- Type
- Final term past paper
- Course
- BIF401 Bioinformatics I
- Size
- PDF 527 KB
- Updated
- 23 Oct 2026
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bif401) (bioinformatics 1) MCQ’s for final term, Organised by Muhammad Kashif
151-250
------- provide mass of intact molecules and its fragments
MS1 and MS2
theoratical data is usually ----- as compared to exp. Data, larger Three scoring schemes can be applied to ------ score
the match at each stage of protein search
In the above scoring method, MW and PST stabs for ____ & _____ respectively
MS1 & MS2
_____ are assembled by Ribosomes in cellular cytoplasm
Proteins
Amino acids have characteristics like polarity, hydrophobicity, and charge states. these characteristics are governed by
Elemental composition of an amino acid’s side chain (R group)
Hydrophobic amino acids are non-polar due to very
little dipole moments between H and C
Core of amino acids is ______ and surface is ______ Hydrophobic
& hydrophilic
At pH ____ Five amino acids are charged, 2 negatively and 3 positively 7 pK values for an amino acid is the pH at which:
Exactly half of the chargeable group is charged
The pK of aspartic and glutamic acids are ___-& ____ respectively.
3.9 & 4.2
If pH < pK for an amino acid, the amine side chains____
Gain proton and hence basic
If pH > pK for an amino acid, _________ loses a proton and hence acidic
The carboxyl side chain
Lysine and arginine have pK ____ &___ respectively.
10.5 & 12.5
Glycine residues increase backbone flexibility because : They
have no R group (only an H)
______ reduce the flexibility of polypeptide chains.
Proline residues
____ Cement together by making _____ to stabilize 3-D protein structures
Cysteines, disulfide bonds
Chemically _____ remain in the core of protein.
Inactive amino acids
Backbone is highly polar (hydrophilic) due to polar ___ and ___ in each peptide unit
-NH & C=O
A-helices & B-sheets are stabilized by____ H-bonds The very few hydrophobic "patches" on protein surface are involved in:
Protein-protein interactions
Alpha Helix is Stabilized by H-bonds between every ____ in backbone
~ 4th residue
Proteins fold spontaneously to achieve:
Thermodynamic stability
If a protein is ____, then it can lead to a lack of function in the protein
Misfolded
Given algorithms and procedures to fold a protein, we can:
Fold amino acid chains to form 3D proteins
Each amino acid can fold into____, ____ & ____
Alpha Helices, Beta Sheets and Loops
If computations of protein folding take 1/10th of a nano-second(10 -10), then to compute all the folding possibilities will take
1.6 x 1030 years
All the information required for folding a protein into its native structure is present within the:
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