Biochemistry
9th Edition
ISBN: 9781319114671
Author: Lubert Stryer, Jeremy M. Berg, John L. Tymoczko, Gregory J. Gatto Jr.
Publisher: W. H. Freeman
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Question
Chapter 2, Problem 27P
Interpretation Introduction
Interpretation:
The reason why the definite groups in the folded proteins have about more than 500 pKavalues should be determined.
Concept introduction:
A peptide bond exists between the two amino acids. During the formation of a peptide bond, a molecule of water is released. The carboxyl group of one amino acid gets linked with the amino group of the other amino acid. Polypeptides and proteins are the chains formed by the amino acids.
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. A protein gives, under conditions of buffer composition, pH, and tem-
perature that are close to physiological conditions, a molecular weight
by sedimentation equilibrium measurements of 140,000 g/mol. When
the same protein is studied by SDS gel electrophoresis in the absence
or presence of the reducing agent B-mercaptoethanol (BME), the pat-
terns seen, respectively, in lanes A and B are observed. Lane C contains
standards of molecular weight indicated. From these data, describe the
native protein, in terms of the kinds of subunits present, the stoi-
chiometry of subunits, and the kinds of bonding (covalent, noncova-
lent) existing between subunits. /
A
B
- BME
+ BME
STD
Serum albumin,
67,000
Ovalbumin,
43,000
Carbonic anhydrase,
30,000
Trypsin inhibitor,
20,000
10
2.
4.
Co
cm migrated
need help to calculate P1 for amino acid Tryptophan. Also please check if I draw the mechanism correctly and completely???
Predict the number of bands and apparent mol. wt. of the following proteins on SDS gels.
1. A trimeric protein containing three chains, each with a molecular weight of 60,000 Da (60 kDa).
Chapter 2 Solutions
Biochemistry
Ch. 2 - Prob. 1PCh. 2 - Prob. 2PCh. 2 - Prob. 3PCh. 2 - Prob. 4PCh. 2 - Prob. 5PCh. 2 - Prob. 6PCh. 2 - Prob. 7PCh. 2 - Prob. 8PCh. 2 - Prob. 9PCh. 2 - Prob. 10P
Ch. 2 - Prob. 11PCh. 2 - Prob. 12PCh. 2 - Prob. 13PCh. 2 - Prob. 14PCh. 2 - Prob. 15PCh. 2 - Prob. 16PCh. 2 - Prob. 17PCh. 2 - Prob. 18PCh. 2 - Prob. 19PCh. 2 - Prob. 20PCh. 2 - Prob. 21PCh. 2 - Prob. 22PCh. 2 - Prob. 23PCh. 2 - Prob. 24PCh. 2 - Prob. 25PCh. 2 - Prob. 26PCh. 2 - Prob. 27PCh. 2 - Prob. 28PCh. 2 - Prob. 29PCh. 2 - Prob. 30PCh. 2 - Prob. 31PCh. 2 - Prob. 32PCh. 2 - Prob. 33PCh. 2 - Prob. 34PCh. 2 - Prob. 35PCh. 2 - Prob. 36PCh. 2 - Prob. 37P
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- The extinction coefficient or absorptivity (ɛ) of protein A at 340 nm is 6440 M-1 cm-1, whereas protein B does not absorb at 340 nm. What absorbance will be observed when light at 340 nm passes through a 5 mm cuvette containing 10 µM of protein A and 10 µM of protein B? Beer-Lambert-law; A = ɛ x C x1; A = absorbance, C= concentration, 1= pathlength).arrow_forwardGiven: Cryo-EM structure of PCoV_GX spike glycoprotein 1. What can you tell me about the identity of the protein? 2. What is the importance of this protein?arrow_forwardWhy different amino acids have different Rf values? If you separate a mixture of amino acids consist of glutamic acid, histidine, glycine, tryptophan and isoleucine with paper chromatography using NH3: Benzene (10:90) as a mobile phase what do you expect the Rf values of the amino acids will be?arrow_forward
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