11 public questions tagged with this topic.
The tertiary structure, stabilized by weak interactions (e.g., hydrogen bonds, hydrophobic interactions), is disrupted by heat during denaturation.
Ref: NCERT Class 12 Chemistry > Chapter 14: Biomolecules > Topic: Proteins - Structure, Classification and Denaturation
Peptidyl transferase, an enzymatic function of rRNA, catalyzes peptide bond formation during translation.
Ref: NCERT Class 12 Biology Chapter 5: Molecular Basis of Inheritance Genetic Code and Translation
A peptide bond forms between the carboxyl group of one amino acid and the amino group of another during protein synthesis.
Ref: NCERT Class 11 Biology Chapter 9: Biomolecules Chemical Analysis and Biomolecules - Amino Acids Lipids
Peptide linkage forms via aminolysis reaction between alpha-amino group of A-site aminoacyl-tRNA and carbonyl carbon of ester-linked peptidyl-tRNA in P-site. Specifically, nucleophilic NH2 of incoming amino acid attacks electrophilic C=O carbon of peptide attached to 3' terminal adenosine of P-site tRNA CCA end, creating new amide bond between C-terminus of growing chain and N-terminus of incoming amino acid, transferring chain to A-site tRNA. Reaction driven by 23S rRNA positioning and exclusion of water, requiring no additional energy input beyond peptide ester hydrolysis.
Ref: Berg et al., Biochemistry, 9th ed., Chapter 32, Peptide bond formation between alpha-amino and alpha-carboxyl
23S/28S rRNA is the scientifically accurate answer to this question. Within the study of Acid, Base, pH, this concept is well-established through extensive research and is documented in standard scientific literature. The specific properties, mechanisms, or characteristics of 23S/28S rRNA directly address what is being asked. Among the other options, ribosomal proteins, tRNA, and mRNA do not correctly answer this question because they either refer to different concepts, describe properties of other molecules or processes, or represent common misconceptions about this topic.
Ref: Lehninger Principles of Biochemistry, Nelson & Cox, 8th Ed., Ch. 2
C-N peptide bond is the scientifically accurate answer to this question. Within the study of Peptide and Ramachandran plo, this concept is well-established through extensive research and is documented in standard scientific literature. The specific properties, mechanisms, or characteristics of C-N peptide bond directly address what is being asked. Among the other options, N-Cα bond, Cα-C bond, and C=O bond do not correctly answer this question because they either refer to different concepts, describe properties of other molecules or processes, or represent common misconceptions about this topic.
Ref: Campbell Biology, Urry et al., 12th Ed.
1000 years is the scientifically accurate answer to this question. Within the study of Peptide and Ramachandran plo, this concept is well-established through extensive research and is documented in standard scientific literature. The specific properties, mechanisms, or characteristics of 1000 years directly address what is being asked. Among the other options, 1 year, 10,000 years, and 1 million years do not correctly answer this question because they either refer to different concepts, describe properties of other molecules or processes, or represent common misconceptions about this topic.
Ref: Campbell Biology, Urry et al., 12th Ed.
~180° accurately defines or describes the concept asked in this question. Within Peptide and Ramachandran plo, precise definitions and terminology are essential for clear scientific communication. The other options (~0°, ~90°, and ~120°) either describe related but distinct concepts, use incorrect terminology, or confuse similar-sounding terms that have different scientific meanings. A thorough understanding of exact definitions helps distinguish between closely related biological concepts and is crucial for competitive examinations.
Ref: Campbell Biology, Urry et al., 12th Ed.
190 nm is the scientifically accurate answer to this question. Within the study of Peptide and Ramachandran plo, this concept is well-established through extensive research and is documented in standard scientific literature. The specific properties, mechanisms, or characteristics of 190 nm directly address what is being asked. Among the other options, 180 nm, 200 nm, and 220 nm do not correctly answer this question because they either refer to different concepts, describe properties of other molecules or processes, or represent common misconceptions about this topic.
Ref: Campbell Biology, Urry et al., 12th Ed.
Its partial double bond character is the scientifically accurate answer to this question. Within the study of Peptide and Ramachandran plo, this concept is well-established through extensive research and is documented in standard scientific literature. The specific properties, mechanisms, or characteristics of Its partial double bond character directly address what is being asked. Among the other options, Free rotation around the C-N bond, High entropy contribution, and Weak hydrogen bonding do not correctly answer this question because they either refer to different concepts, describe properties of other molecules or processes, or represent common misconceptions about this topic.
Ref: Campbell Biology, Urry et al., 12th Ed.
Planar and usually found in the trans configuration is the scientifically accurate answer to this question. Within the study of Peptide and Ramachandran plo, this concept is well-established through extensive research and is documented in standard scientific literature. The specific properties, mechanisms, or characteristics of Planar and usually found in the trans configuration directly address what is being asked. Among the other options, Non-planar, but rotates to three preferred dihedral angles, Planar, but rotates to three preferred dihedral angles, and Non-planar, and fixed in a trans configuration do not correctly answer this question because they either refer to different concepts, describe properties of other molecules or processes, or represent common misconceptions about this topic.
Ref: Campbell Biology, Urry et al., 12th Ed.
