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Cell Metabolism 3
Cell Metabolism Lecture 3- Proteins: Composition and Structure
| Question | Answer |
|---|---|
| Compensatory Respiratory Alkalosis | how the blood helps maintain its pH through respiration |
| Structural Functions of Proteins | -Matrix for bone -Connective tissue -Collagen and elastin |
| Dynamic Functions of Proteins | -Catalysis of metabolic rxns via enzymes -Transport: hemoglobin/myoglobin for oxygen -Myosin and Actin allow for contraction and changes in cell shape |
| Protective Functions of Proteins | -Immunoglobin/Interferon: antibacterial/antiviral -Fibrin: stops loss of blood |
| Control Functions of Proteins | -Hormones allow for large scale control and changes. Ex. Insulin-regulate blood sugar, Somatotropin- regulates growth -Control and regulation of gene expression: transcriptional factors, histones, polymerases |
| Disulfide Bonds | Cystein is unique as it can create disulfide bonds. Cysteins can bond together by creating a disulfide bridge |
| Peptide Bonds | -C--N bond -not flexible |
| Primary Structure | -amino acid sequence -specific by the peptide bonds b/n amino acids -covalently bonded -Amino terminal, 1st amino acid in the chain -Carboxy terminal, last amino acid in the chain |
| Conservative Substitution | replacement of an aa by one of the similar polarity |
| Non-conservative Substitution | replace a residue by one aa of a differnet polarity |
| Invariant Substitution | highly conserved, important to the functionality of the protein rather than its structure |
| Consider aside from polarity | volume and surface area- ex. Glycine and Tryptophan have the same polarity by are dramatically different in size |
| Secondary Structure | alpha helices beta sheets random coil |
| Alpha helices | - held together by h bonds b/n backbone atoms not side chains. the side chains are on the outside of the helix |
| Beta sheets | -flat structures that are either parallel or antiparallel. H bonds b/n backbone atoms hold the sheets together; side chains projects above and below the plan of the sheet |
| Secondary Structure does not arise from interaction with the side chains | Alpha helices and beta sheets arise through H-bond interactions b/n N-H and C=O groups on the peptide bonds |
| Key Concept about primary and secondary structure | charges and arrangement of the primary structure will determine the secondary structures generated. Changes to the primary structure can result in dramatic changes to secondary and higher levels of organization. |
| Tertiary Structure | -3D structure of the protein |
| Domain | -any sequence of the polypeptide chain that can correctly fold into its 2ndary and tertiary structures independent of the rest of the sequence. -often have specific binding purpose |
| Quaternary Structure | subunits- independent polypeptide chains that come together to form a single protein complex |
| Conformation | refers to the final shape of a protein under particular conditions -involves all weak interactions |
| Folding | -native conformation: the natural, often lowest energy conformation the protein adopts (driven by primary structure) -denatured: loss of any specific conformation -assisted by chaperonins -it is fast! nature finds correct conformation instantaneously |
| Chaperones | -scaffolds/enzymes that can aid in the folding of proteins, especially mis-folded ones -protein disulfide isomerase: coordinates disulfide bonds -heat shock proteins: upregulated during elevated temps -help block hydrophobic faces to prevent aggregatio |
| Dynamic Aspects of Proteins | -not static entities -computations that increase heat on a system of atoms and evaluate motion -low freq harmonics -motions are responsible for substrate binding of drugs, allosteric effects, e- transfer, viruses, catalytic activity |
| Conformaitonal changes occur by.. | ..the binding of small molecules, substrates, phosphorylation etc... |
| Globular Proteins | -spheriod in shape -hydrophilic with hydrophobic core -functions: catalysts, transporters, regualtors |
| Fibrous Proteins | -larger amount of 2ndary structure -long and rod shaped -low solubility -functions: structural rather than dynamic -collagen, keratin, tropomyosin |
| Collagen | -present in all tissues and organs -provides form and strength -primary sequence: GLY-X-Y -helix w/in a helix structure |
| Glycoproteins | -part of ABO and Rh blood system -histocompatibility -tumorigenesis |
| Prions | -infections agents in the absence of DNA or RNA -appear to be capable of altering conformation of other proteins |
| Creutzfedlt-Jakob Disease | Symptoms: ataxia, dementia, paralysis, always fatal, inherited or sporadic mutation or infections process: kuru |
Created by:
clewis3
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