n →π* Interactions Modulate the Properties of Cysteine Residues and Disulfide Bonds in Proteins
Noncovalent interactions are ubiquitous in biology, taking on roles that include stabilizing the conformation of and assembling biomolecules, and providing an optimal environment for enzymatic catalysis. Here, we describe a noncovalent interaction that engages the sulfur atoms of cysteine residues a...
| Main Authors: | , |
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| Other Authors: | |
| Format: | Article |
| Language: | English |
| Published: |
American Chemical Society (ACS),
2020-06-01T16:41:51Z.
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| Subjects: | |
| Online Access: | Get fulltext |