Bio1 Molecules/ Fundamentals Flashcards
Any substance that takes up space and has mass
Matter
What matter is composed of?
Elements
Substance that has specific chemical/physical properties
Element
Smallest unit of matter/retains all chemical properties of element
Atom
Combining 2 or more atoms creates a
Molecule
Atoms carbon tends to bond with in an organic molecule
Hydrogen,oxygen,nitrogen
Molecules that contain more than one element
Compounds
Strong attractive forces that hold atoms WITHIN a molecule
Intramolecular forces
Force that exists BETWEEN molecules
Intermolecular forces
Is intra or intermolecular forces stronger?
Intramolecular forces are stronger
Type of force that determines physical properties
Intermolecular forces
Molecules that have potential of bonding to other identical molecules through chemical reactions
Monomers
The process which polymers are formed by monomers bonding is called
Polymerization
3 varieties of carbohydrates
Monosaccharides,disaccharides,polysaccharides
Monosaccharides have a ratio of precisely
1 carbon per water molecule
Monosaccharide empirical formula
(CH2O)n
5 carbon monosaccharides
Pentodes
6 carbon monosaccharides
Hexoses
Sugar molecule is ALPHA if hydroxyl Group on first carbon
Points down
Sugar molecule is BETA if hydroxyl group on first carbon
Points up
An example of pentose (5carbon sugar)
Ribose
____ and _____ are examples of hexoses (6carbon sugars)
Glucose , Fructose
Glucose and fructose are
Isomers
Type of carbohydrate that forms when 2 monosaccharides bond
Disaccharide
Monosaccharides monomers bond via which reaction
Dehydration/condensation reactions
Functional group and atom that combine in dehydration/condensation reaction
Hydroxyl (OH) and Hydrogen
Type of bond in dehydration/condensation reaction
Covalent
What is released in a dehydration/condensation reaction?
H2O
Opposite of dehydration/condensation reaction
Hydrolysis; adds H2O to covalent bond splits monomers apart
Bond that forms when carbohydrate attaches to another molecule
Glycosidic
Carbohydrates linked to lipids are called
Glycolipids
Carbohydrates linked to proteins
Glycoproteins
1glucose + 1 fructose =
Sucrose
1 galactose + 1 glucose=
Lactose
1 glucose + 1 glucose=
Maltose
Polysaccharides are long polymers of
Monosaccharides
2 polysaccharide purposes
Storage, structure
Crucial storage polysaccharide in plants
Starch
Starch contains many glucose monomers in____ and ____ forms
Linear, branched
Linear plant starch
Amylose
Type of glycosidic bonds in amylose
Alpha-1,4- glycosidic bonds
Branched form of plant starch
Amylopectin
Type of bonds in amylopectin
- Alpha1,4 glycosidic (linear)
- Alpha1,6 glycosidic (branched)
Storage polysaccharide found in humans
Glycogen
Glycogen contains many
Glucose monomers
Which is more branched amylopectin or glycogen?
Glycogen more branched
Types of bonds glycogen
- alpha 1,4 glycosidic
- MANY alpha 1,6 glycosidic
Glycogen primarily stored in what type of human cells?
Liver cells(mostly) ; also muscle cells
Name 2 alpha glucose polysaccharides
Starch(amylose or amylopectin) and glycogen
Structural polysaccharide found in plant cell walls, wood and paper
Cellulose
Cellulose is a ___
Glucose polymer
Type of bonds in cellulose
Beta 1,4 glycosidic bonds
What beta 1,4 glycosidic bonds in cellulose do?
Allow cellulose to form linear strands that pack together parallel
Intermolecular force that holds adjacent cellulose strands together in parallel
Hydrogen bonds
Due to its structure cellulose has
High rigidity
Can humans digest cellulose?
