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73 Cards in this Set
- Front
- Back
Classification of Proteins according to composition |
Simple Conjugated Derived |
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Classification of Proteins according to Solubility |
Fibrous Globular |
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Classification of Proteins according to function |
Enzymes Structural Defense Transport and Storage Regulatory and Receptor Muscle contraction and Mobility |
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Composition of protein defined as naturally occurring |
Simple |
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Composition of protein that is linked with nonprotein groups |
Conjugated |
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Derivatives of proteins resulting from the action of enzymes, heat or chemical reagents |
Derived proteins |
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Consists of peptide chains compactly folded or coiled |
Globular |
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Consists of long peptide chains or groups of such chains; coiled in spiral or helix formation |
Fibrous |
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Fibrous proteins are cross linked by _________. |
Disulfide bonds and H bonds |
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Linear sequence of amino acids; determines its 3D structure and its properties |
Primary structure |
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Arrangement in the space of the atoms in the peptide backbone; arrangement of polypeptide chain into an organized structure |
Secondary structure |
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Secondary structure is stabilized by ______ between peptide. |
H bonding |
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Secondary structure bonds: |
Alpha helix Beta pleated sheet |
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Coil direction; L-Amino Acid favor the right hand coil |
Alpha helix |
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Alpha helix H bonds occur between ___ O of backbone C=O to ___ H atom of backbone NH. |
1st ; 13th |
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peptide backbone is almost completely extended |
Beta pleated sheet |
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Two adjacent peptides |
Parallel Antiparallel |
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More common adjacent peptide and is rich in Alanine and Glycine (silk fiber and spider web) |
Antiparallel |
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Clusters held together by non-covalent interactions; combinations of secondary structure |
Supersecondary structures or Structural motifs |
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Repetitive secondary structure |
Motifs |
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Combination of several motifs of secondary structures into a compact arrangement; 3D arrangement; noncovalent forces |
Tertiary structure |
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Association of 2 or more polypeptide chains that may be identical or different to form a multi-subunit protein molecule |
Quaternary structure |
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2 or more polypeptide chains |
Oligomeric |
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Almost identical subunits |
Homotypic |
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Different subunits |
Heterotypic |
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Occurs after translation in the presence of molecular chaperones |
Protein folding chaperones |
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Facilitates the protein folding |
Chaperones |
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Prevent aggregation of heat-denatured proteins or polypeptides |
Heat shock proteins |
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Proteins responsible for structural support; H2O insoluble; examples are collagen, elastin, keratin |
Fibrous proteins |
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Proteins responsible for transport; H2O soluble; examples enzymes, antibodies, hormones |
Globular proteins |
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Proteins are highly expressed when cells are exposed to _______ temperature. |
Increased |
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when a protein shape changes and goes back to primary structure because of high temperature |
Protein denaturation |
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Newly found amino acids found in bacteria |
Selenocysteine Pyrrolysine |
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Peptide bond via ________ |
Condensation reaction |
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Polymers of amino acids |
Peptides and proteins |
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A protein which assumes many forms; causative agent of mad cow disease |
Prion |
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Biopolymers constructed from monomeric units knows as amino acids |
Proteins |
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Proteins needed in diet because the body cannot synthesize them |
Essential proteins |
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Proteins needed by the body but can be manufactured or synthesized by the body |
Non-essential amino acids |
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<100 amino acids |
Peptides |
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> or = to 100 amino acids |
Proteins |
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Charged/polar R-groups generally _____________ on soluble proteins |
Map to surfaces |
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Nonpolar R-groups tend to be ___________ in the cores of soluble proteins. |
Buried |
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Membrane proteins have adapted to __________ environments. |
Hydrophobic |
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Misfolded proteins problems: |
Protein aggregation Could lead to Alzheimer's disease |
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The _______ of amino acids determines its distinct chemical and biological properties. |
Side chain / R group |
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The only amino acid that is not chiral. |
Glycine |
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Nonpolar side chains |
MF RIP LWV |
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Neutral Polar side chains |
QT CYS N |
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Most amino acids prefer the __ configuration. |
L |
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For higher levels of protein structure, they are determined using __________ techniques. While for primary structure, use __________ methods. |
Instrumental ; Chemical |
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Before protein sequencing, it is necessary to remove first the ________ bonds. |
Disulfide |
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Sanger technique uses ____________ which reacts with the N terminal residue under alkaline conditions. |
2, 4 dinitrofluorobenzene |
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Edman technique uses _______________ which derivatizes the N terminal amino acid residue but still leaves the rest of the chain sequence intact. |
Phenylisothiocyanate |
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Trypsin cleaves at |
Lys Arg |
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Pepsin cleaves at |
W FLY |
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Chymotrypsin cleaves at |
F Y W |
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Carboxypeptidase cleaves from __ terminus while aminopeptidase cleaves from __ terminus. |
C ; N |
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Protein isolation based on charge |
Ion exhange chromatography |
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Protein isolation based on molecular size |
Gel filtration chromatography |
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Protein isolation based on selective binding to a specific molecule; use of antigen and antibodies |
Affinity chromatography |
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Protein isolation based on charge and molecular size |
Gel electrophoresis |
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Protein isolation based on isoelectric point of the protein; done in serum samples |
Chemical precipitation |
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Used as support medium for low molecular weight biochemicals such as amino acid and carbohydrates |
Polyacrylamide |
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Used as support medium for large molecules like nucleic acids and proteins |
Agarose |
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The larger the protein, the more of the ______ it absorbs. |
Anion |
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Used to completely denatures protein in protein gel electrophoresis method |
Sodium Dodecyl Sulfate (SDS) |
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In chemical precipitation, ______ tend to precipitate, leaving _______ in the solution. |
Globulin ; albumin |
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An ion exhange chromatography that begins at a basic pH; net negative charge |
Anion exhange |
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An ion exhange chromatography that begins at an acid pH; positive charge adhering to negative charge |
Cation exhange |
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Add _____ to make negative to positive |
Acid |
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Proteins with more negative charge move ______ |
Faster |
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If proteins contain more than ___ polypeptide chain, chains are separated and purified. |
One |