lecturenoteschap4-09-4slides

lecturenoteschap4-09-4slides - BCMB 3100: Partial notes...

Info iconThis preview shows pages 1–4. Sign up to view the full content.

View Full Document Right Arrow Icon
1 1 BCMB 3100: Partial notes Chapter 4 (Part 1) Diversity of proteins 3D structure of proteins Fibrous vs globular proteins Conformation vs configuration 1°, 2°, 3° and 4° structure Peptide groups in polypeptide vs angles, Ramachandran plot helix vs -sheet 2 Diversity of proteins ________________ - study of large sets of proteins, such as the entire complement of proteins produced by a cell E. coli has about _________ different polypeptides (average size 300 amino acids, M r 33,000) • Fruit fly ( Drosophila melanogaster ) about 16,000, humans, other mammals about 40,000 different polypeptides 3 E. coli proteins on 2D gel electrophoresis E. coli expresses ~4000 proteins Page 85 4 3D STRUCTURE OF PROTEINS Two classes of proteins: ________________: water insoluble, static, "tough", extended, provide mechanical support ( -keratin, collagen) _______________: compact, "spherical", usually: hydrophobic interior & hydrophilic exterior enzymes
Background image of page 1

Info iconThis preview has intentionally blurred sections. Sign up to view the full version.

View Full DocumentRight Arrow Icon
2 5 Diversity of proteins 3D structure of proteins Fibrous vs globular proteins Conformation vs configuration 1°, 2°, 3° and 4° structure Peptide groups in polypeptide vs angles, Ramachandran plot helix vs -sheet BCMB 3100: Partial notes for Chapter 4 6 The biological activity of a protein depends on its conformation _______________: spatial arrangement of substituent groups that are free to assume different positions in space, without breaking any bonds, because of the freedom of bond rotation The number of potential conformations of a protein is _____________. Under physiological conditions the protein assumes a single stable shape: native conformation ________________: a spatial arrangement of atoms that can not be changed without breaking covalent bonds 7 Levels of Protein Structure __________________: the covalent backbone of a polymer ___________________: the residue-by-residue conformation of the backbone of a polymer ___________________: the 3D conformation of a polymer in its native folded state ___________________: the 3D structure of a multisubunit, particularly the manner in which the subunits fit together Supersecondary structure: clusters of secondary structure (e.g.  ) Domain: a distinct structural unit of a polypeptide; domains have separate functions and may fold as independent, compact units 8 Fig. 4.1 Levels of protein structure
Background image of page 2
3 9 Diversity of proteins 3D structure of proteins Fibrous vs globular proteins Conformation vs configuration 1°, 2°, 3° and 4° structure Peptide groups in polypeptide vs angles, Ramachandran plot helix vs -sheet BCMB 3100: Partial notes for Chapter 4 10 Fig. 4.5 Resonance structure of the peptide bond (a) Peptide bond shown as a C-N single bond (b) Peptide bond shown as a double bond (c) Actual structure is a hybrid
Background image of page 3

Info iconThis preview has intentionally blurred sections. Sign up to view the full version.

View Full DocumentRight Arrow Icon
Image of page 4
This is the end of the preview. Sign up to access the rest of the document.

This note was uploaded on 12/03/2011 for the course CHEM 3100 taught by Professor Dervartanian during the Fall '09 term at University of Georgia Athens.

Page1 / 27

lecturenoteschap4-09-4slides - BCMB 3100: Partial notes...

This preview shows document pages 1 - 4. Sign up to view the full document.

View Full Document Right Arrow Icon
Ask a homework question - tutors are online