The folded states of globular proteins in aqueous solutions are stabilized primarily by
If you're seeing this message, it means we're having trouble loading external resources on our website. Show If you're behind a web filter, please make sure that the domains *.kastatic.org and *.kasandbox.org are unblocked. Question: Video Answer: Get the answer to your homework problem. Try Numerade free for 7 days We don’t have your requested question, but here is a suggested video that might help. Related QuestionSecondary structures in proteins are stabilized by: a. ionic interactions between side chains of amino acids b. hydrogen bonds between peptide bonds c. hydrophobic interactions between peptide bonds d. weak non-covalent interactions between side chains e. hydrogen bonds between side chains of amino acids DiscussionYou must be signed in to discuss. Video TranscriptThe primary second dream tertiary structures are described. The alpha carbon that bonds with the car boxes group has some rotation, which gives us different angles, but in limited values these angles are called the torch and angles. Poly peptide chains can be found in the sheets, alpha helix and more. It is stable because of the forces that are present between the assets located at some distance from each other, the ionic interactions or the salt linkages between the charge the groups on the side chains helps. The wholeprotein can't be stable as such. The correct answer is option year. The hydrogen bonds that are formed between the peptide bonds don't have the same stabilizing effect as the option. Hence, option B. Is it the correct answer? When the car boxing group of one amino acid reacts with the main group of other amino acid with the release of water, a chemical bond is formed between two molecules. The interactions between the backbone and bonds don't exist. Is not the correct answer. There are violent interactions between the side chains. There is a short distance. Both forces have attractive and repulsive components. The answer is not the correct one. Hydrogen bonds are formed between the side chains of the polar acids and between a call boxes oxygen and a hydrogen donor group. The helix structure is stable by these bonds. The correct answer is option E. Biophys J. 1996 Oct; 71(4): 2033–2039.
It is clear that intramolecular hydrogen bonds are essential to the structure and stability of globular proteins. It is not clear, however, whether they make a net favorable contribution to this stability. Experimental and theoretical studies are at odds over this important question. Measurements of the change in conformational stability, delta (delta G), for the mutation of a hydrogen bonded residue to one incapable of hydrogen
bonding suggest a stabilization of 1.0 kcal/mol per hydrogen bond. If the delta (delta G) values are corrected for differences in side-chain hydrophobicity and conformational entropy, then the estimated stabilization becomes 2.2 kcal/mol per hydrogen bond. These and other experimental studies discussed here are consistent and compelling: hydrogen bonding stabilizes globular proteins. Full text is available as a scanned copy of the original print
version. Get a printable copy (PDF file) of the complete article (1.4M), or click on a page image below to browse page by page. Links to PubMed are also available for Selected References. Selected ReferencesThese references are in PubMed. This may not be the complete list of references from this article.
Articles from Biophysical Journal are provided here courtesy of The Biophysical Society How are globular proteins stabilized?Hydrogen bonding stabilizes globular proteins.
What stabilizes a folded protein?Isopeptide bonds are covalent amide bonds between amino-acid side chains that stabilize a fold, or connect two proteins.
Are globular proteins stabilized by hydrophobic interactions?The globular conformation of proteins is stabilized predominately by hydrophobic interactions.
How is a protein fold Stabilised?Folded proteins are stabilized by thousands of noncovalent bonds between amino acids. In addition, chemical forces between a protein and its immediate environment contribute to protein shape and stability.
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