3381 Lec 11: Tertiary and Quaternary Structures
Tertiary Structure of Globular proteins
For globular proteins.
Hydrophobic side chains inside, polar side chains on surface
Interiors are densely packed (75% of space occupied)
Secondary structures (alpha an
3381 Proteins Lec 8. Protein Chemistry, Sequence Analysis and Evolution
Techniqus in Protein Chemistry and Protein Sequencing
Now a days it is rare to determine the entire sequence, but some techniques remain
The complete amino acid sequence of a
3381 Lecture 12: Protein Stability
the 3D structure, the conformation of a protein is essential for its activity.
Nascent polypeptide must assume this conformation.
Protein folding: conversion of the unfolded (U) form to the native folded (N) form
3381 Lecture 7: Protein Analysis: Electrophoresis, Mass Spectrometry, Analytical
It is the migration of ions in an electric field.
High resolution but low capacity, preparative not good but if trying to analyze low
3381 Lecture 4: Amino Acids
Proteins are made from alpha amino acids because they have a primary amino group as
a substituent of the alpha carbon atom, the carbon next to the carboxylic acids.
Only L amino acids are used in protein synthesis
The 20 amino
3381 Proteins Lec. 13 How do Proteins Fold?
Not well understood, many ways to view it
Hierarchical folding, some areas of secondary structure may form, followed by
coalescence into native structure
Fold in less than a few second.
Proteins fold to their na
3381 Proteins Lec 9. Steric Constraint and Secondary Structure
A polypeptide is a polymer of amino acid residues linked by amide (peptide) bonds.
Primary, secondary, tertiary and quaternary structures.
Quaternary structure-> multi subunit proteins.
Lecture 10 Biochem 3381 Fibrous Porteins, Crystallography and NMR
Fibrous proteins: coiled coils and collagen
Alpha keratin is the major protein of skin, hair, nails etc. It consists of bundles of helices
arranged as dimers, protofilaments and microfibril
Lecture 5: Biochem Primary Structure- Protein Purification 1
Theoretically there are 20 different choices available for each amino acid residue in a
polypeptide chain, it is easy to see that a huge number of diffe
3381: Lecture 13, Membrane Proteins
Integral vs Peripheral
Integral: embedded in the lipid bilayerusually required detergent to extract from
They associate tightly with membrane through hydrophobic interactions and can be
separated from membranes
3381 Proteins Lecture 6 Protein Purification II
Solubility, Salting out, etc
Fractionations Based on solubility- adjust conditions or add a precipitant that causes
some proteins to become less soluble and come out solution. A little bit of salt cause
Biochem Lecture 2: Water Properties and Interactions
The Structure of Water
Water properties are essential to its structure and function.
Consists of two H atoms bonded to an oxygen atom.
O-H distance of 0.958 A and the angle formed by the three atoms is