No; it passes through digestive tract as fiber
Chitin is a __
Structural polysaccharide
Chitin is found in ____ and ____
Fungi cell walls, insect exoskeleton
Chitin is a structural polysaccharide of ____
N-acetylglucosamine monomers
Types of bonds in chitin
Beta 1,4 glycosidic bonds
Two beta glucose polysaccharides
Chitin and cellulose
Proteins contain polymers called
Polypeptides
Polypeptides contain monomeric subunits called
Amino acids
4 things central carbon in amino acid bonded to
- amino group(NH2)
- Hydrogen atom
- carboxyl group(COOH)
- R group
Total number of amino acids
20
Amino acids are linked via covalent bond called
Peptide bond
Amino acids form peptide bonds via
Dehydration/condensation reactions
Reactions that separate amino acids of polypeptide
Hydrolysis
Enzyme that catalyzes peptide bond formation
Peptidyl transferase
Peptidyl transferases are ___
Aminoacyl transferases
Polypeptides have a ___ terminus and a ____ terminus
Amino(N-) ; carboxyl(C-)
Primary structure of a protein
It’s amino acid sequence
All proteins have
Primary structure
Secondary structure of protein
Folds due to intermolecular forces between atoms of polypeptide backbone
All the amino acid structural features EXCLUDING R group
Polypeptide backbone
Secondary structure does not include
Interactions between R group atoms
Which level protein structure includes alpha helices and beta pleated sheets?
Secondary
Most common intermolecular force for secondary structure? And where do they occur?
Hydrogen bonding; occurs between carboxyl(COOH)and amino groups(NH2
The common interactions between R groups in tertiary structure
- Ionic bonding
- Hydrogen bonding
- Dipole-dipole interactions
- Van see Waal( London dispersion forces)
- Hydrophobic interactions
- Disulfide bonding
Tertiary structures usually involve
Non-covalent interactions
Bond in tertiary structures that involve covalent interactions
Disulfide bond
Which amino acids allow disulfide bond formation?
Cysteine
Structure that refers to large proteins that have multiple subunits(multiple polypeptide chains)
Quaternary
Multiple polypeptide chains in a quaternary structure, entire structure is
Protein
Causes proteins to lose secondary,tertiary,quaternary structures
Protein denaturation
Denatured proteins retain
Primary structure
Loss of shape leads to
Loss of protein function
Causes of protein denaturation
- excess temp
- chemicals
- pH changes
- Radiation
3 structural classifications of proteins
- fibrous
- globular
- intermediate
Intermediate and globular structural proteins are
Soluble
Fibrous structural proteins are
Insoluble
Protein that forms structural component of cells
Fibrous structural protein
Example of fibrous protein
Collagen
Proteins that are folded tightly and perform many functions
Globular
Example of globular structural protein
Albumin
Fiber shaped proteins that perform many functions
Intermediate
Example of intermediate structural protein
Fibrinogen
The 2 compositional protein classifications are
Simple, conjugated
Simple protein compositions contain only
Amino acids(ex: albumin)
Conjugated protein compositions contain
Amino acids+ non protein components
Examples of conjugated proteins
Glycoproteins (mucin)
Metalloproteins(hemoglobin)
Lipoproteins(LDL/HDL)
Molecules that increase reaction rates
Catalyst
What part of reaction do catalysts not affect?
Spontaneity
Catalysts are not
Used up in reaction; they manipulate meaning reaction does not change them
Catalysts lower this to speed up reaction
Activation energy/transition state energy
Catalysts cannot change
Energy absorbing(endothermic) reactions to ——-> energy releasing(exothermic) reactions and vice versa
Catalysts do not affect energy of
Reactants or products
Biological, globular protein catalysts are
Enzymes
Substrates bind to enzymes at the
Active site
Active sites have unique properties and
Substrate specificity
Measures how efficient enzyme is converting substrate to product
Scecificity constant
Enzymes bind at active site via
Induced fit model
Example of RNA enzyme
Ribozyme
Non protein molecules that assist enzymes
Cofactors
Cofactors usually help enzymes by donating/accepting a component such as
Electrons
Organic cofactors (ex vitamins)
Coenzymes
Inorganic cofactors are
Metal ions ( iron, magnesium)
Enzymes that are bound to their cofactor
Holoenzymes
Enzymes not bound to cofactor
Apoenzyme
Cofactors that tightly/covalently bind to their enzyme in holoenzyne
Prosthetic groups
Proteins have highest enzymatic activity when ____ and____ are in optimal ranges
pH and temp
Enzyme regulation where inhibitors compete with substrate for active sites
Competitive inhibition
Can outcompete competitive inhibitor by
Adding more substrate
What is enzyme saturation
When all the active sites are occupied
Inhibitor binds to allosteric site of enzyme
Non competitive inhibition
Different location then active site of enzyme catalysis
Allosteric site
Non competitive inhibitor binds to allosteric site modifies the
Active Site ;so substrate has reduced/inability to bind
