Term
Carboxylic Groups of Amino Acids are ______ than Simple Organic Acids |
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Definition
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Amino group of amino acids are ______ bases than most simple amines |
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Definition
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Definition
The dipolar ionic form of amino acids. Any molecule that contains a mixture of positive and negative charges |
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pH less than or equal to 1 |
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Definition
a.a. is in cationic form- move towards cathode |
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Term
pH = to pKa of carboxyl group |
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Definition
a.a. exists in 50:50 mixture of cationic and zwitter ionic forms |
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Definition
a.a. exists in 50:50 mixture of anionic and zwitter ionic form |
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pH greater than or equal to 12 |
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Definition
anionic form is predominant- migrate toward anode |
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Term
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Definition
solution pH at which the opposite charges exactly balance one another |
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Term
Hydrophobic (Nonpolar) A.A. |
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Definition
Gly, Ala, Val, Leu, Ile, Pro, Met, Phe, Trp |
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Trp has properties somewhere between |
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Definition
nonpolar and polar but not charged a.a. |
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Term
Gly has properties somewhere between |
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Definition
nonpolar and polar but not charged a.a. |
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Term
Polar But Not Charged A.A. |
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Definition
Cys, Tyr, Thr, Ser, Gln, Asn |
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Term
Cys can't form _____ but has a _____ dipole |
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Definition
hydrogen bonds, permanent |
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Term
Cys and Tyr have _____ acid/base properties in vitro and therefore are always in the _____________ form |
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Definition
weak; protonated, uncharged |
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Definition
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A.A with negatively charged side chains (Acidic) |
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Definition
Asp, Glu. Carboxyl side chain is always ionized |
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A.A. with positively charged side chains (Basic) |
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Definition
Lys, His, Arg. the imidazole side chain of His is the only side chain that has buffering properties at physiological pH |
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Term
____ configuration is the primary isomer that exists in nature and is used by living cells |
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Definition
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Term
Some bacteria and fungi use __ configuration a.a. |
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Definition
D. However, often toxic to other living organisms |
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Term
Calculation of Isoelectric Point |
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Definition
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Definition
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Side chains of a.a. project ____ from the back bone of the molecule |
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Definition
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Bond between a.a. in a protein |
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Definition
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Definition
has no acid or base properties, but very polar. has two resonance forms. Partial double bond characters: results in restricting the rotation around canon-nitrogen bond; limits number of conformations and places the six atoms of the peptide bond in the same plane |
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Term
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Definition
molecule containing two a.a. joined by a single peptide bond |
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Definition
3 a.a. held together by 2 peptide bonds |
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Definition
4 a.a. held together by 3 peptide bonds |
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Term
In general, Peptides contain ____ or fewer a.a. residues |
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Definition
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Definition
between 12 and 20 a.a. exist in numerous random shapes |
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Term
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Definition
greater than 20 a.a. fold into a single stable low energy conformation |
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Definition
often used with polypeptide interchangeably, however protein is reserved for molecules that when correctly folded perform some cellular function |
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Definition
Single correctly folded polypeptide chain |
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Definition
Supramolecular complexes composed of two or more polypeptide chains |
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Term
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Definition
composed of two or more polypeptides with the same sequence of a.a. |
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Term
Heteromultimeric Proteins |
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Definition
composed of several different polypeptides |
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Term
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Definition
Individual polypeptide chains that comprise a multimeric protein |
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Term
Amino Terminus/ N-Terminus |
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Definition
end of the molecule that contains a free amino group: not involved in the formation of a peptide bond |
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Term
Carboxy Terminus/Carboxyl Terminus/C-Terminus |
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Definition
opposite end of N-Terminus, free carboxyl group |
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Term
When naming sequence of proven the _____ is always the left most a.a. |
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Definition
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Definition
N-Terminus and side chains of basic a.a. carry positive charge and C-Terminus and side chains of acidic a.a. carry a negative charge |
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Term
Solution pH less than pI of protein |
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Definition
protein has a net positive charge |
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Term
Solution pH is greater than pI of molecule |
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Definition
protein has a net negative charge |
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Definition
biological catalysts of chemical rxns that occur within the cell |
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Term
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Definition
regulate activities of the cell and ability of other proteins to carry out their cellular function Ex: Peptide and protein hormones, Allosteric Enzymes (control key cellular rxns), gene inducers (stimulate gene expression), gene repressors (inhibit gene expression). |
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Definition
carry specific substances from one place to another. Ex: membrane transporters (carry polar molecules across cell membranes), Hemoglobin, Serum Albumin (carries a wide variety of drugs and metabolites through out the body). |
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Definition
Reservoir of an essential nutrient. Ex: Myoglobin (stores oxygen in skeletal muscle tissue), Ferritin (stores iron in liver and bone marrow), Ovalbumin (storage depot of a.a. for developing birds), Casein (major protein in mammalian milk stores a.a. for growing infants) |
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Definition
provide strength, support, and form to cells, tissues, and organisms. Ex: Collagen (major protein of bone, tendons, and cartilage) Alpha-Keratin (skin, hair, horns, hooves, and fingernails), Beta-Keratin (skin), Tubulin, actin, and spectrin (make up cytoskeleton). |
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Contractile & Motile Proteins |
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Definition
Provide cell/organism with motion. Ex: Actin and Myosin of muscle cells and Tubulin of cilia and flagella. Dynein and Kinesin drive movement of vesicles and organelles along cytoskeletal tracks within the cell. |
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Definition
act as bridges by binding to and localizing specific proteins to specific sites within the cell. Site upon which supramolecular complexes are formed. |
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Definition
play an active role in cell defense or in defense of organism. Ex: Antibodies, Hemostasis Cascade (protects organism from excessive blood loss) Toxins, Keratins of skin. |
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Definition
act as bridges by binding to and localizing specific proteins to specific sites within the cell. Site upon which supramolecular complexes are formed. |
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Definition
Endow organism with capacity to survive abiotic stresses. Ex: Cytochrome P450 (important factor in biological detoxification of xenobiotics). Metallothionein (cysteine rich protein that functions by binding and sequestering toxic heavy metals). Heat Shock Proteins "Hsp" (aid in refolding of proteins damaged by heat or signal for their destruction if too severely damaged). |
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Definition
display functions that do not fit under other classifications. Ex: Glue Protein secreted by mussels |
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