Chapter 2 Continue Flashcards
External surface of cell membrane and mucus of respiratory and digestive tracts
Glycoproteins
External surface of cell membrane
Glycolipids
Cells that hold cells and tissue together
Proteoglycans (mucopolysaccharides)
Carbon compound with high ratio of hydrogen and Carbon
Lipids
Five primary types of lipids
fatty acids, triglycerides, phospholipids, eicosanoids, steroids
Chain of 4 to 24 carbon atoms
Fatty Acids
Carboxyl (acid) group on the end
Fatty Acids
Four types of fatty acids
Saturated, unsaturated, polyunsaturated, essential fatty acids
Carbon atoms saturated with hydrogen, straight,
Can not have more hydrogen,
Solid( room temp)
Saturated
Contains C=C bonds w/o hydrogen Bent Cis double bond Can have more hydrogen Liquid( room temp)
Unsaturated
Take unsaturated fat chemically make it have the structure of saturated
Ex crisco
Risk of heart disease
Trans Fat
Same as unsaturated but has more Cis double bonds
Polyunsaturated
A single molecule of glycerol can be covalently linked by THREE fatty acids to make this
Triglyceride
Primary function of a triglyceriod
Store energy long term
Phosphate group combined to two fatty acid chains is the structure of
Phospholipids
What a cell membrane is made of is its function
Phospholipids
Produced in all tissues
Eicosanoids
Function is to stay in one place and communicate between cells
Eicosanoids
Structure looks like a carbohydrate but is a lipid
Eicosanoids
A lipid with 17 of its carbon atoms in four rings
Steroids
“Parent” steroid from which the other steroids are synthesized
Cholesterol
Communicate between cells by moving around
Steroids
Are used to strengthen the cell (like a pack on a tube)
Cholesterol
“Good” or “Bad” cholesterol is defined how
By how it is stored
“Good” cholesterol
Lower ratio of lipid to protein
HDL high density lipoprotein
“Bad” cholesterol
High ratio of lipid to protein
Contributes to cardiovascular disease
LDL low density lipoprotein
A polymer of amino acids
Proteins
Central carbon with three attachments
Amino acids
How do amino acids differ
R group
What is the purpose of a protein
Make DNA
What the structure of a protein
Amino acids put together
Molecule composed of two or more amino acids joined by peptide bonds
Peptide
Amino group of one amino acid to the carboxyl group of the next; formed by dehydration synthesis
Peptide bond
Peptide name for two amino acids
Dipeptides
Peptide name for three amino acids
Tripeptides
Peptide name for fewer than 10-15 amino acids
Oligopeptide
Peptide name for more than 15 amino acids
Polypeptide
Peptide name for more than 50 amino acids
Proteins
Polypeptides and proteins are in what peptide group
Protein group
Three dimensional shape of protein crucial to function
Conformation
Extreme conformational change that destroys function
Extreme heat
Ex. When cooking an egg
Desaturation
What is the primary structure for a protein
To sequence amino acid which is encoded in the genes
Springlike shape secondary structure for protein
Alpha helix
Pleated, ribbon shape
Zig zag secondary structure for proteins
Beta
Further bending and folding of proteins into globular and fibrous shapes of protein structure
Tertiary structure
Compact tertiary structure well suited for proteins embedded in cell membrane ; a glob
Globular proteins
Slender filaments better suited for roles as in muscle contraction and strengthening the skin; string like curly then straight , curl then straight
Fibrous proteins
Association of two or more desperate polypeptide chains
Ex insulin
Quaternary structure
Conjugated proteins contain a non amino acid moiety
Prosthetic group
Tough structural protein, gives strength to hair nails and skin
Keratin
Durable protein contained in deeper layers of skin bones cartilage and teeth
Collagen
To which signal molecules bind recieve and send messages
Receptors
Any hormone or molecule that reversible binds a protein
Ligand
Channels in cell membrane what govern what passes through
Membrane transport
Enzyme
Catalysis
Molecule with the ability to change shape repeatedly
Motor protein
Proteins that bind cells together
Cell adhesion
Proteins that function as biological catalysts
Enzymes
Substance an enzyme acts upon
Substrate
Energy needed to get reaction started
Lowers activation energy
Highly specific fit for and enzyme substrate specificity
Lock and key
Water splitting; adding h and oh from water
Hydrolysis
Enzymes are not consumed by the reaction only replaced by building with genes
Truss biking of enzymes
Happens quickly one enzyme molecule can consume millions of substrate molecules per sec
Astonishing speed
Factors that change enzyme shape
pH and temperature
Chain of reactions with each step usually catalyze by a different enzyme
A->B->C->D
Metabolic Pathways
Nitrogen base Sugar Phosphate groups are the three components of what
Nucleotide
Best known nucleotide
ATP
Body’s most important energy transfer molecule and briefly store energy
Adenosine Triphosphate ATP
Between the second and third phosphate group there are
High energy bonds
Most energy (ATP) goes where
Active transport
What does the mitochondria do
Makes ATP
Are there other nucleotides other than ATP
Yes
Double helix; ATCG; without oxygen in the ribose
DNA (deoxyribonucleic acid)
Single strained;AUCG; with oxygen in the ribose
RNA (ribonucleic acid)