Unit 5: 3-D Structure and Folding Flashcards

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1
Q

What is conformation

A

spatial arrangement of atoms in a protein that depends on rotation of bonds, does not involve bond breaking/making

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2
Q

What does native protein mean

A

protein in any of their functional folded conformation

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3
Q

primary structure

A

peptide bonds; aa sequence

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4
Q

secondary structre

A

hydrogen bonds, alpha helices, beta sheets

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5
Q

tertiary structure

A

interplay of side chains/R groups in folded protein

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6
Q

Quaternary structure

A

non covalent interaxn btwn diff polypeptide chains

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7
Q

What does X-ray crystallography measure

A

locations and intenisty of spots produced on photographic film by beam of x rays after the beam is diffracted by e- of an atom

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8
Q

What are the steps involved in x-ray crystallography

A

make crystal(most difficult). diffraction pattern. e- density map. atomic model

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9
Q

What is essential to fit protein to e- density map

A

sequence data

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10
Q

What is nuclear magnetic resonance

A

physical phenomenon in which the nuclei in a magnetic field absorbs and re-emits electromagnetic radiation

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11
Q

Disadvantage of nuclear magnetic resonance

A

only identifies structures of small portions

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12
Q

advantage of nuclear magnetic resonance

A

analysis carried out on macromolecule in sln, no crystals needed. allows for movement

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13
Q

Describe the planar nature of peptide bond

A

has partial double bond character, even though it is drawn as single bond. length of peptide bond supports a double bond nature of peptide linkage. charge on carbonyl )2 and amino H2 also indicate double bond nature. peptide linkage that forms btn 2 aa is planar

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