Biochemistry
9th Edition
ISBN: 9781319114671
Author: Lubert Stryer, Jeremy M. Berg, John L. Tymoczko, Gregory J. Gatto Jr.
Publisher: W. H. Freeman
expand_more
expand_more
format_list_bulleted
Concept explainers
Question
Chapter 8, Problem 23P
Interpretation Introduction
Interpretation:
Whether
Concept introduction:
A constant which expresses the substrate’s concentration if the velocity of reaction equals to the half of the maximum velocity of the reaction is known as Michaelis-Menten constant. It is denoted by
Expert Solution & Answer
Want to see the full answer?
Check out a sample textbook solutionStudents have asked these similar questions
Choose Two. The Ramachandran plot
indicates:
B
H
Ca
|||||||
Ⓒ. The
C1
I
A. Combined preference
about both
H
しょしい
O
conformation
preference for
a
C1-C² and c²_N bonde
Existence of a peptide in an a-helical
conformation
Or P sheeted
The prefered conformation about Can
bond.
The prefered conformation about C1-C²
bond
The prefesed conformation about
peptide bond.
. A nervous polecat. Pyrrolysine (Pyl, O) and Selenocysteine (Sec, U) are two uncommon amino acids.
Knowing that these amino acids exists, translate the following amino acid sequence into one – letter code: Thr
– Trp – Ile – Thr – Cys – His – Tyr – Leu – Ile – Thr – Thr – Ile – Glu – Phe – Glu – Arg – Arg – Glu – Thr – Ala
– Arg – Glu – Asn – Thr – Tyr – Pyl – Sec – Met – Ala – Leu – Phe – Pyl – Tyr.
Help ASAP, thanks!"Which is a characteristic of cooperative binding that is exhibited by a protein?"
Chapter 8 Solutions
Biochemistry
Ch. 8 - Prob. 1PCh. 8 - Prob. 2PCh. 8 - Prob. 3PCh. 8 - Prob. 4PCh. 8 - Prob. 5PCh. 8 - Prob. 6PCh. 8 - Prob. 7PCh. 8 - Prob. 8PCh. 8 - Prob. 9PCh. 8 - Prob. 10P
Ch. 8 - Prob. 11PCh. 8 - Prob. 12PCh. 8 - Prob. 13PCh. 8 - Prob. 14PCh. 8 - Prob. 15PCh. 8 - Prob. 16PCh. 8 - Prob. 17PCh. 8 - Prob. 18PCh. 8 - Prob. 19PCh. 8 - Prob. 20PCh. 8 - Prob. 21PCh. 8 - Prob. 22PCh. 8 - Prob. 23PCh. 8 - Prob. 24PCh. 8 - Prob. 25PCh. 8 - Prob. 26PCh. 8 - Prob. 27PCh. 8 - Prob. 28PCh. 8 - Prob. 29PCh. 8 - Prob. 30PCh. 8 - Prob. 31PCh. 8 - Prob. 32PCh. 8 - Prob. 33PCh. 8 - Prob. 34PCh. 8 - Prob. 35PCh. 8 - Prob. 36PCh. 8 - Prob. 37PCh. 8 - Prob. 38PCh. 8 - Prob. 39PCh. 8 - Prob. 40PCh. 8 - Prob. 41PCh. 8 - Prob. 42PCh. 8 - Prob. 43PCh. 8 - Prob. 44PCh. 8 - Prob. 45PCh. 8 - Prob. 46PCh. 8 - Prob. 47PCh. 8 - Prob. 48PCh. 8 - Prob. 49P
Knowledge Booster
Learn more about
Need a deep-dive on the concept behind this application? Look no further. Learn more about this topic, biochemistry and related others by exploring similar questions and additional content below.Similar questions
- V-A. Which of the following amino acids will elute first in a cation-exchange column using a buffer at pH 7? 1. Asp or Lys 2. Arg or Met 3. Gly or Val 4. Ser or Alaarrow_forward. A protein has been sequenced after cleavage of disulfide bonds. The protein is known to contain 3 Cys residues, located as shown below. Only one of the Cys has a free - SH group and the other two are involved in an -s-s- bond. A Phe Cys « N-terminus Cys- - Met Cys- C-terminus The only methionine and the only aromatic amino acid (Phe) in this protein are in the positions indicated. Cleavage of the intact protein (i.e., with disulfide bonds intact) by either cyanogen bromide or chymotrypsin does not break the protein into two peptides. Where is the -s-s- bond (i.e., AB, BC, or AC)?arrow_forwardUnderstanding the Relevance of Chaperones in Protein Folding Protein molecules, like all molecules, can be characterized in terms of general properties such as size, shape, charge, solubility/hydrophobicity. Consider the influence of each of these general features on the likelihood of whether folding of a particular protein will require chaperone assistance or not. Be specific regarding just Hsp7O chaperones or Hsp7O chaperones and Hsp60 chaperonins.arrow_forward
