Term
| ? mutation : Amino Acid #1 changed to similar amino acid #2 Ex Leucine to Isoleucine (both are hydrophobic |
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| ?-? mutation is an amino acid #1 changed to a dissimilar amino acid. Example Glu to Val |
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| ? mutation: Change nucleotide but not amino acid. |
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| The ? ? ? character of peptide bonds results in polypeptide chains that are "flexible but conformationally restricted" |
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Term
| Most amino acid residues adopt the ? configuration. ? residue is an exception |
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Term
| Bonds flanking alpha-carbons in polypeptides have angles that can vary from ? to ? |
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Term
| Due to freedom of rotation about N-C(alpha) and C(alpha)-C' bonds,? different conformations possible for a polypeptide chain |
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| ? and ? angles determine the path of the polypeptide chain in three dimension space |
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Term
# of conformations not infinite, some forbidden due to ? ?.
A ? ? displays the allowed set of angles. |
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Definition
steric clashes
Ramachandran plot |
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Term
| 10 Amino acids would be how many angstroms long? |
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Term
| Side chains of an alpha helix ? ? from the helix axis |
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Term
| When one side of helix has hydrophobic side chains and the other has hydrophilic, helix is called ? |
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Term
| What has more extended structures than an alpha helix? |
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Term
| How many residues per strand on beta strand? |
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Term
| What is the pitch for beta strand? |
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Term
| In ?, side chains project above and below plane of sheet. |
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Term
| What is the reason that silk is very strong and flexible but not stretchable? |
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Definition
| The beta sheets are already stretched pretty far |
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Term
| Nearly 1/3 of residues in globular proteins are involved in ? ? |
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Term
| The most common reverse turn is the ? |
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Term
| In a reverse turn the 1st residue HYDROGEN BONDS to the ? |
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Term
| ? and ? are common in beta-turns but tend to disrupt alpha helix |
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Term
| How many residues are required to complete a turn |
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Term
| Loops are located on ? of protein; participate in interactions with other molecules |
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Term
| ? do not have regular, periodic structure. Still often well defined structurally |
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Term
| ? comprise "supersecondary" structures that are intermediate between secondary and tertiary structures |
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Term
| Examples of motifs include ?-?-?, zinc finger, 4-helix bundle |
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Term
| Nuclear Magnetic Resonance (NMR) spectroscopy can determine structure of protein in ? |
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Term
| What is a feature of some transcription factor proteins that bind DNA and direct transcription |
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Term
| Helix-loop-helix contains helix having side chains that form base - specific, ?-? contacts with target DNA |
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Term
| The zinc finger DNA binding motif is only about ? resides long |
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Term
| What uses side chains of two His and two Cys residues to coordinate Zn2+ ion (which stabilizes structure |
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Term
| Zinc finger and ? ? DNA binding motif are commonly found in transcription factors |
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Term
| Zinc finger binds into major groove of ?-? double helix |
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Term
| Zinc finger occurs via ?-?, salt bridges, and hydrophobic interactions. Particular side chains make BASE-SPECIFIC contacts |
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Term
| The ?-? ? is a common tertiary fold in both water soluble and membrane bound proteins. |
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| Hydrophobic packing stabilizes what structure? The electron transport chain protein cytochrome b-562 also folds into this |
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Term
| The ? ?: myoglobin and hemoglobin (alpha-domain proteins) has 8 alpha helices for Mb ( 7 for Hb alpha; 8 for beta) form this unique structure |
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Term
| In the globin fold the noncovalently attached heme is embedded in a ? ? |
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Term
| Heme consists of ? ? ? plus Fe++ |
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Term
| Triosephosphate isomerase (TIM) and other glycolytic enzymes (aldolase, enolase, pyruvate kinase) have domains that fold into this structure |
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Definition
| alpha/beta or TIM barrel fold ( an alpha/beta domain protein) |
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Term
| What is an elaborate closed barrel structure that contains alternating segments of alpha-helices and beta-strands? |
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Definition
| The alpha/beta or TIM barrel fold |
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Term
| ? is the plasma carrier for retinol its metabolite binding unit has an elaborate cage-like structure, an UP-AND-DOWN Beta-BARREL. |
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Definition
| RBP (Retinol Binding Protein) |
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