Flashcards
amino acids
Cards in this deck (32)
- 1All proteins are made up from ___ amino acids20
- 2Describe an amino acidCentral Carbon that bonds to:
-Hydrogen
-NH2 (amino functional group)
-COOH (carboxyl functional group)
-distinctive R-group - 3How do amino acids act in water-amino acid acts as base
attracts proton to form NH3+
-Carboxyl group acts as acid
loses H to become COO-
helps amino acid stay in solution and become more reactive - 4Non-ionized form of amino acid
- 5Ionized form of amino Acid
- 6polymerizationcondensation reaction/dehydration synthesis
reverse- hydrolysis - 7peptide bondwhen a carboxyl group of 1 amino acid reacts with the amino acid of the second
- 8oligopeptidespolypeptides containing fewer than 50 amino acids
- 9proteinspolypeptides containing more than 50 amino acids
- 103 key characteristics within a polypeptide1) R-Group orientation:
-side chains can interact with each other or with water
2)Directionality:
-free amino group (NH3) on left called N-terminus
-free carboxyl group (COOH) on right called C-terminus
3)Flexibility
-single bonds on either side of the peptide bond can rotate, making the entire structure flexible - 11Catalysis proteinsenzymes speed up chemical reactions
- 12defense proteinsantibodies and complement proteins attack pathogens
- 13movement proteinsmotor and contractile proteins move the cell or molecules within the cell
- 14signalingproteins convey signals between cells
- 15structurestructural proteins define cell shape and comprise body structures
- 16transportcarry materials
- 17membrane proteinscontrol molecular movement into and out of the cell
- 18primary structure of proteinsa unique sequence of amino acids
each protein has a unique shape - 19secondary structure of proteinsformed by hydrogen bonds between the carbonyl group of one amino acid and the amino group of the other
- 20secondary structure shapes and how they are formeda polypeptide must bend to allow hydrogen bonding forming:
alpha helices
and beta pleated sheets
depends on the primary structure
large number of hydrogen bonds increases stability - 21Tertiary structure of proteinsresults from interactions between R-groups or between R-groups and peptide backbone
cause 3D bending and folding - 22interactions that form tertiary structure of proteins-Hydrogen bonds
-Hydrophobic interactions
-Van der waals interactions
-covalent disulfide bonds
-ionic bonds - 23Hydrogen bonds in tertiary structure of proteinsform between hydrogen atoms and the carbonyl group in the peptide bonded backbone
and between hydrogen and negatively charged atoms in side chains - 24hydrophobic interactions in tertiary structure of proteinswithin a protein increase stability of surrounding water molecules by increasing hydrogen bonding
- 25Van der waals interactions in tertiary structure of proteinsweak electrical interactions between hydrophobic side chains
- 26covalent disulfide bonds in tertiary structure of proteinsforms between sulfur-containing R-groups
- 27Ionic bonds in tertiary structure of proteinsform between groups that have full and opposing charges
- 28quaternary structurecombination of polypeptides
- 29macromolecular machinesgroups of multiple proteins that assemble to carry out a particular function
- 30denatured proteinunfolded protein that is unable to function normally
- 31molecular chaperoneshelp proteins fold correctly into cells
- 32prionsimproperly folded forms of normal proteins that are present in healthy individuals
-amino acid sequence= same
shape= different
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- Biology (Amino Acids) Flashcards on amino acids, created by Katlin DiPietro on 10/02/2017.
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- Katlin DiPietro
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