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Test Bank for Beckers World of the Cell 8th Edition Chapter 3 10th Edition by Jeff Hardin
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Test Bank for Beckers World of the Cell8th Edition Chapter 3 10th Edition by
Jeff Hardin
Protein Functions - ANSEnzymes- Catalysts
Structural- support and shaper
Motility- contraction and movement of cells and intracellular needs
Transport-ovement of other substances into and out of and within cell
Hormonal- immediate communication between cells in distant parts of organism
Receptor-respond to chemical stimuli
Defensive-antibodies
Storage-reserviour of amino acids
Dehydration Synthesis - ANSThe process of stringing individual amino acids together into a
linear polymer.
As the three atoms of H2O are removed the carboxyl carbon of 1 amino acid and the amino
nitrogen of a second are linked directlyThe process of stringing individual amino acids together
into a linear polymer.
As the three atoms of H2O are removed the carboxyl carbon of 1 amino acid and the amino
nitrogen of a second are linked directly. driven by ATP
Peptide Bond - ANSCovalent C-N bond linking two amino acids
N-Terminus - ANSA Chain of amino acids has an intrinsic directionality because it always has an
amino group at one end and carboxyl group at the other end. The end with Amino group is
N-Terminus
C- Terminus - ANSEnd of amino acid chain that ends with carboxyl group
Polypeptide - ANSImmediate product of amino acid polymerization. Has unique, stable,
three-dimensional snap and is biological active. Some consist of single, and their shape is due
to the folding and coiling that occur spontaneously as the chain is formed. Both a polymer with
amino acids as its monomeric repeating units; on the other had it may sometimes be a
monomer unit that is part of multimeric protein
Monomeric Protein - ANSSingle polypeptide
Multimeric protein - ANSConsist of two or more polypeptides that are often called polypeptide
subunits.
, if composed to two it is referred to as a dimer
If composed of 3 timer
If composed of 4 tetramer
Hemoglobin - ANS/multimeric protein compose of four subunits two alpha and two Beta
changes. Each subunit contains a heme group with a iron atom that can bind a single O
molecule. iron attachment is known as a prosthetic group.
Conformation - ANSInitial folding depends on several different kinds of bonds and interactions,
including the covalent disulfide bond and non covalent interactions, including Hydrogen bonds,
ionic bonds, Van der Walls and hydrophobic interactions.
Amino Acid Residue - ANSInteractions for conformations, actions involve the carboxyl, amino
and R groups of amino acids.
Disulfide bond - ANSForms between the sulfur atoms of two cysteine amino acids residues.
these become covalently linked following oxidation reaction that removes 2 H from sulfhydryl
groups. Covalent bond
Intramolecular bonds - ANSstabilize the conformation, within one peptide
Intermolecular bonds - ANSbetween two peptide chains
insulin - ANSDimeric protein inter linked
Primary - ANSFormal designation. The order which appears from one end to the other. N to C
terminus. Important for genetic and structure.
secondary - ANSCommon. Describes local regions that results from hydrogen bonds between
NH and CO groups. forming alpha and beta sheets .
Tertiary structure - ANSFinal Folding. Comes about because of properties of R groups . Neither
respective or predictable., complex globular shape, due to interactions between R-groups, such
as hydrophobic interactions, van der Waals interactions, hydrogen bonds, and disulfide bridges
Quaternary Structure - ANSTwo or more interact, Highest level of organization occurring when
protein contains more than one polypeptide chain. Interactions creating a functional protein;
coded by genes and amino acids; three dimensional arrangement
alpha helix - ANS3.6 amino acids per turn. Repeating polymers. peptide bonds form on the
fourth amino acid. Every peptide is bonded CO group by hydrogen bonds to peptide bond
directly below it. NH directly above it. Intramolecular.
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