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