Chapter Five And Six Flashcards by Leah Zimmerman

Amino acid sequence determines what

Protein shape

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What type of boding maintains shape

Noncovalent bonding

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What type of bonding determines flexibility and rotation

Covalent

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What do you want the easiest shape to form

Least energy required to make

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What are molecular chaperones

Help the protein fold correctly

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What are some diseases that are caused by improper protein folding

Alzheimer’s, Huntington’s, creuzfeldt-Jakob

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What are prions

Misfolding proteins in the brain

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Symptoms of Parkinson’s

Resting tremor, rigidity, festinating Gate, dementia

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Aggregates of misfolded proteins- prions- form what

Amyloid fibrils

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What are some shapes of proteins

Globular, fibrous, sheets,rings, and spheres

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What can help determine shape of protein in lab

X-ray crystallography, NMR, and threading

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What are some folding patterns of proteins

Alpha helix, beta sheet and H bonding

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Examples of alpha helix

Keratin

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Where can keratin be found

Nails, hair, skin, horns

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Example of beta sheet

Fibroid

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Where can fibroin be found

Silk

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Hydrogen bonds in alpha helixes bond with every what number of peptide bond

Fourth

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What is a coiled coil

Two alpha helixes that tuck in the hydrophobic areas

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In beta sheets, how do H bonds form

Between peptides that are laying side by side

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Anti parallel has what size loop

Short loop

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Parallel beta sheet has what type of loop

Long

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What is an example of beta sheet

Antifreeze protein

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What is a protein domain

Independently folding polypeptide chain from which other proteins are constructed

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What are targets for proteins

Unstructured protein regions

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What are unstructured protein regions

Larger proteins with numerous domains connect by polypeptide chain containing unstructured sequences

Are unstructured protein regions tucked into the protein

No, not folded

What are flexible tethers

Provide movement and flexibility, help scaffold proteins bring proteins together, intracellular signaling pathways, assist elastin in forming rubberlike fibers

Unstructured regions in UPRs can do what

Bend, flex, wrap around larger target proteins

What are protein families

Groups of proteins with similar amino acid sequences and conformations, look similar and have similar functions

What are examples of protein families

Serine proteases, chemotrypsin, trypsin, elastase

Dimer and tetrameres are examples of

Large protein molecules containing weak noncovalent forces

Example of large protein molecule

Hemoglobin

Filaments, sheets or spheres are larger proteins that depend on

Complimentary binding sites and have indefinite number of bindings

Elongated fibrous proteins spans

Long distances

Examples of elongated fibrous proteins

Keratin, extracellular matrix, collagen and elastin

What are extracellular proteins

Covalent cross linkages that strengthen proteins by formation of disulfide bonds that are found extracellularly

How do protein binding work

Proteins interact with ligands through weak or strong binding

Proteins have what type of binding with noncovalent bonds

Complementary binding

Function of antibodies

Hunt pathogens

Describe binding of antibodies

Tight and specific

Structure of antibody

Y shaped

Where is the specificity of binding in antibodies

At the y ends

How does binding occur in antibodies

Triggered by an immune response

Enzymes as catalysts are highly...

Specific for a single reaction

Function of lysozyme

Break down polysaccharide chains

How do lysozymes break down polysaccharides

Add water to molecule

Examples of non protein molecular coenzyme assistants

Retinal, heme molecules, and coenzymes

Catalytic activities of enzymes are regulated by

Gene expression, compartmentalizations, feedback regulation

What are the different types of binding in catalytic enzymes

Allosteric binding, phosphate binding

What are allosteric enzymes

Enzymes with two binding sites

How do allosteric enzymes work

Bind in both binding sites then change conformations

Function of phosphorylation

Involves attachment of a phosphate group to an amino acid side chain

Phosphorylation changes what in protein

Activity

Kinases function

Add phosphate

Phosphotases function

Take away phosphate

How do GTP binding proteins work

GTP in protein becomes hydrolyzed to form GDP inactivating the protein then GDP leaves protein, GTP then reactivates protein

Function of motor proteins

Cellular movement

What are protein machines

Large complexes that allow proteins to act in a coordinated manner due to hydrolysis of GTP or ATP

Example of covalent modifications in protein machines

Receptor tyrosine kinase

How are proteins studied in vitro

Cultured cells, differentiated properties are maintained, raw materials