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Understanding Macromolecular Behavior in Electric, Magnetic, and Centrifugal Fields, Slides of Physical Chemistry

The fundamental principles of macromolecular structure and dynamics, focusing on the behavior of biological macromolecules in various fields. Topics include the chemistry of macromolecules, their primary, secondary, tertiary, and quaternary structures, molecular interactions, and the role of water in macromolecular systems. The document also discusses symmetry relationships between molecules and the importance of weak interactions.

What you will learn

  • What is the difference between primary, secondary, tertiary, and quaternary structures of macromolecules?
  • How do weak interactions contribute to the stability of macromolecules?
  • What are the different types of torsion and dihedral angles in macromolecules?
  • What role does water play in macromolecular systems?
  • How do symmetry relationships apply to macromolecules?

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2021/2022

Uploaded on 02/03/2022

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Biological macromolecules, protein, RNA, DNA & polysaccharides
Provides a description of their structures at various levels, from the
atomic level to large multisubunit assemblies.
Their behavior in electric, magnetic, or centrifugal fields
Basic principles of structure and structural complexity found in
biological macromolecules.
1.1 Physical properties
Chapter 1
Macromolecular Structure and Dynamics
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Download Understanding Macromolecular Behavior in Electric, Magnetic, and Centrifugal Fields and more Slides Physical Chemistry in PDF only on Docsity!

Biological macromolecules, protein, RNA, DNA & polysaccharidesProvides a description of their structures at various levels, from theatomic level to large multisubunit assemblies.Their behavior in electric, magnetic, or centrifugal fieldsBasic principles of structure and structural complexity found inbiological macromolecules.

Physical properties

Chapter 1

Macromolecular Structure and Dynamics

Chemistry: covalent bonded in specific proportions according to weight or stoichiometryand with unique geometry.

1.1.1 Macromolecules

What is a molecule?

4

The DNA of human chromosome/ tens of billions of atoms25 residues/ oligomersDNA condensing j-protein of the virus g4/24 aa

What is considered to be large?

Monomers: building blocks (aa/sugars) polymerized to a macromolecule

.

Primary structure (

: linear arrangement/ colvent linked polymer

Secondary structure (

: local regular structure, helical structures

Tertiary

structure

3-D

topology

of

the

molecule,

functional

molecule

structure. domain, motif etc. Quaternary structure (

: multiple distinct polymers (or subunit) that form a

functional comples. Tetramer, dimer etc.

1.1.2 Configuration and Conformation

Conformation

Configuration

The

arrangement

of atoms or groups of atoms in a molecule is

described by the terms configuration and conformation.

The position of groups around one or more nonrotating

bonds or around chiral centers

Configuration

To change the configuration of a molecule, chemical

bonds must be broken and remade.

Ex.

cis

  • or

trans

-configurations

anti clockwise

defined

as

an

atom

having

no

plan

or

center

of

symmetry.

Ex:

L

D

-stereoisomer of a chiral molecule

The Stereochemistry of monomers

Most biological macromolecules are chrial moleculesL- and D-glyceraldehydeL-: rotate in an anti-clockwise direction around the chrial carbon.D-: rotate in a clockwise direction around the chrial carbon.Biopolymers are typically constructed from only one enantimer (L form)of the monomer building block.

Amino acid / the chiral center is the carbon directly adjacent to the carboxylic acid (the

C

α

-carbon)

Counter Clockwise/ S

The Stereochemistry of monomers

Clockwise/ R

Conformation of molecules

The rotation around a single bond is described by torsion angle

θ

of the

atoms around the bound A-B-C-D

Torsion angle: “

θ

(-

°

to +

°

)

Dihedral angle “

φ

(

°

to +

°

)

Properly folded conformation of a protein ⇒

native conformation

functional form

Unfolded or denatured conformation ⇒

nonfunctional

proteolysis by the cell

Weak interactions

Conformation of a macromolecule is stabilized by

weak interactions

with

energies of formation that are at least one order of magnitude less than thatof a covalent bond.

Distance-dependent interactionsInversely proportional to the distance r (or r2, r3 etc)

Weak interactions

Longer range interactions charge-charge

α

1/r

charge-dipole

α

1/r

2

dipole-dipole

α

1/r

3

Short range interactions dipole-induced dipole interaction (dispersion)

α

1/r

4

dispersion (very short-range interaction ~1nm)

α

1/r

6

steric repulsion

α

1/r

12

Longer-range interactions (charge-charge, charge-dipole and dipole-dipole)are dependent on the intervening medium, shielded in a polar medium andweakened.The least polarizable medium is

vacuum

dielectric constant of k

ε

o = 4

π

8.85 x 10

C

2

/J m (D)=

Inversely related to the dielectric of the mediumWeakened in a highly polarizable medium such as

water

(~80D).

Dielectric constant/ the environment factor in stabilizing the conformation of amacromolecule.How the environment affects the weak interactions2 additional interactions (hydrogen bonds & hydrophobicity)

Longer-range interaction

Biological system70% water, aqueous solution, dilute aqueous solution Membranes Nonaqueous environment,For protein that are integral parts of the bilayer of the membranesex: TATA-binding proteinAn important aromatic interaction between a

Phe

of protein and the

1.3 The Environment in the Cell nucleotide base of the bound DNA.Represent an important nonaquous enviroment Solvent molecules Water (ex: between protein and its bound DNA)often helps to mediate interaction,treated as part of the macromolecule rater than part of the bulk solvent.