Store, transmit and express hereditary information. Made of C, H, O, N and P. Each nucleotide consists of a phosphate, pentose sugar and a nitrogenous base.

A phosphate group is added to the 5’ carbon of the sugar (which is attached to the base) to form a nucleotide

Stores information, primary structure of proteins, sequences of RNA molecules Heritable. 2 chains of covalently bonded nucleotides - sugar to phosphate bonds = phosphodiester. Hydrogen bonds between bases in center.

link adjacent nucleotides: Phosphodiester linkage Directionality and 5’ to 3’

Transmits and translates DNA information into proteins. Many enzymatic and regulatory fxns. Only 1 kind DNA but 15 known RNA (ex; 3 main: mRNA, tRNA, rRNA)More interesting than DNA?RNA forms variable structures: Less stable than DNA, but means reversible

The most complex biological molecules C, H, O, N and a little S. Dehydration synth. joins monomers= “Peptide bonds”

21 known biological amino acids All amino aids contain an amino and carboxyl group, bonded to a central “alpha” carbon. Differs in the structure of variable group (R) which is bonded to the alpha carbon.

“chain” Sequence of amino acids in one polypeptide chain Peptide bonds between amino acids

“coil” Regular, repeating 3D structures found in all polypeptide chains Alpha-helix (spiral) & Beta-pleated sheets Due to hydrogen bonding between atoms of the polypeptide (no R groups involved yet)

“compress” 3D shape of one polypeptide chain (aka “conformation”)Forms due to interactions between R group atoms and: Other R groupsThe cellular environment (hydrophilic/hydrophobi acidic or basic pH… ionic or covalent?) R group interactions vary

“combine” 3D shape of any protein made of more than one polypeptide chain (many are). The overall structure when multiple chains combine for a functional protein.

Functions of Proteins:

Function of a protein include: Enzyme- carry out chemical reactions or assist in creating new molecules Antibody-help protect body from disease Storage Protein for developing young

Functions of Proteins 2:

Transport- bind to and carry small atoms and molecules through the body Messenger- transmit signals (ex: hormone) Movement- muscles Structural- provide structure and support

Change in the structure of a protein...results in a change in function Inactive (do not work well, if at all) May be reversed or irreversible (ex: frying an egg, fever denatures proteins in blood)

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Nucleic Acids & Pro.

Term	Definition
Nucleic Acids	Store, transmit and express hereditary information. Made of C, H, O, N and P. Each nucleotide consists of a phosphate, pentose sugar and a nitrogenous base.
Phosphate group	A phosphate group is added to the 5’ carbon of the sugar (which is attached to the base) to form a nucleotide
DNA	Stores information, primary structure of proteins, sequences of RNA molecules Heritable. 2 chains of covalently bonded nucleotides - sugar to phosphate bonds = phosphodiester. Hydrogen bonds between bases in center.
Polynucleotides	link adjacent nucleotides: Phosphodiester linkage Directionality and 5’ to 3’
RNA	Transmits and translates DNA information into proteins. Many enzymatic and regulatory fxns. Only 1 kind DNA but 15 known RNA (ex; 3 main: mRNA, tRNA, rRNA)More interesting than DNA?RNA forms variable structures: Less stable than DNA, but means reversible
Protein	The most complex biological molecules C, H, O, N and a little S. Dehydration synth. joins monomers= “Peptide bonds”
Amino Acids	21 known biological amino acids All amino aids contain an amino and carboxyl group, bonded to a central “alpha” carbon. Differs in the structure of variable group (R) which is bonded to the alpha carbon.
Primary structure	“chain” Sequence of amino acids in one polypeptide chain Peptide bonds between amino acids
Secondary Structure	“coil” Regular, repeating 3D structures found in all polypeptide chains Alpha-helix (spiral) & Beta-pleated sheets Due to hydrogen bonding between atoms of the polypeptide (no R groups involved yet)
Tertiary structure	“compress” 3D shape of one polypeptide chain (aka “conformation”)Forms due to interactions between R group atoms and: Other R groupsThe cellular environment (hydrophilic/hydrophobi acidic or basic pH… ionic or covalent?) R group interactions vary
Quaternary structure	“combine” 3D shape of any protein made of more than one polypeptide chain (many are). The overall structure when multiple chains combine for a functional protein.
Functions of Proteins:	Function of a protein include: Enzyme- carry out chemical reactions or assist in creating new molecules Antibody-help protect body from disease Storage Protein for developing young
Functions of Proteins 2:	Transport- bind to and carry small atoms and molecules through the body Messenger- transmit signals (ex: hormone) Movement- muscles Structural- provide structure and support
Denaturation	Change in the structure of a protein...results in a change in function Inactive (do not work well, if at all) May be reversed or irreversible (ex: frying an egg, fever denatures proteins in blood)

Created by: nuhaSalim

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