Kin 101: Chapter 2 Flashcards
Organic Molecules
Molecules that contain Carbon
Biomolecules (definition)
Organic molecules in living organisms
Biomolecule (types)
Carbs, Lipids, Protein, and Nucleotides
Carbohydrates
Sugars; Energy and Building Blocks
Lipids
Fats, and Oil; Energy and Building Blocks
Protein
Poly of AA; Energy and Building Blocks
Nucleotides
DNA, RNA, ATP; structure for genetic material, to store energy and regulate metabolism
Mixed Biomolecules
Conjugated proteins, glycosylated molecules, polymers
Conjugated Proteins
Proteins combined with another biomolecule
What are Glycosylated Molecules
Molecules attached to carbohydrates
Polymers
Biomolecules made of repeating units
High Energy Electrons
Electrons in certain atoms can capture energy from their environment and transfer it to other atoms
Free Radicals
Unstable molecules with an unpaired electron. They are thought to contribute to aging and to the development of certain diseases
Non-covalent Interactions determined what?
Interactions are based upon bonds, determine solubility, shape, and their reversibility and functional pairing
Types of Carbohydrates
There are fast (glucose) and slow (fructose) carbohydrates, as well as mono, di, oligo, and polysaccharides
Monosaccaride
Simple sugar that is the building blocks of carbohydrates. Ex. Ribose
Disaccharides
Glucose, plus another monosaccharide
Polysaccaride
Glucose polymers, all living cells store these
What is the best form of Carbohydrates for sports performance?
Combination of more than one, glucose and fructose
Ogliosaccaride
Carbohydrate who’s molecules are composed of a relatively small number of monosaccharide unit
What are lipids made of?
Glycerol and Fatty Acids (mono, di, or tri)
Saturated Fatty acid
No double bonds between carbons
Monounsaturated Fatty acid
One double bond between carbons
Polyunsaturated Fatty acid
Two or more double bonds between carbons
What are some lipids, that don’t count as “true lipids”
Phospholipids, Steroids, and Eicosanoids
Solubility
Ability of a solute to dissolve in a solvent
Hydrophobic
Not soluble in water; non polar molecules
Hydrophilic
Soluble in water; ions, and ionic or polar molecules
Nucleotide (molecule)
Consists of 1 or more phosphate, a five carbon sugar, and a carbon-nitrogen ring; used for energy transfer (ATP, ADP, AMP)
What does ATP stand for? and what is its purpose
Adenosine Triphosphate; the common energy currency of the body
Nucleic Acid, definition and an example
Nucleotide Polymers, that store and transfer genetic info; DNA RNA
What are Amino Acids
The building blocks of proteins
Protein Types
Peptide, oligopeptide (2-9 AA), polypeptide (10-100 AA), and proteins (>100 AA)
4 Structures of Proteins (Amino Acid Chain Names)
Primary, Secondary (a-helix, or b-strands), Tertiary; collagen (fibrous or globular), and Quartinary; hemoglobin
What biomolecule has the most complex shape?
Proteins
Does the shape of a protein relate to its function?
Yes
Enzymes
Biological catalysts that speed up chemical reactions
Membrane Transporters
In cell membranes help move substances back and forth between the ICF and ECF
Signal Molecules
The molecules that are responsible for transmitting information between cells in your body (act as hormones)
What is a Receptor
Proteins that bind signal molecules and initiate cellular responses
Binding Proteins
Bind and transport molecules throughout the body
Immunoglobulins
Extracellular immune proteins that help protect the body from foreign invaders and substances
Regulatory Proteins main function is to?
Turn cell processes on and off
Binding Site variability
The protein’s binding site changes shape (conformation) to fit more closely to the ligand
Binding Site
Location on a protein where substrate can attach
Specificity (in terms of Proteins)
The ability of a protein to bind to a certain ligand or a group of closely-related ligands
Affinity
Strength of a bond and the desire for that bond to occur
Mass Action and Binding Reactions
(eq)
If equilibrium is disturbed by adding or removing one of the products, the reaction equation will shift direction to restore the equilibrium condition
Cofactors
Share the binding site
Allosteric Activators
Modify the active site of the enzyme so that the affinity for the substrate increases
Chemical modulation
Affects protein binding reversibly or irreversibly to proteins and alter their binding affinity
Antagonists (modulator)
Inhibitors: chemical modulators that bind to a protein and decrease its activity
What does small changes in pH or temperature do?
Modulate protein to be denatured
Denatured
When a protein loses its conformation
Net (in terms of protein)
Build up and break down of proteins to always have a net amount
What do Reaction Rate and Saturation do?
They Influence Protein Activity
Conformation change
Change in shape of a macromolecule
pH
The measure of the concentration of free H+ concentration or the acidity of a substance
Buffers (pH)
Substances that moderate changes in pH
Acidic Vs Basic
H+=A OH-+B
Cofactor
Attached to proteins; is required for the protein’s biological activity. A non-protein chemical compound.
Up-regulation
Signalling pathways programmed for the production of proteins. A cell increases its response to a substance or signal from outside the cell to carry out a specific function
Down-regulation
The programmed removal of proteins
How does protein powder prove the importance of understanding saturation
For example if you take more than the amount your body can possible satirize you are just wasting the rest because the body can only hold so much
4 Important biological roles of electrons
idk
How is molecular shape directly related to its function
The molecule’s shape and chemical properties facilitate interactions with other molecules and determine its role in the cell
Seven important functions of soluble proteins in the body
Structure
Signaling
Defense
Transport
Contractile
Storage
Enzyme
Solubility enhances the rate of which preotein wants to bind
Competition in protein-ligand binding
A competitive binding assay typically measures the binding of a labeled ligand to a target protein in the presence of a second, competing but unlabeled ligand
