Cell Phys Exam #1

Cards (87)

  • Glycosidic bond is the two-bond link between the rings in an oligosaccharide or polysaccharide
  • Common disaccharides:
    • Sucrose: Glucose and Fructose linked by α(1→2)β
    • Lactose: Galactose and Glucose linked by β(1→4)
    • Maltose: Glucose and Glucose linked by α(1→4)
  • Lactose itself cannot be absorbed by the intestine and must be broken down into absorbable sugars Glucose and Galactose
  • Starch contains two types of glucose polymer:
    • Amylose: linear polymer of D-glucose residues in (α 1  4) linkage
    • Amylopectin: has stretches of similarly linked residues between branch points. The linkage at the branch is (α 1  6)
  • Glycogen is a polymer of (α 1  4) linked subunits of glucose, with (α 1  6) - linked branches
    • Glycogen is an excellent source of energy and the storage form of Glucose
    • Major storage sites for Glycogen are the Liver and Muscle
  • Cellulose is a structural element in plant cell walls and is a homopolysaccharide composed of D-glucose units in β configuration
    • Chitin is a linear homopolysaccharide composed of N-acetylglucosamine residues in β linkage, found in the exoskeletons of arthropods like insects, lobsters, and crabs
  • Amino acids are classified into three groups:
    • Essential amino acids: Cannot be made by the body and must come from food
    • Nonessential amino acids: Can be produced by the body
    • Conditional amino acids: Usually not essential, but needed during sickness or stress
  • Peptide Bonds:
    • Amino acids react to form peptide (amide) bonds
    • Direction is always N-terminal to C-terminal
    • Different peptide lengths: Dipeptide (2 residues), Tripeptide (3 residues), Oligopeptide (a few residues), Polypeptide (many residues), Protein (many residues with defined 2D and 3D structure)
  • Disulfide Bonds:
    • Disulfide bonds between two Cysteine residues play a major role in the crosslinking, folding, and stability of proteins
    • Protein crosslinking increases rigidity, functions, and proteolytic resistance
    • Insulin is an example of a protein with cysteine crosslinking, connected by disulfide bonds
  • Protein Structure:
    • Proteins come in various sizes and shapes, with fibrous proteins having a thread-like shape and globular proteins having spherical shapes
    • Proteins with one polypeptide chain have primary, secondary, and tertiary structures
    • Proteins with two or more chains have a quaternary structure
  • Levels of structure in proteins:
    • Primary structure: sequence of amino acids linked by peptide bonds
    • Secondary structure: arrangement into units like α helix
    • Tertiary structure: folded polypeptide, part of the quaternary structure of multi-subunit proteins like hemoglobin
  • Folding and Denaturing Proteins:
    • Protein folding (tertiary structure) is primarily driven by the hydrophobic effect and electrostatics
    • Denaturation: complete or partial unfolding of a protein, causing loss of biological activity
    • Proteins can be denatured by heat, mechanical agitation, pH changes, detergents, organic solvents, and chaotropic agents
  • Detergents, organic solvents (acetone, alcohols), and chaotropic agents (e.g. urea, guanidinium ion) cause hydrophobic disruption
  • Sickle cell anemia:
    • Mutation of Glutamic acid to Valine in hemoglobin leads to aggregation and sickle shape
    • Can confer resistance to malaria but cause painful obstruction of capillaries
  • Huntington's disease (HD):
    • Caused by abnormal huntingtin protein with more than 36 CAG repeats
    • Mutant protein prone to aggregation, leading to symptoms
  • Enzyme Km is a measure of substrate affinity, lower Km means tighter substrate binding
  • Enzymes have unique shapes with active sites for specific substrates
  • Enzyme "Accessories" Terminology:
    • Enzymes require cofactors for catalysis
    • Apoenzyme is the protein part of the enzyme
    • Holoenzymes consist of apoenzymes and cofactors
    • Cofactors include metal cofactors (e.g. Zn++), coenzymes (e.g. NAD(H)), and prosthetic groups (e.g. Heme)
  • Enzyme Regulation:
    • Allosteric regulation alters enzyme structure and activity
    • Competitive, uncompetitive, and mixed/noncompetitive inhibition
    • Reversible inhibition mechanism
  • DNA Replication:
    • Begins at Origins of Replication
    • Strands open to form Replication Forks
    • New strands grow at the forks
    • RNA primers made on lagging strand and erased by DNA repair enzyme
  • Cell Cycle:
    • Cyclins (G1/S, S, M, G1) regulate cell cycle progression
    • M-Cdk triggers spindle assembly in mitosis
    • Mitotic spindle structure and phases (metaphase, anaphase, telophase, cytokinesis)
  • Biochemistry:
    • Hemiacetals formed by reaction between alcohol and aldehydes
    • Glucose monitors use Glucose oxidase to react with metals for electric current
    • Dietary fibers lower cholesterol levels
  • Protein Structure:
    • Phenylketonuria caused by lack of phenylalanine hydroxylase
    • Red blood cells can't use fat for ATP production
    • Three amino acids (Serine, Threonine, Tyrosine) can be phosphorylated
  • Protein Structure:
    • Peptide backbone with attached side chains
    • Nonpolar amino acid side chains form a hydrophobic core
    • Differences between fibrous and globular proteins
    • Glycine is rare in alpha helix and beta sheet structures due to conformational flexibility
  • DNA:
    • Write the complementary sequence of the given DNA template
  • 3 main sections of the cells: nucleus, cytoplasm, and outer layer
  • what do both prokaryotes and eukaryotes have in common? both have DNA, ribosomes, a plasma membrane, and cytoplasm
  • sugars make up polysaccharides
  • fatty acids make up fats, lipids, and membranes
  • amino acids make up proteins
  • nucleotides make up nucleic acids
  • a bacterial cell is 30% chemicals and 70% H2O
  • glycosidic bonds is 2 bonds sharing an oxygen
  • lactose can't be absorbed by intestines
  • lactose must be broken down into glucose and galactose
  • 2 types of glucose polymer in starch: think (Amy)
  • glycogen is stored in the liver and muscles
  • examples of INSOLUBLE fiber is: whole-wheat flour, wheat bran, green beans
  • fiber: normalizes bowel movements, helps maintain bowel heath, lowers cholesterol, and controls blood sugar
  • nucleotide: has a phosphate TAIL