Human Anatomy & Physiology (11th Edition)
11th Edition
ISBN: 9780134580999
Author: Elaine N. Marieb, Katja N. Hoehn
Publisher: PEARSON
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Discuss the general structure of the carrier proteins within our cells. Describe how their
structure allows function.
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- Identify a disease or condition related to protein mis-folding. Which protein is misfolded? Is this a genetically inherited condition or is it transmissible?arrow_forwardAn intermediate folding stage seen in protein denaturation or renaturation is called : a) domain b) motif c) subunit d) molten globule Proteins which do not renature spontaneously when denaturation conditions are removed may need the assistance of: a) a prosthetic group b) a higher salt concentration c) a lower temperature d) a chaperone protein The information needed for correct protein folding is encoded in: a) the surrounding molecules b) the protein’s amino acid sequence c) the pH of the aqueous medium d) the electrolyte composition of the aqueous solutionarrow_forwardIn your own wordsarrow_forward
- Amino acids at the interaction site ( F,I and L) and its G protein partner (P, L, Y) are very conserved.If the amino acids are swapped between the protein and GPCR is binding expected to be as tight?arrow_forwardThe activity provides you with a version of the NGF pathway, an example of a RTK. All of the proteins involved can be in ON/OFF states. Using this cell signaling pathway you will be asked a variety of questions to determine how the molecules are regulated, but also how a cell would respond if this cell signaling party steps were interrupted or activated. Neural Growth Factir (NGF) Ras- Ras- GDP GTP Trk-A Ras-GEF braf braf МЕК МЕК ERK ERK ERK ERK STAT STAT Spiouty DNA Nucleus Cytosolarrow_forwardThe primary function of chaperones is to ... Select an answer and submit. For keyboard navigation, use the up/down arrow keys to select an answer. a b C transport proteins from one cellular location to another. help proteins fold into their final conformation by binding to exposed hydrophilic regions. help proteins fold into their final conformation by binding to exposed hydrophobic regions. help proteins fold into their final conformation by binding to exposed basic and acidic regions.arrow_forward
- Non covalent bonds are very important in cell biology, could you explain why and provide an example that illustrates their importance ( do not chose protein folding as an example) What are the different levels of protein structure and what are the different parameters (sequence, type of bonds, etc...) that influence protein folding at these different levels?arrow_forwardFarnesylation of ras allows it to: a.) be tethered to the plasma membrane. b.) be an integral membrane protein c.) be a soluble protein d.) reveal a nuclear localization signalarrow_forward2.) Below is a diagram of two models of protein sorting mechanisms. After analyzing the two models, how would you distinguish between these two models? Write down all your answers.| (A) VESICLE TRANSPORT MODEL (B) CISTERNAL MATURATION MODEL cisternae vesicular tubular cluster CGN ER cis medial trans TGNarrow_forward
- You are investigating a lysosomal storage disease and you discover that newly synthesized lysosome hydrolases (proteins that should be sent to the lysosome) are secreted from the cells rather than being delivered to the lysosomes (where they should normally be located). What is the most likely explanation for this finding? (Hint: what might be different about the proteins that would cause them to not end up in the correct location?)arrow_forwardPlease fill in the following blanks with the options that correctly finishes the sentence. a. At a low O₂ pressure the [Select] hemoglobin is in a [Select] [Select] [Select] 9 [Select] " bond with [Select] heme, and the protein's central channel is [Select] b. The proximal histidine forms a(n) [Select] state is stabilized. In this conformation state, the heme prosthetic groups is each subunit's heme is more likely to be the proximal histidine is [Select ] bond with while the distal histidine forms a(n) [Select] to thearrow_forwardA. What change should disrupt the interaction between proteins 1 and 2 the most? Why? B. What change would disrupt the interaction between proteins 1 and 2 the least? Why?arrow_forward
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