Substrate binding induces conformational changes that optimize catalysis.
Myoglobin has a high oxygen affinity and releases oxygen only at low oxygen tension.
pI = (2.34 + 9.60)/2 = 5.97.
Hydroxyproline stabilizes the collagen triple helix through hydrogen bonding.
Tryptophan and tyrosine absorb ultraviolet light strongly near 280 nm.
RNase A spontaneously refolded after denaturation, proving sequence determines structure.
Hydrophobic residues at heptad repeat positions interlock to stabilize the coiled-coil.
Amphipathic helices possess hydrophobic and hydrophilic faces suited for membrane environments.
Domains are independently folded structural units within one polypeptide.
Burying hydrophobic residues releases ordered water molecules, increasing entropy.
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