By Arvind Kumar Misra
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Additional info for Fundamentals of Cell and Molecular Genetics
2 Tertiary structure of proteins Tertiary structure of a protein refers to the relative arrangement of various domains of the polypeptides. The regions that are far apart in the primary chain may be brought close to each other in the tertiary folding of the polypeptide chain. Tertiary structure also generates specific relative locations of various side chains of the amino acids present in the polypeptide chain. This relative localization of the side chains creates various structural and functional domains of proteins.
3: Generalised scheme for addition of polyA tail in eukaryotic hnRNA processing. 3 Removal of introns and splicing Two groups of introns are generally recognised. First group of introns need additional machinery for removal and splicing of associated exons. I shall call them as „assisted splicing introns‟. Second group of introns is called as „self splicing introns‟ because they have inbuilt catalytic activity for auto-removal and splicing of associated exons. 1 Assisted splicing introns Splicing of exons in this group of introns in most eukaryotes needs splicing machinery called as „spliceosome‟.
3 d, e). These strands align with each other in parallel or anti-parallel manner to create sheets. strands in a sheet are held together with the help of hydrogen bonds. Hydrogen bonds give rise to polarity in polypeptides. For example, the amino-terminal of a helix has more positive charge while the c-terminal is relatively negatively charged. This dipolar nature of polypeptides coupled with the Amino acids, polypeptides and proteins 49 properties of R groups give rise to several interactive properties of polypeptides, making them extremely versatile macromolecules capable of freely interacting among themselves as well as with other macromolecules of the cells.
Fundamentals of Cell and Molecular Genetics by Arvind Kumar Misra