Biochem_Ch5Iii

Front 1

Differentiate Globular and fibroud protiens?

Back 1

a

Front 2

What does it mean for a protien to not have a regular structure?

What is it not described by?

Back 2

a

Front 3

Tertiary:
-examples
-define?
-Techniques: name two

Back 3

a

Front 4

tertiary:
1)Xray:
-wavelength?
-must have what? Define it?
-Diagram it?
-Xrays interact with what and how? Diagram light and dark spots?
-What is used to reconstruct image?
-Whats need to focus image? Whats lacking?

Back 4

a

Front 5

tertiary:
1)...
-Is crystallization easy?
-Give three reasons why?
a. Type of crystals and why?
b. use knowledge of what to enhance what?
c. what is obtained from crystal vs. solution?

Back 5

a

Front 6

tertiary:
2) NMR:
-type used in macromolecules? give examples?
-nmr helps you ID what?
-Whats not needed here and why?
-Compare to xray
-size of protien
-how many resolutions possible? what does that mean?

Back 6

a

Front 7

SIDE CHAIN:
-name 3 general principlesof tertiary aa?

1. What kind of residues are interior? Why?
2. what residues are on surface?
3. what residues are on both sides and why?

Back 7

a

Front 8

SSS
-another word for it?
-compare to what wrt size? bigger or smaller?
-common arrangement of what kind of aa structure?
-List 5 types of SSS?Draw each.
-Some SSS give indication of what? Give example.

Back 8

a

Front 9

DOmAINS:
-define?example?
-type of core every domain has?
-define linker and its fnc?
-What has seperable func?
-Usefulness?
-how have domains evolved?
-encoded by?

Back 9

a

Front 10

PRotien FAmilies:
-compare to aa seq tech
-define
-often used for what kind of protiens that share what?

Back 10

a