Bootcamp.com - Fundamentals of Biology (answered_ updated 2022)
any substance that takes up space and has mass is called _____
what is matter is
... [Show More] composed of?
an ______ is a substance that has specific chemical and physical properties
an _____ is the smallest unit of matter that still retains all the chemical properties of an element
can an atom break-down into something smaller, while still retaining the properties of the original element?
molecules result whenever _____ atoms join together
what atoms does carbon tend to bond with in an organic molecule?
_____ are molecules that contain more than one element
what are the strong attractive forces that hold atoms within a molecule?
which type of force exists between molecules?
which type of force is weaker... intra- or intermolecular?
which type of force (intra-/intermolecular) determines physical properties?
_____ are molecules that have the potential of bonding to other identical molecules through chemical reactions
_____ is the process when monomers bond together, and it forms _____
_____ are substances that have a large # of monomers bonded together
what are the 3 varieties of carbohydrates?
monosaccharides have a ratio of precisely _____ _____ per water molecule, and they have the empirical formula _____
5 carbon monosaccharides are called _____
6 carbon monosaccharides are called _____
a sugar molecule is classified as an alpha sugar if the hydroxyl (OH) group points _____ on the first carbon
a sugar molecule is classified as a beta sugar if the hydroxyl (OH) group points _____ on the first carbon
ribose is a _____ sugar (monosaccharide)
glucose and fructose are _____ sugars (monosaccharides)
glucose and fructose are _____ of each other
what type of carbohydrate results when 2 monosaccharide monomers bond/join together?
monosaccharide monomers join together via what type of reaction?
what functional group and atom combine in a dehydration/condensation reaction?
what type of bond is formed and what is released in a dehydration/condensation reaction?
what is the opposite of a condensation/dehydration reaction - why?
what is the name of the bond that forms when a carbohydrate attaches to another molecule?
carbohydrates linked to lipids are known as _____
carbohydrates linked to proteins are known as _____
which disaccharide contains 1 glucose and 1 fructose?
which disaccharide contains 1 galactose and 1 glucose?
which disaccharide contains 2 glucoses linked together?
polysaccharides are long polymers of _____
_____ may or may not have branching
some polysaccharides are for _____, and others are for _____.
_____ is a crucial storage polysaccharide in plants
starch contains many _____ monomers in linear forms as well as branched forms
linear plant starch is called _____
what type of glycosidic bonds are in amylose?
what is amylopectin?
what type of glycosidic bonds are in amylopectin?
_____ is a storage polysaccharide found in humans
glycogen contains many _____ monomers
is amylopectin or glycogen more branched?
what type of bonds does glycogen have?
glycogen is primarily stored in what type of human cells?
name two alpha-glucose polysaccharides
_____ is a structural polysaccharide found in plant cell walls, wood, and paper -
cellulose is a _____ polymer
what type of bonds does cellulose contain - what do they do?
what type of intermolecular force holds adjacent cellulose strands together in parallel?
cellulose has high ____ due to its structure
can humans digest cellulose?
chitin is a _____ polysaccharide
chitin is found in the cell walls of _____ and in the exoskeletons of ____
chitin is a structural polysaccharide of _____ monomers
what type of bonds are in chitin?
chitin looks a lot like _____
name two beta-glucose polysaccharides
proteins contain polymers called _____, and each of these polymers contain monomeric subunits called ______.
in an amino acid, what 4 things is the central (alpha) carbon bonded to? -
how many amino acids are there?
amino acids in a polypeptide are linked together via a covalent bond called a ______ bond
how do amino acids form peptide bonds with one another? -
which type of reactions separate the amino acids of a polypeptide? -
a peptide bond is an _____ bond. These bonds occur between _____ and _____ functional groups
what enzymes catalyze peptide bond formation?
peptidyl transferases are _____ transferases
polypeptides have an _____ terminus and a _____ terminus
the _____ structure of a protein is its amino acid sequence - primary
all proteins have _____ structure
the _____ structure of a protein are folds that occur in a polypeptide chain due to intermolecular forces between atoms of the polypeptide backbone -
the _____ is the amino acid structural features other than the R-group -
does the secondary structure include interactions between R-group atoms?
which level of protein structure includes alpha helices and beta-pleated sheets?
what is the most common type of intermolecular force for secondary structure and where do they occur between?
the _____ structure is the 3D structure of larger polypeptide chains due to (usually) non-covalent interactions between amino acid R-groups
what are the common interactions between R-groups in tertiary structure? -
usually tertiary structures involve non-covalent interactions; however, ______ bonds are the "covalent exception"
which amino acids allows disulfide bond formation?
