
quaternary structure by the characteristic three-dimensional arrangement of its
constituent subunits, each a polypeptide.
units of secondary structure consist of short stretches of alpha
Motifs
helices and beta sheets
Native conformation the most stable possible 3D structure of a particular polypeptide
