Chapter 5 Flashcards
What are 6 carbon sugars called
Hexose
What are 5 carbon sugars called
Pentose
What are 3 carbon sugars called
Triose
Definition of saturated fats
Fatty acid that only has single bonds allowing more hydrogen atoms on the carbon skeleton
Definition of unsaturated fats
Fatty acids that have one or more double bond
What is trans fat
Unsaturated fat formed by hydrogenation of oils containing one or more trans double bonds
Definition of cholesterol
Steroid that forms part of cell membrane and act as a precursor for synthesis of other steroids
Functions of proteins
Catalyst, defense, storage, transport, communication, movement, structural support.
Catalyst term
Chemical agent that increases rate of a reaction without being consumed by it
Polypeptides
Polymer of many amino acids linked by peptide bonds
Protien
Biologically functional molecules consisting of 1 or more polypeptide with a specific formation
Amino acids
Organic molecule that has carboxyl and amino groups; monomer of polypeptide
What is the alpha carbon
The asymmetrical carbon in an amino acid
What is the r group
Distinguishing feature of amino acids
Primary structure
Linear, dictates secondary structure and tertiary structure
Secondary structure definition
Coiled or folded from hydrogen bonds, between the polypeptide backbone
What causes hydrogen bonding in secondary structures
The oxygen atoms negative charge and nitrogen atoms being slightly positive
What causes alpha helix in secondary structure
Coil held together by hydrogen bond between every 4th amino acid
what is the Beta pleated sheet
The folds in secondary structure, 2 or more segments of polypeptide lying parallel connected by hydrogen bonds
What is tertiary structure
Overall 3D shape resulting from polypeptides interacting with side chains
What is a hydrophobic interaction in amino acids
Type of interaction in amino acids with non polar R groups that end up in clusters at its core
In tertiary structures what holds nonpolar bonds
Van deer walls interaction
What bonds holds the tertiary structure together
hydrogen bonds (between polar R groups) and ionic bonds (between positive and negative R groups)
What bonds reinforces the shape of tertiary structures
Disulfide bridges or covalent bonds
What is quaternary structure
contain 2 or more polypeptides chains combined into one functional protein
Biology perspective of sickle cell disease
Disease caused by nucleotide change in alpha globin gene causes hemoglobin to aggregate changing cell shape
Denaturation definition
For proteins, a process which disruption of weak chemical bonds and interactions make proteins lose their innate shape
What technique is used to study 3-D shape of molecules
X-ray crystallography
What is nucleic acid
Polymer of nucleotides
Function of RNA
Protein synthesis, gene regulation, and genome for viruses
What is the flow of genetic information
DNA>RNA>protein
What synthesis mRNA
DNA
Function of mRNA
Interact with ribosomes to direct production of polypeptides
Where is DNA located
Nucleus
Where does mRNA relay information
Cytoplasm
What is a nucleoside
Portion of nucleotide without a phosphate group; lost after polymerization
What are nitrogenous bases
Have 1-2 rings that include nitrogen atom. They are bases because the nitrogen tends to be basic in solutions
What is pyrimidines
One six membered ring
Purines
One six membered ring fused to a five membered ring
What bond forms sugar phosphate backbone of nucleic acid
Phosphodiester bond