the _____ structure refers to large proteins that have multiple subunits (i.e. contain multiple polypeptide chains)
while there are multiple polypeptide chains in a quaternary structure, the entire structure is considered to be _____
_____ causes proteins to lose their secondary, tertiary, and quaternary structures
denatured proteins retain their _____ structure
loss of _____ leads to a loss of protein function
what are some causes of protein denaturation?
what are 3 structural classifications of proteins?
fibrous structural proteins are (soluble/insoluble)
fibrous structural proteins are long polymer _____
_____ form the structural components of cells
what is an example of a fibrous structural protein?
globular structural proteins are (soluble/insoluble)
_____ structural proteins are folded tightly and perform many functions -
what is an example of a globular structural protein?
intermediate structural proteins are (soluble/insoluble)
_____ structural proteins are fiber-shaped and perform many functions -
what is an example of a intermediate structural protein?
what are 2 compositional protein classifications?
simple protein compositions contain only _____
conjugated protein compositions contain _____
what are some examples of conjugated proteins? - glycoproteins (mucin); metalloproteins (hemoglobin); lipoproteins (LDL/HDL)
_____ are molecules that increase reaction rates
despite speeding up reactions, catalysts do not affect the _____ of a reaction - spontaneity
_____ are not used up by the reactions they manipulate, meaning the reaction does not change them
_____ do not change energy absorbing reactions to energy releasing ones, or vice versa
catalysts do not affect the energy of _____ or _____
_____ are biological, globular (usually) protein catalysts
substrates bind to enzymes at the _____ (location), which have unique properties and _______ _________.
the _____ measures how efficient an enzyme is in converting substrate to product. When this value is ______, the enzyme's active site will have a high substrate affinity, and the enzyme is highly efficient.
enzymes bind at the active site via the _____ model
not all enzymes are proteins - give an example of an RNA enzyme:
______ are non-protein molecules that assist enzymes
cofactors usually help enzymes by donating/accepting some reaction component, such as _____
________ are organic cofactors (e.g. vitamins)
inorganic cofactors are usually _____
_____ refer to enzymes that are bound to their cofactor - holoenzymes
what is an apoenzyme?
cofactors that tightly/covalently bind to their enzyme in a holoenzyme are known as _____
Protein enzymes have optimal _____ and _____ ranges in which they have the highest enzymatic activity.
_____ is a form of enzyme regulation, where inhibitors compete with substrates for active sites
we can outcompete a competitive inhibitor by adding more _____ -
what is enzyme saturation?
_____ is when an inhibitor binds to the allosteric site of an enzyme -
what is an allosteric site?
a noncompetitive inhibitor binding to the allosteric site modifies the _____ so that the substrate has reduced binding or cannot bind
___________ are enzymes that have both an active site and an allosteric site -
a molecule that binds to an enzyme at a site other than the active site and affects its activity
we cannot _____ allosteric inhibitors by adding more substrate
the rate of enzyme catalysis is unaffected by increasing the substrate concentration in _____ inhibition
_____ is the substrate concentration [X] at which the velocity is 50% of the Vmax
a _____ Km indicates that Vmax is reached at low substrate concentrations because enzyme ability/function is high
a _____ Km indicates that Vmax is reached at high substrate concentrations because enzyme availability/function is low
in competitive inhibition, Km increases and Vmax _____
this enzyme cleaves a phosphate group off of a substrate molecule -
this enzyme adds a phosphate group to a substrate molecule using inorganic phosphate
this enzyme transfers a phosphate group from an ATP molecule to a substrate molecule.
in noncompetitive inhibition, Km stays the same and Vmax _____
lipids are _____, non-polar molecules, meaning they do not mix well with water
_____ store energy; provide insulation; contribute to cell membranes; lead to the synthesis of critical hormones
what are the components of a triglyceride?
what are adipocytes?
triglycerides are produced by _____ reactions
which groups of which molecules react to form a triglyceride?
what type of bonds exist between glycerol/fatty acids in a triglyceride?
