Academic Integrity: tutoring, explanations, and feedback — we don’t complete graded work or submit on a student’s behalf.

1. Beta sheets come in two major flavors: parallel and anti-parallel. Which of t

ID: 1004040 • Letter: 1

Question

1. Beta sheets come in two major flavors: parallel and anti-parallel. Which of these types of beta sheets, typically, creates the most "local" interactions?

a)Parallel

b)Antiparallel

c)They are typically equal in interaction distance.

d)No answer text provided.

2.You have the diprotic peptide:

Ala-Phe

Alanine information:
pKa of carboxy end = 1.82
pKa of amine end = 9.50

Phenylalanine information:
pKa of carboxy end = 2.42
pKa of amine end = 9.20

(These numbers are made up, but use them in your calculation!)

What is the pI of this dipeptide? Be precise to the hundredth's place.

3.You have the diprotic peptide:

Asp-Tyr

Aspartic acid information:
pKa of carboxy end = 1.72
pKa of amine end = 9.40
pKR = 3.76

Tyrosine information:
pKa of carboxy end = 2.06
pKa of amine end = 9.10

(These numbers are made up, but use them in your calculation!)

What is the pI of this dipeptide? Be precise to the hundredth's place.

4.What is the primary driving force in the folding of proteins?

a)Formation of hydrogen bonds

b)Formation of salt bridges

c)Formation of dislufide bridges

d)Minimization of exposed hydrophobic residues to the solvent

e)Forming alpha helices and beta sheets

5.You have two proteins, protein A and protein B, that you believe interact with one another and form a quaternary structure/complex (the AB complex).

You have two containers, one that holds protein A, and one that holds protein B.

You mix the two containers together into a new container.

Which of the following techniques would best determine if if the two proteins in your new container have complexed together?

a)A typical SDS PAGE

b)Size exclusion chromatography

c)IR Spectroscopy

d)1H NMR

6.Use the following website to answer this question:

http://www.scripps.edu/~cdputnam/protcalc.html

What is the estimated pI of aquaporin, according to the above website?

The primary sequence of aquaporin is:

MASEFKKKLF WRAVVAEFLA TTLFVFISIG SALGFKYPVG NNQTAVQDNV KVSLAFGLSI ATLAQSVGHI SGAHLNPAVT LGLLLSCQIS IFRALMYIIA QCVGAIVATA ILSGITSSLT GNSLGRNDLA DGVNSGQGLG IEIIGTLQLV LCVLATTDRR RRDLGGSAPL AIGLSVALGH LLAIDYTGCG INPARSFGSA VITHNFSNHW IFWVGPFIGG ALAVLIYDFI LAPRSSDLTD RVKVWTSGQV EEYDLDADDI NSRVEMKPK

Explanation / Answer

1). a) Parallel

The local interactions in parallel beta sheets is common than in the anti-parallel beta sheets because the parallel beta sheets are highly unstable and are more prone to form hydrogen bonds.