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Cell Bio MU
Chapter 2
| Question | Answer |
|---|---|
| Covalent bonds pg. 33 | Pairs of electrons are shared btw pairs of atoms |
| Electronegative atom pg. 34 | An atom's attractive force; nitrogen and oxygen are strongly negative |
| Polar pg. 34 | Molecules, such as water, that have an asymmetric distribution of charge (of dipole) |
| Nonpolar pg. 34 | Molecules that lack electronegative atoms and strongly polarized bonds, such at molecules that consist entirely of carbon and hydrogen atoms |
| Ions pg. 34 | An atom or molecule with a net electric charge due to the loss or gain of one or more electrons |
| Anion pg. 34 | Negatively charged ion (extra electrons) |
| Cation pg. 34 | Positively charged ion (fewer electrons than normal) |
| Noncovalent bonds pg. 34 | Do not depend on shared electrons but rather on attractive forces between atoms having an opposite charge |
| Free radicals pg. 35 | Atoms or molecules that have orbitals containing a single unpaired electron tend to be highly unstable (free radicals) |
| Ionic bond (or a salt bridge) pg. 35 | A crystal of table salt is held together by an electrostatic attraction btw positively charge Na+ and negatively charged Cl- ions; usually a metal and nonmetal |
| Hydrogen bond pg. 36 | When hydrogen atom is covalently bonded to an electronegative atom, the single pair of shared electrons is greatly displaced toward the nucleus of the electronegative atom, leaving the hydrogen atom with a partial positive charge; attracts to a (-) charge |
| Hydrophilic pg. 36 | ("water loving"); ex. sugars and amino acids |
| Hydrophobic pg. 36 | ("water fearing"); ex. steroid or fat molecules |
| Hydrophobic interaction pg. 37 | The association of nonpolar molecules; ex. droplets of fat in soup reappearing instantly even after it's been mixed |
| Van der Waals force pg. 37 | A weak attractive force btw two molecules with transitory dipoles are very close to one another and oriented in the appropriate manner |
| Acid pg. 39 | A molecule that is capable of releasing (donating) a hydrogen ion |
| Base pg. 39 | Any molecule that is capable of accepting a proton |
| pH pg. 39 | Measurement of concentration of hydrogen ions |
| Buffers pg. 40 | Compounds that react with free hydrogen or hydroxyle ions, thereby resisting changes in pH |
| Biochemicals pg. 40 | The compounds produced by living organisms |
| Functional Groups pg. 41 | Particular groupings of atoms that often behave as a unit and give organic molecules their physical properties, chemical reactivity, and solubility in aqueous solution |
| Ester bonds pg. 41 | One of the two most common linkages btw functional groups; form btw carboxylic acids and alcohols |
| Amide bonds pg. 41 | One of the two most common linkages btw functional groups; form btw carboxylic acids and amines |
| 1st...A classification of biological molecules by function | Macromolecules: the molecules that form the structure and carry out the activities of cells are huge, highly organized molecules; contain anywhere form dozens to millions of carbon atoms |
| 2nd..."" | The building blocks of macromolecules: most cells contain a supply (pool) of low-molecular-weight precursors that are ready to be incorporated into macromolecules; sugars-polysaccharides, amino acids-proteins; nucleotides-nucleic acids; fatty acids-lipids |
| 3rd..."" | Metabolic intermediates (metabolites): metabolic pathways- each series of chemical reactions; metabolic intermediates- the compounds formed along the pathways leading to the end products that have no function per se |
| 4th..."" | Molecules of miscellaneous function: include vitamins, function primarily as adjuncts to proteins; certain steroid or amino acid hormones; molecules involved in energy storage (ATP); regulatory molecules (cyclic AMP); and metabolic waste products (urea) |
| Carbohydrates (or glycans) pg. 43 | Include simple sugars (or monosaccharides) and all larger molecules constructed of sugar building blocks; function primarily as stores of chemical energy and as durable building materials for biological construction |
| Glycosidic bonds pg. 44 | Sugars join together via this covalent bond to form larger molecules; form by reaction btw carbon atom C1 of one sugar and the hydroxyl group of another sugar, generating a --C--O--C- linkage btw the two sugars |
| Oligosaccharides pg. 45 (oligo = few) | Small chains of sugars; often found covalently attached to lipids and protein, converting them into glycolipids and glycoproteins, respectively |
| Glycogen pg. 45 | Insoluble polymer of glucose; stored glucose; transforms into glucose when the body needs sugar |
| Polysaccharide pg. 45 | A polymer of sugar units joined by glycosidic bonds; glycogen is a type of polysaccharide |
| Starch pg. 46 | Surplus chemical energy in plants, similar to glycogen in that it is a polymer of glucose |
| Cellulose pg. 47 | Major component of plant cell walls; cotton and linen consist largely of cellulose; form tough, durable structural materials |
| Glycosaminoglycans (or GAGa) pg. 47 | Group of polysaccharides that has a more complex structure; have the structure --A--B--A--B--, where A and B represent two different sugars; best-studied is heparin, which is secreted by cells in the lungs and other tissues in response to tissue injury; |
| Fats pg. 47 | Consist of a glycerol molecule linked by ester bonds to three fatty acids |
| Triacylglycerol pg. 47 | The composite molecule of fats |
| Fatty acids pg. 47 | Long, unbranched hydrocarbon chains with a single carboxyl group at one end |
| Amphipathic pg. 47 | Molecules having both hydrophobic and hydrophilic regions; such molecules have unusual and biologically important properties |
| Saturated pg. 48 | Fatty acids that lack double bonds, such as stearic acid |
| Unsaturated pg. 48 | Fatty acids that have double bonds, ; naturally occurring fatty acids have double bonds in the cis configuration |
