intro to bioengineering midterm review

what is biomedical engineering?
a. engineering applied to human health
b. biological/medical application of engineering principles or engineering equipment
c. application of science, mathematics, and engineering principles to improve human health
d. all of the above

d. all of the above

what are the bioengineering subdisciplines?
a. physiological modeling, biomechanics, biomedical imaging, medical machines
b. physiological modeling, biomechanics, biomedical instrumentation and sensors, biomedical imaging, biomolecular engineering and biotechnology, artificial organs, system biology, and bioinformatics
c. biomedical imaging, bioinformatics, biomolecular engineering, biotechnology, and biomechanics
d. none of the above

b. physiological modeling, biomechanics, biomedical instrumentation and sensors, biomedical imaging, biomolecular engineering and biotechnology, artificial organs, system biology and bioinformatics

what are two strong common bonds?
a. covalent and ionic
b. ionic and hydrogen
c. hydrogen and van der Waals forces
d. ionic and van der Waals forces

a. covalent and ionic

what are two common weaker bonds?
a. covalent and ionic
b. hydrogen and van der Waals
c. ionic and van der Waals
d. covalent and hydrogen

b. hydrogen and van der Waals

What type of covalent bond has an unequal distribution of electrons?
a. nonpolar
b. polar
c. neither

b. polar

what type of covalent bond has equal and symmetrical electrons?
a. nonpolar
b. polar
c. neither

a. nonpolar

what is an ionic bond?
a. an interaction involving a hydrogen atom located between a pair of other atoms having a high affinity for electrons
b. an interatomic linkage that results from the sharing of an electron pair between two atoms
c. type of linkage formed from the electrostatic attraction between oppositely charged ions in a chemical compound

c. type of linkage formed from the electrostatic attraction between oppositely charged ions in a chemical compound

what is a hydrogen bond?
a. type of linkage formed from the electrostatic attraction between oppositely charged ions in a chemical compound
b. an interaction involving a hydrogen atom located between a pair of other atoms having a high affinity for electrons
c. an interatomic linkage that results from the sharing of an electron pair between two atoms

b. an interaction involving a hydrogen atom located between a pair of other atoms having a high affinity for electrons

what is the difference between hydrophilic and hydrophobic?
a. hydrophilic; non-water soluble - hydrophobic; water-soluble
b. hydrophobic; non-water soluble - hydrophilic; water-soluble

b. hydrophobic; non-water soluble - hydrophilic; water-soluble

what does it mean if Gibbs Free Energy (G) is less than 0?

the reaction is spontaneous

what does it mean if Gibbs Free Energy (G) is greater than 0?

the reaction needs input of energy

How can you explain what Enthalphy (H) is?

it is the internal energy of a compound

How can you explain an Enthalpy change?

Overall energy change of the reaction ; negative value = heat released
positive value = heat required

What are some of the macromolecules?

polysaccharides, proteins, nucleic acids and lipids

How can you explain diffusion?

diffusion is the movement of particles from a high to a low concentration

what is the difference between active transport and diffusion?

active transport is from a low to high concentration where diffusion is a high to low concentration

Gene

a gene is a sequence of DNA or RNA which codes for a molecule that has a function

what is gene locus (loci)?

it is the physical location of a gene on a particular chromosome

How does polygenic inheritance work?

most characteristics are influenced by several genes

How does pleiotropy work?

each gene can influence a variety of traits

How does epigenetics work?

heritable phenotype changes that do not involve alterations in the DNA sequence

Characteristics of protein

structural support, communication, catalyze chemical reactions, neutralize foreign pathogens

the primary structure of a protein

the amino acid sequence of the polypeptide chain

the secondary structure of protein

protein structure is formed by folding and twisting of amino acid chain