Biology: Proteins and Nucleic Acids
Biology: Proteins and Nucleic Acids BIOL 1107
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Brittany Ariana Borzillo
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This 4 page Class Notes was uploaded by Brittany Ariana Borzillo on Friday September 16, 2016. The Class Notes belongs to BIOL 1107 at University of Georgia taught by Norris A. Armstrong in Fall 2015. Since its upload, it has received 7 views. For similar materials see Principles of Biology I in Biology at University of Georgia.
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Date Created: 09/16/16
PROTEINS AND NUCLEIC ACIDS Proteins are one of the most abundant organic molecules in living systems with the most diverse range of functions of all macromolecules Types and Functions o Enzymes Produced by living cells Catalysts in biochemical reactions Usually complex or conjugated proteins Help break down, rearrange, and synthesize Catabolic enzymes Break down substrates Catalytic enzymes Impact rate of reaction Hormones Chemical-signaling molecules secreted by endocrine cells that act to control or regulate physiological processes, including growth, development, metabolism, and reproduction Usually small proteins or steroids o Have different structures and molecular weights o Structure is critical to function o Denaturation When changes in temperature, pH, and exposure to chemicals lead to permanent changes in the shape of protein, leading to loss of function Amino acids o Monomers that make up protein Each has a fundamental structure, containing a central (alpha) carbon bonded to an amino group, a carboxyl group, and a hydrogen atom 20 make up all proteins o essential amino acids isoleucine, leucine, cysteine amino acids that are necessary for construction of proteins in the body but are not produced by the body o sequence and number of amino acids determines the shape, size, and function of proteins o amino acids are attached to one another by double bonds formed by dehydration synthesis (peptide bond) carboxyl group from one releases hydroxyl and amino group releases a hydrogen to produce water linkages are referred to as peptides and become polypeptides free amino group on one end called the N-terminal free carboxyl group on opposing end called C-terminal PROTEIN STRUCTURE the shape of protein is critical to its function enzyme blinds to a specific site referred to as an active site o changing structure manipulates site primary structure o unique sequence of amino acids in polypeptide chain o determined by gene encoding of protein change in coding of the nucleotide sequence may lead to different amino acids being added to the chain secondary structure o local folding of the polypeptide in some regions o most common are the alpha-helix and beta-pleated sheets helix held together by hydrogen bonding variant groups protrude out of the helix chain sheets formed by hydrogen bonding between atoms on the background of the polypeptide chain variant groups extend above and below the sheets tertiary structure o three-dimensional structure o arrangement of variant groups causes three-dimensional structure quaternary structure o proteins formed from several polypeptides o weak interactions between subunits strengthen overall structure protein folding o chaperones assist in folding proteins associate with the target protein during folding act by preventing aggregation of polypeptides which make up complete structure denaturation o often reversible because the primary structure of the polypeptide is conserved in the process if the denaturing agent is removed allows protein to resume function NUCLEIC ACIDS most important macromolecules for continuity of life o carry genetic blueprint of a cell and carry instructions for the formation of the cell DNA o Deoxyribonucleic acid o Genetic material found in all living things o Genetic material found in all living things o Found in nucleus and organelles of eukaryotic cells o Prokaryotic cells just have DNA inside o Genome Entire genetic content of a cell o Determines which genes are “on” RNA o Ribonucleic acid o Mostly involved with protein synthesis o mRNA messenger RNA communicates with cells nucleotides o monomers that make up DNA and RNA o polynucleotides are multiple nucleotides combines o nitrogenous base, pentose (5-carbon) sugar, one or more phosphate groups DNA Nitrogenous Bases Adenine o Purine (2-Carbon Ring) Guanine o Purine (2-Carbon Ring) Cytosine o Pyrimidines (1-Carbon Ring) Thymine o Pyrimidines (1-Carbon Ring) o Carbon labeled as 1’, 2’, 3’, etc. o Phosphodiester 5’—3’ linkage Phosphate residue attached to hydroxyl group of the 3’ carbon od the sugar of the next nucleotide DNA Double-Helix Structure o Sugar and phosphate lie on the outside of the helix, forming the backbone of DNA o Nitrogenous bases are stacked on the interior o A T (U) o G C o During DNA replication, each strand is copies, resulting in a daughter DNA double-helix containing a parental strand and a newly synthesized strand RNA Single-stranded Ribose, nitrogenous base, and phosphate mRNA o messenger RNA o carries message from DNA controls cellular activity o if a cell requires certain protein to be synthesized the gene is turned on and mRNA is synthesized rRNA o ribosomal RNA o major constituent of ribosomes on which mRNA binds o enzymatic activity catalyzes formation of the peptide bonds between two aligned amino acids tRNA o transfer RNA o one of the smallest RNA 70-90 nucleotides o carries amino acids to site of protein synthesis microRNA o smallest RNA o regulates gene expression interferes with mRNA messages extensive intermolecular base pairing transcription o DNA dictates the structure of protein Translation o RNA dictates the structure of protein
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