addition of H2O to a triglyceride's esters will break the fatty acids off the glycerol backbone by a _____ reaction
_____ fatty acids have no double bonds
saturated fatty acids form _____, stacked chains that can pack tightly
saturated fatty acids tend to be _____ at room temperature
_____ fatty acids can possess 1 (or more) double bonds
_____ fatty acids have 1 double bond
_____________ fatty acids have 2 or more double bonds
cis-unsaturated fatty acids create _____ in the fatty acid chain, meaning they do not pack tightly
cis-unsaturated fats tend to be _____ at room temperature - liquid
trans-unsaturated fatty acids pack together _____, and they are very bad for health
_____ are a unique type of lipid (fat) found in cell membranes
what are the components of a phospholipid? - a three-carbon glycerol backbone attached to 1 phosphate group and 2 fatty acid tails
phospholipids are _____, meaning they have both hydrophobic and hydrophilic properties
_____ are like phospholipids but with a carbohydrate group rather than a phosphate group
cell membranes form through spontaneous _____ of phospholipids into a bilayer
_____ is another class of lipid that makes up around 30-50% of a eukaryotic cell membrane
cholesterol contains _____ hydrocarbon rings and is also amphipathic
what are the factors that modulate membrane fluidity?
what maintains membrane fluidity in the cold?
what maintains membrane fluidity in the heat?
the _____ makes cholesterol, and we can also get it from the _____
cholesterol is a starting material for vitamin _____ and a precursor to _____ acids
_____ is the most common steroid precursor
_____ are used as hormones and are a structural component of membranes (cholesterol)
describe the general structure of a steroid:
lipids are insoluble and must be transported through the blood in structures called _____
lipoproteins contain a _____ of phospholipids, cholesterol, and proteins
lipoproteins contain a lipid _____ that contains more cholesterol and triglycerides
_____ (lipoproteins) have a low density of proteins and are generally considered unhealthy
_____ (lipoproteins) have a high density of proteins and are generally considered to be healthy
waxes & carotenoids are _____ derivatives
______ contain esters of fatty acids and monohydroxy alcohols
waxes are often used as a _____, protective coating
describe the general structure of a carotenoid:
describe the general function of a carotenoid: -
describe the general structure of a sphingolipid: -
describe the general function of a sphingolipid:
what are 2 common nucleic acids to know?
_____ have a pentose sugar attached to a nitrogenous base -
a _____ is a pentose sugar attached to a nitrogenous base and a *single* phosphate group -
nucleic acids are polymers made of _____ -
nucleoside diphosphate structure:
nucleoside triphosphate structure:
what are the 4 possible bases of a DNA nucleotide?
what are the 4 possible bases of a RNA nucleotide?
nucleotides can be further categorized depending on their nitrogen base as a _____ or _____
nitrogenous bases that are _____ have 2 rings
nitrogenous bases that are _____ have 1 ring -
Adenine and Guanine have 2 rings and are classified as _____
Cytosine, Uracil, and Thymine have 1 ring and are classified as _____ -
_____ nucleotides have ribose sugars with a hydroxyl (OH) on the 2' carbon -
_____ nucleotides have deoxyribose sugars without a hydroxyl (OH) on the 2' carbon
RNA is more reactive (less stable) than DNA because of its _____
_____ groups attach to the nucleotide sugar at the 5' carbon - phosphate
5' _____ of one nucleotide connect to the 3' _____ of another nucleotide in nucleic acids
bonding between a 5' phosphate and a 3' hydroxyl forms a _____ bond in nucleic acids, creating the sugar-phosphate backbone
nucleic acids have _____, with a 5' and 3' end
_____ add to growing nucleic acid polymers by losing two phosphates (as _____)
DNA manifests as a _____, _____ helix - antiparallel; double-stranded
purines can only hydrogen bond to _____ -
pyrimidines can only hydrogen bond to _____ -
adenine and thymine (or uracil) pair together via _____ hydrogen bonds -
cytosine and guanine pair together via _____ hydrogen bonds -
unlike DNA, RNA is usually _____ stranded -
What are the fundamental statements of the cell theory? - 1. All lifeforms have one or more cells
2. The cell is the most simple unit of life
3. All cells come from other cells
(Scientists concluded that the cell theory should be more specific as newer technologies allowed them to study cells in greater depth. Therefore, we now have the modern cell theory.)
what are the fundamental statements of the modern cell theory? - 1) all life is composed of one or more cells,
2) cells are the basic structural, functional, and organizational unit of life.
3) all cells come from pre-existing, living cells via cell division.
4) metabolism and biochemistry (energy flow) occur within cells, where all cells have the same chemical composition.
does the cell-theory apply to viruses?
the central dogma of genetics states that information flows from _____ to _____ to _____
an exception to the central dogma of genetics are _____, mis-folded proteins that cause other proteins to mis-fold -
what is the hypothesis for the creation of the first cell as we know it?
the RNA world hypothesis suggests that self-replicating _____ molecules were the precursor to current life
what are 2 central facts that support the RNA world hypothesis? [Show Less]