Chapter 2 - Chemical Principles Flashcards
Proteins
-organic molecules that contain carbon, hydrogen, oxygen, nitrogen, and sometimes sulfur
-make up 50%+ of a cells dry weight
-essential aspects of structure and function
-consist of subunits called Amino Acids
Enzymes
-proteins that speed up chemical reactions
Protein Fucntions
-transport chemical in and out of cells
-kill bacteria
-can be toxins
-contraction of animal muscle cells
-cell movement
-structure of cell walls, membranes, cytoplasmic components
-can have regulatory functions such as hormones
Amino Acids
-the building blocks of proteins
-contain at least one carboxyl group and one amino group attached to the same carbon atom
-a side group also attaches, this is the amino acids distinguishing feature
Carboxyl Group
-COOH
-a central C double bonded to an O and a single bonded OH
Amino Group
-NH₂
-a N single bonded to the central C with 2 Hydrogens single bonded separately
Side (R) Group
-distinguishing feature
-can be H, CH2, an organic molecule
-affect the total structure of the protein
Dehydration Synthesis
-anabolic, requires ATP
-removes a water group to bind amino acids together
Peptide Bonds
-formed by dehydration synthesis
-bind Amino Acids together on opposite sides to create a polypeptide chain
-for every bond, one water molecule is releases
How many Amino Acids make up 1 protein molecule?
about 250-300
Primary Structure
-the Amino Acids are linked together to form a polypeptide chain
-a genetically determined sequence
Secondary Structure
-repeated twisting or folding of the polypeptide chain
-results from hydrogen bonds joining the peptide bond atoms at various locations
-can form as helices/helix or pleated sheets
Tertiary Structure
-3D structure of a polypeptide chain
-folding is not repetitive/predictable
-not held together by hydrogen bonds, instead by action in the side groups (polar molecules)
Quaternary Structure
-gathering of 2+ polypeptide chains to operate as a single functional unit
-same bonds as tertiary
-may be globular or fibrous
Denaturation
-hostile environment (ie. temp, pH, Na+ conc.) may unravel the protein
-this makes the protein no longer functional
Nucleic Acids
-consist of nucleotides
-DNA and RNA
Nucleotides
-have a pentose sugar, phosphate group, and a nitrogen base
Nitrogen Base
-can be purine or pyrimidine
-cyclic compounds made uo of carbon, hydrogen, oxygen, and nitrogen
-GCATU
-create the rungs of the ladder
Purine Base
-double ring structures
-adenine (A)
-guanine (G)
Pyrimidine Base
-single ring structure
-thymine (T)
-cytosine (C)
-uracil (U)
Nucleoside
combination of a purine/pyrimidine + a pentose sugar without a phosphate group
Hydrogen Bonds
-hold together the rungs on the ladder (nitrogen bases)
-shown as broken lines yes are rather stable
G + C
-guanine and cytosine held together by a triple hydrogen bond
A + T
-adenine and tyrosine held together by a double hydrogen bond
Pentose Sugar Group
-a 5 carbon atom in the shape of a pentagon with one oxygen
-carbons are numbered 1-5 starting after the oxygen group and moving clockwise
-with phosphate creates the backbone
-there is an OH group bound to C2 and this extra O creates ribose sugar
-each C is hyphenated to differ from Cs not apart of the sugar
Phosphate Group
-often starts as PO4- which is unbalanced
-phosphate becomes balance when it makes DNA
-creates backbone of the ladder
DNA
-2ʹ-deoxyribonucleic acid
-the master molecule of the cell
-GCAT
-double helix form/twisted ladder
RNA
-ribonucleic acid
-the workbench for protein synthesis
-sugar is full ribose, not deoxygenated
-single stranded rather than double helix
-has uracil: GCAU
Types of RNA
1) mRNA: messenger RNA
2) rRNA: ribosomal RNA
3) tRNA: transfer RNA
-all have roles in protein synthesis
What makes deoxyribose?
-ribose has a OH group at C2
-deoxyribose has only a H at C2
ATP
-adenosine triphosphate
-principle energy carrying molecule of the cell
-stores energy released by some chemical reactions
-consists of an adenosine unit (adenine and ribose) and three phosphate groups
