Parallel polypeptide chains in beta-pleated sheet conformation are held together by hydrogen bonds all answers are correct R-group interactions covalent bonds
Added by Susan T.
Close
Step 1
Step 1: Beta-pleated sheets are a secondary structure of proteins. Show more…
Show all steps
Your feedback will help us improve your experience
Madhur L and 58 other Chemistry 101 educators are ready to help you.
Ask a new question
Labs
Want to see this concept in action?
Explore this concept interactively to see how it behaves as you change inputs.
Key Concepts
Recommended Videos
Which type of interaction stabilizes the α-helix and the β-pleated sheet structures of proteins? peptide bonds hydrogen bonds hydrophobic interactions disulfide bonds
Madhur L.
Which of the following bonds may contribute to the protein tertiary structure? Hydrogen bonds between R groups b Hydrophobic interactions between R groups Ionic bonds Disulfide bonds between two subunits or polypeptide chains Hydrogen bonds between the polypeptide backbone
Adi S.
α helices and β sheets are formed by which of the following? hydrogen bonds, ionic interactions, Van der Waals forces, disulfide bonds. None of these answer choices are correct. The evolution of proteins, as exemplified by superfamilies, shows conservation of what? structure, sequence, size, charge, isoelectric point. One advantage of having the amino acids of a structural motif contiguous within a polypeptide is to facilitate folding of the nascent polypeptide, to facilitate multimer formation, to facilitate quaternary structure formation, to facilitate protein-protein interactions. All of these answer choices are correct. In an amino acid, what is bonded to the central carbon atom, Cα? An R group, a hydrogen, a carboxyl group, and an amino group.
Dominador T.
Recommended Textbooks
Chemistry: Structure and Properties
Chemistry The Central Science
Chemistry
Transcript
18,000,000+
Students on Numerade
Trusted by students at 8,000+ universities
Watch the video solution with this free unlock.
EMAIL
PASSWORD