Genetics: Analysis and Principles
Genetics: Analysis and Principles
6th Edition
ISBN: 9781259616020
Author: Robert J. Brooker Professor Dr.
Publisher: McGraw-Hill Education
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Chapter 24, Problem 6CONQ
Summary Introduction

To review:

The revelations made from the alignment of sequences of five homologous proteins.

Introduction:

The alignment of three or more than three biological sequences, which may be DNA (deoxyribonucleic acid), RNA (ribonucleic acid), or protein known as multiple sequence alignment. The alignment methods that are mainly used are iterative methods, progressive alignment construction, hidden markov models and consensus methods.

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Suppose that there is an unknown protein that underwent Edman sequencing method. From N- terminal determination, a biochemist found out that there are two N-terminal amino acid residues, V and G. What is the original sequence of the protein given the following peptide fragments: after digestion with Chymotrypsin: G-L-S-R-G-M-w V-A-L-F Q-L-Y L-R-V-W G-M-V-E-A-D-I-P K-S-P-E-M-T-W R-M-A-S-E-K-P-G-H after digestion with Trypsin: P-G-H V-W-G-M-V-E-A-D-I-P M-A-S-E-K G-M-W-Q-L-Y-L-R S-P-E-M-T-W-R G-L-S-R V-A-L-F-K after digestion with Cyanogen Bromide: T-W-R-M W-Q-L-Y-L-R-V-W-G-M V-E-A-D-I-P A-S-E-K-P-G-H V-A-L-F-K-S-P-E-M G-L-S-R-G-M
You have discovered a novel protein that has a pI = 5.5. To study the functional properties of this new protein, your research group has made a mutant that contains two amino acid changes—namely, a surface Phe residue in the normal protein has been replaced by His (side chain pKa = 6.1) and asurface Gln has been replaced by Glu (side chain pKa = 6.0). Is the pI of themutant protein predicted to be greater than, less than, or the same as the pIof the normal protein? Support your answer with the appropriate calculation.
The following sequence alignment shows the point mutation that exists in hemoglobin for some cases of sickle cell (HbS) compared to wild type adult hemoglobin (HbA) VLSPADK (HBA) VLSPAVK (HbS) Based solely on the peptide fragment shown, answer the following questions: What is the charge range for the HbA peptide shown above? **Hint, what is convention for how charge ranges are written?? At physiological pH, what is the charge of the HbS peptide? →>>> What is the impact of this point mutation? Choose the letter for the answer choice that best applies. a. Allows for hydrophobic contacts in HbS that lead to higher order structures beyond the a2ß2 heterotetramer b. Allows for ionic interactions in HbS that aids in interactions with solvent c. Destabilizes the ionic interactions of the dimer-dimer interface and prevents the T- to R- state transition d. Prevents the coordination of Fe²+ at the protoporphyrin ring
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