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#protein stability

7 public questions tagged with this topic.

Lipid Link Protein

Which detergent is most likely to maintain a protein’s native structure during extraction?

Extraction of integral membrane proteins for functional study demands detergent that disrupts lipid bilayer but avoids complete unfolding of polypeptide. Ionic strong detergents like SDS bind cooperatively to protein backbone at about one SDS per two amino acids, imparting negative charge, disrupting secondary structure and denaturing enzymes, suitable for electrophoresis but not activity assays. Non-ionic detergents Triton X-100, Nonidet P-40, dodecyl-beta-D-maltoside DDM and octyl glucoside are milder; they replace lipids around transmembrane helices forming protein-detergent micelles, maint

Ref: Privé, Methods 2007, Detergent choice; Garavito & Ferguson-Miller, J Biol Chem 2001.

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Amino Acids Basics

What type of interaction primarily stabilizes the tertiary structure of proteins?

Disulfide bonds accurately describes the structural composition or molecular organization asked about in this question. In Amino Acids Basics, knowledge of molecular structure is directly linked to understanding biological function. The specific arrangement of chemical components in Disulfide bonds determines its physical properties, biological activity, and interactions with other molecules. The other options (Peptide bonds, Hydrogen bonds, and Ionic bonds) describe different structural arrangements, incorrect stoichiometry, or compositions of different biological molecules.

Ref: Lehninger Principles of Biochemistry, Nelson & Cox, 8th Ed., Ch. 3

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Ramachandran plot

The lifetime of a peptide bond is approximately:

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.

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Protein

Which type of β-sheet is more stable?

Antiparallel is the accurate classification or categorization for the organism, molecule, or concept described in this question. In Protein Structure, proper classification is based on shared characteristics including morphological, biochemical, genetic, and evolutionary criteria. Antiparallel meets the specific diagnostic features and defining criteria that distinguish it from related groups. The other options (Parallel, Both are equally stable, and Depends on environment) belong to different taxonomic groups, represent different classification levels, or possess distinct characteristics that

Ref: Lehninger Principles of Biochemistry, Nelson & Cox, 8th Ed., Ch. 4

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Protein

Which of the following factors stabilizes a protein's tertiary structure?

Disulfide bonds accurately describes the structural composition or molecular organization asked about in this question. In Protein Solubility, knowledge of molecular structure is directly linked to understanding biological function. The specific arrangement of chemical components in Disulfide bonds determines its physical properties, biological activity, and interactions with other molecules. The other options (High temperature, pH at isoelectric point, and High salt concentration) describe different structural arrangements, incorrect stoichiometry, or compositions of different biological mole

Ref: Lehninger Principles of Biochemistry, Nelson & Cox, 8th Ed., Ch. 4

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Protein

Which of the following agents disrupts hydrophobic interactions?

SDS accurately identifies the binding site, binding partner, or molecular interaction described in this question. In Protein Solubility, molecular recognition and binding specificity are governed by complementary shape, charge, and hydrophobic interactions between molecules. SDS binds at the specified location due to its structural complementarity and specific non-covalent or covalent interactions. The other options (DTT, Urea, and NaOH) describe binding to different sites, involve different types of molecular interactions, or represent incorrect binding partners.

Ref: Lehninger Principles of Biochemistry, Nelson & Cox, 8th Ed., Ch. 4

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Protein

Which amino acid sequence is most resistant to degradation?

A sequence rich in Proline, Glutamate, Serine, and Threonine is the scientifically accurate answer to this question. Within the study of Protein Degradation, this concept is well-established through extensive research and is documented in standard scientific literature. The specific properties, mechanisms, or characteristics of A sequence rich in Proline, Glutamate, Serine, and Threonine directly address what is being asked. Among the other options, A sequence rich in Arginine and Lysine, A sequence rich in Methionine and Cysteine, and A sequence rich in Phenylalanine and Tyrosine do not corre

Ref: Lehninger Principles of Biochemistry, Nelson & Cox, 8th Ed., Ch. 4

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