| Oils pg. 48 | Fats that are liquid at room temperature |
| Specificity pg. 50 | Proteins have shapes and surfaces that allow them to interact selectively with other molecules; they exhibit a high degree of specificity |
| Polypeptide chain pg. 50 | During the process of protein synthesis, each amino acid becomes joined to two other amino acids, forming a long, continuous, unbranched polymer (polypeptide chain) |
| Peptide bonds pg. 51 | Result from the linkage of the carboxyl group of one amino acid to the amino group of its neighbor, with the elimination of a molecule of water; the amino acids that make up polypeptide chains are joined with this bond |
| Side chain or R group pg. 51 | Bonded to the (alpha sign)-carbon,; highly variable among the 20 building blocks, and it is this variability that ultimately gives proteins their diverse structures and activities |
| Two of the four categories of amino acids (classified on the character of their side chains) pg. 51 | 1) Polar charged: aspartic acid, glutamic acid, lysine, and arginine; 2) Polar, uncharged: asparagine, glutamine (the amides of aspartic acid and glutamic acid), threonine, serine, tyrosine |
| Cont. other two ... | 3)Nonpolar: alanine, valine, leucine, isoleucine, tryptophan, phenylalanine, methionine 4) The other three amino acids: glycine, proline, cysteine |
| Disulfide (-SS-) bridge pg. 53 | Often form between 2 cysteines distant from one another in the polypeptide backbone or 2 separate polypeptides; help stabilize the intricate shapes of proteins, esspec. those outside cells where they're subjected to more physical and chemical stress |
| Posttranslational modifications (PTMs) pg. 54 | Not all amino acids described are found in all proteins, nor are the various amino acids distributed in an equivalent manner. |
| Cont. ... | A # of the other amino acids are also found in proteins, but arise by alterations to the side chains of the 20 basic amino acids after their incorporation into a polypeptide chian |
| Conformation pg. 55 | Refers to the three-D arrangement of the atoms of a molecule, that is, to their spatial organization |
| Alpha helix pg. 55 | One of the two conformations proposed. The backbone of the polypeptide assumed the form of a cylindrical, twisting spiral |
| Beta-pleated sheet pg. 56 | One of the two conformations proposed by Pauling and Corey; consists of several segments of a polypeptide lying side by side |
| X-ray crystallography pg. 57 | Usually determines the detailed tertiary structure of a protein |
| Fibrous proteins, Globular proteins pg. 58 | Most proteins can be categorized on the basis of their overall conformation as being either fibrous proteins, which have an elongated shape, or globular proteins, which have a compact shape |
| Domains pg. 59 | Most proteins can be categorized on the basis of their overall conformation as being either fibrous proteins, which have an elongated shape, or globular proteins, which have a compact shape |
| Conformational changes pg. 60 | Predictable (nonrandom) movements within a protein that are triggered by the binding of a specific molecule; typically involve the coordinated movements of various parts of the molecule |
| Subunit pg. 60 | Many proteins such as myoglobin are composed of only one polypeptide chain, most are made up of more than one chain (subunit) |
| Quaternary structure pg. 60 | Name of the structure of proteins composed of subunits |
| Multiprotein complex pg. 61 | When different proteins, each with a specific function, become physically associated |
| Denaturation pg. 63 | The unfolding or disorganization of a protein |
| Native pg. 64 | Correctly folded molecules |
| Self-assembly pg. 64 | The linear sequence of amino acids contained all of the information required for the formation of the polypeptide's three-D conformation; Ribonuclease, in other words, is capable of self-assembly |
| Molecular chaperones pg. 65 | "Helper proteins"; several families of proteins whose function is to help unfolded or misfolded proteins achieve their proper three-D conformation |
| Isoforms pg. 76 | Different versions of a protein; adapt to function in different tissues or at different stages of development |
| Families (or superfamilies) pg. 77 | Most proteins are members of a much larger family |
| Strands pg. 77 | Long chains of monomers |
| Nucleotides | Nucleic acids (which are made of macromolecules, which are made of a long chain(strand) of monomers) |
| DNA (deoxyribonucleic acid) pg. 77 | One type of nucleic acid found in living organisms; serves as the genetic material of all cellular organisms, though RNA carries out that role in many viruses; info stored in DNA is used to govern cellular activities through the formation of RNA messages |
| RNA (ribonucleic acid) pg. 77 | Carries out the DNA role for many viruses |
| Pyrimidines pg. 78 | Smaller molecules consisting of a single ring |
| Purines pg. 78 | Larger molecules consisting of two rings |
| Adenine and Guanine pg. 78 | RNAs contain these two different purines |
| Cytosine and Uracil pg. 78 | RNAs contain these two different pyrimidines |
| Thymine pg. 78 | In DNA, uracil is replaced with thymine, a pyrimidine with an extra methyl group attached to the ring |
| Ribozymes pg. 78 | RNA's having a catalytic role are called RNA enzymes |
| Adenosine triphosphate (ATP) pg. 79 | A nucleotide used to derive the energy being put to use at any given moment in any living organism |
| Guanosine triphosphate (GTP) pg. 79 | A nucleotide of enormous importance in cellular activities; binds to a variety of proteins (called G proteins) and acts as a switch to turn on their activities |
| Molecular Chaperones pg. 81 | Hsp70 and related molecules-- bc of their role in assisting the assembly of proteins by preventing undesirable interactions |
Created by:
Briawna
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