- t, a The n of 4-19. In a common protein analysis, a dye binds to the protein and the color of the dye changes from brown to blue. The intensity of blue color is proportional to the amount of protein present. Protein (ug): 0.00 9.36 18.72 28.08 37.44 Absorbance: 0.466 0.676 0.883 1.086 1.280 2 (a) After subtracting the blank absorbance (0.466) from the remaining absorbances, use the method of least squares to determine the equation of the best straight line through these five points (n and intercept to express the equation in the form y (±s,) = [m (±sm)]x + [b (±sp)] with a reasonable number of signifi- cant figures. 02 5). Use the standard deviation of the slope and and (b) Make a graph showing the experimental data and the cal- culated straight line. and (c) An unknown gave an observed absorbance of 0.973. Cal- culate the number of micrograms of protein in the unknown, and estimate its uncertainty. nreearrow_forwardSIGNALS AND TARGETS. Listed below are sample polypeptides/proteins with their signal molecule/peptide. Answer the questions that follow. If you are asked to give the amino acid sequence, provide the sequence using the three-letter names of the amino acids (eg. ser-ala-met). Catalase with H2N-...KERINGKERIANGEKSAMSKL-COOH Provide the amino acid sequence of the signal peptide Where will this polypeptide be transported? (specify the compartment) What is the name of the specific receptor of this polypeptide? The receptor may also have what alternative function?arrow_forwardChoose all that apply. This molecule is O || O-P-O-P-O-P-O- 0 O a lipid O™ one of the building blocks of protein a nucleotide triphosphate ATP one of the building blocks of RNA a protein O™ one of the building blocks of DNA a nucleic acid a carbohydrate the energy currency of the cell an amino acid OIPIO о O™ N H₂N OH OH N Narrow_forward
- APPLICATIONS ON PROTEINS S TY Question #1: A shampoo bottle lists "partially hydrolyzed protein" as one of its ingredients. What is the difference between partially hydrolyzed protein and completely hydrolyzed protein? partially hydrolyzed protein completely hydrolyzed proteinarrow_forwardBeta folding. Parallel and antiparallel beta folding sheets (be able to draw). Beta loops. Examples of proteins formed mainly by this structure.arrow_forwardHello, please help me with my assignment. Can you answer ALL QUESTIONS EXCEPT QUESTIONS 1-31. Which of the following statements is accurate regarding these protein structures?a. Proteins in a quaternary structure consist of a simple polypeptide chain.b. Interactions between the R groups in amino acids form tertiary structure.c. Secondary structures are formed by multiple polypeptide chains.d. The two types of primary structure are α- helices and β- pleated sheets. 2. What type of bonds are formed between amino acids?a. Peptide bondb. Glycosidic linkagec. Hydrogen bondsd. Ester linkages 3. Which of the following is an example of protein denaturation?a. Amino acids fold into repeating patterns due to hydrogen bonding of the peptide backbone.b. Several amino acids are joined together via peptide bonds.c. A protein binds with a substrate, lowering the activation energy of a reaction.d. A protein is exposed to extremely high heat, causing it to lose its secondary structure and be leftwith…arrow_forward
- Peptides. 1. Draw the peptide Ala-Glu-Gly-Lys, as it would occur at physiological pH = 7.4. The R groups of Ala and Gly are not acidic or basic, therefore do not have a pka and the charge on these R groups is therefore independent of pH. Glu is acidic and Lys is basic, therefore the charge on these amino acids is pH dependent. The pKas are shown below. pKa N-term = 9.0 C-term = 3.5 Glu4.1 Lys = 10.5 2. Draw a circle around the peptide bonds. 3. Label the C-terminus and the N-terminus. 4. What is the overall charge on the peptide at pH 7.4?arrow_forwardwnich snows tne specinicity pockets. The S pocket nas a Ra glutamic acid in the bottom, the S2 pocket is small and hydrophobic, and the S,' pocket is deep and hydrophobic. Suggest a 3-amino acid sequence that this protease would R2 H cleave and indicate between which sites the peptide bond would be broken. S2 Which sequence would this protease cleave? Val-Lys-Phe Phe-Lys-Val Lys-Phe-Val Val-Phe-Lys Phe-Val-Lys O Lys-Val-Phe The peptide bond that is broken is between which sites? O S2 and S,' OS, and S,' O S2 and S1 O S2 and S1, and S and S,' IZarrow_forwardAll proteins . (Choose the most complete answer.) Group of answer choices have the same number of amino acids are synthesized on ribosomes and are made of amino acids connected by peptide bonds are made of amino acids connected by peptide bonds only are synthesized on ribosomes onlyarrow_forward
arrow_back_ios
SEE MORE QUESTIONS
arrow_forward_ios
Recommended textbooks for you
- BiochemistryBiochemistryISBN:9781305577206Author:Reginald H. Garrett, Charles M. GrishamPublisher:Cengage Learning
Biochemistry
Biochemistry
ISBN:9781305577206
Author:Reginald H. Garrett, Charles M. Grisham
Publisher:Cengage Learning
Biomolecules - Protein - Amino acids; Author: Tutorials Point (India) Ltd.;https://www.youtube.com/watch?v=ySNVPDHJ0ek;License: Standard YouTube License, CC-BY