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NWHSU Biochem 1 T1

NWHSU Biochem 1 Clicker questions for Test 1 not incl Quiz 1 Q's

QuestionAnswer
The three-dimensinal structure of macromolecules is formed and maintained primarily through noncovalent interactions. Which one of the following is NOT considered a weak interaction? A. carbon-carbon bonds B.hydrogen bonds C.hydrophobic D.ionic E.VanderW carbon-carbon bonds
is/are covalent stabilizing force (s) in the tertiary/quaternary structure of many proteins. A.Hydrogen bonding B.Disulfide bonds C.Hydrophobic interactions D.Ionic interactions E.Van der Waals interactions Disulfide bonds
The main stabilizing force in Beta sheets is A.ionic bonding B.hydrophobic interaction C.hydrogen-bonding D.Van der Waals interaction Hydrogen-bonding
The main stabilizing force in Alpha Helix's is A.ionic bonding B.hydrophobic interaction C.hydrogen-bonding D.Van der Waals interaction Hydrogen-bonding
What is the first enzymatic modification in Collagen Biosynthesis? Hydroxylation (attachment of OH)
What does Hydroxylation attach to protein chain? OH Group is substituted for H (Hydroxylation is dependent on Vitamin C)
What amino acid is atypical for proteins but collagen's ribosomes use regularly to assemble collagen? Proline (most common sequence of collagen are Glycine-Proline-X, and Glycine-X-Hydroxyproline)
What hydroxylated amino acids are necessary for cross-linking of the triple helices to form triple helix structure? Hydroxylation transforms relative amino acids to Hydroxyproline and Hydroxylysine
What is the second enzymatic modification in Collagen Biosynthesis? Glycosylation (attachment of carbohydrates at the OH site)
What is the third enzymatic modification in Collagen Biosynthesis (which takes place in the Golgi Apparatus)? Formation of Disulfide bonds in triple helix formed by three Proline Alpha chains
When biosynthesizing collagen, what is released in to the extracellular space via a Golgi Vesicle? Procollagen
What is the fourth enzymatic modification in Collagen Biosynthesis (which takes place in the extracellular space)? removal of C and N terminal sequences
Besides Disulfide bonds, what are some additional stabilizing force (s) in the tertiary/quaternary structure of many proteins. A.Hydrogen bonding B.Covalent bonds C.Hydrophobic interactions D.Ionic interactions E.Van der Waals interactions Hydrogen bonding
The vitamin C-dependent modification step in collagen synthesis is A.translation B.hydroxylation C.glycosylation D.cystine formation E.cleaving of C-termini Hydroxylation
The cleaving of the N- and C-terminal sequences to form tropocollagen occurs in the 1.Endoplasmic Reticulum 2.Cytoplasm 3.Golgi Vesicles 5.extracellular space extracellular space
Hemoglobin is mainly located in A.muscle tissue B. the lungs C.white blood cells D.red blood cells E.the serum red blood cells
What amino acid allows for tight winding of the Collagen's triple helix structure A.Tryptophan B. Valine C. Proline D.Glycine Glycine
Myoglobin is mainly located in A.muscle tissue B.the lungs C.white blood cells D.red blood cells E.the serum muscle tissue (Myoglobin stores Oxygen in tissue)
is a prosthetic group of hemoglobin. A.Histidine B.Heme C.CO D.O2 E.Myoglobin Heme
A ligand is A. bound non specifically by its protein B. a chemical species that is reversibly bound to its protein C. always covalently bound to its protein D. always a polypeptide E. always of a complex molecular structure a chemical species that is reversibly bound to its protein
Binding of a ligand leading to a change of affinity at another binding site of the protein, changing the conformation of polypeptide conformation; is called what? allosteric effect
The heme prosthetic group of hemoglobin consists of a pyrrol-ring system with ____bound in its center. A. Fe2+ B. Fe3+ C. NO D. CO E. nothing Fe2+
____is a ligand of hemoglobin. A. Fe2+ B. Heme C. Porphyrine D. O2 E. Myoglobin O2
What allosteric effector increases the sigmoid effect on hemoglobin's affinity for oxygen? BPG (=DPG, 2,3-di or bisphosphoglycerate
High altitude or Low oxygen for hours (12-24)will encourage ? in red blood cells to bind to the effector sites, reduce hemoglobin's affinity for oxygen, releasing oxygen to tissues over days (1-2 days), and increases red blood cell count over weeks (3=+) BPG
With the Bohr effect, as PH goes up, oxygen affinity goes ? up
C6H12O6 (glucose) + 6O2 = 6H2O + ? into solution, (respiration and PH) 6CO2 (six carbon dioxides)
What stabilizes the PH in blood? 1. Buffers inside blood and serum 2. 30% of CO2 carried by Hb 3. 10% carried to lungs as is
CO2 up in tissues but down in lungs, in tissues PH goes ?, Oxygen affinity goes ? down, down
What is different about Fetal Hemoglobin? No binding site for BPG because the amino acid sequence is slightly different (w/in 120 days HbFetal substitutes out for HbAdult)
Myoglobin shows a(n) ______binding curve. A. Linear B. Hyperbolic C. Exponential D. Sigmoid Hyperbolic
BPG plays a role in adaptation of the human body to lower p)2 at higher altitudes by A.lowering the partial pressure of O2 in the tissue B.competitively binding to the heme-Fe2+ C.allosteric D.converting Fe2+ to Fe3+ allosteric, binding to an allosteric binding site on the hemoglobin and lowering hemoglobin's affinity for O2
Fe2+ is protected from ____by surrounding nitrogen atoms in the pyrrole ring structure of heme and a nitrogen atom of a histidine.A. deprotonation B. chelation C. oxidation D. reduction E. protonation oxidation
The mutation behind sickle cell anemia leads to the replacement of ___by _____in subunity Beta. which combination? hydrophilic/phobic glu; hydrophilic/phobic val hydrophilic glu; hydrophobic val
Created by: AnatomyMash