Antimicrobial peptides generally are cysteine-rich, cationic, and amphipathic. 

Because of their positive charge and amphipathic nature, they interact with acidic phospholipids in lipid bilayers, forming pores and disrupting the membranes of bacteria, fungi, parasites, and viruses.

TLS Online TPP Program

#Id: 8511

#Unit 1. Molecules and their Interaction Relevant to Biology

Threading is a computational technique that attempts

to determine the unknown structure of a protein by ascertaining

whether it is consistent with a known protein structure.

TLS Online TPP Program

#Id: 8512

#Unit 1. Molecules and their Interaction Relevant to Biology

Prediction of the structure of a protein based only on its chemical and physical properties is done by ab initio (from the beginning) methods is the Rosetta program

TLS Online TPP Program

#Id: 4333

#Unit 1. Molecules and their Interaction Relevant to Biology

About 75% of the charged residues in proteins are members of ion pairs that are located mostly on the protein surface.

Despite the strong electrostatic attraction interactions contribute little to the stability of a native protein.

TLS Online TPP Program

#Id: 4356

#Unit 1. Molecules and their Interaction Relevant to Biology

The overall probability of RNase A re-forming its four native disulfide links at random is-

TLS Online TPP Program

#Id: 4385

#Unit 1. Molecules and their Interaction Relevant to Biology

Proteins fold to their native conformations via directed pathways rather than stumbling on them through random conformational searches.

TLS Online TPP Program

#Id: 8749

#Unit 1. Molecules and their Interaction Relevant to Biology

Intrinsically disordered proteins lack a hydrophobic core, and have high densities of charged amino acid residues such as Lys, Arg, and Glu. Pro residues are also prominent, as they tend to disrupt ordered structures.