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Mutations

Mutations

Mutations

Mutations

Mutations are changes in the sequence of DNA. These changes can occur spontaneously or they can be induced by exposure to environmental factors. Mutations can be characterized in a number of different ways: whether and how they alter the amino acid sequence of the protein, whether they occur over a small or large area of DNA, and whether they occur in somatic cells or germline cells.
Chromosomal Alterations Are Large-Scale Mutations
While point mutations are changes in a single nucleotide in...

Protein Denaturation

Protein Denaturation

The function of proteins depends on their native three-dimensional structure, which is dictated by the amino acid sequence of the specific protein. Folding of the polypeptide chain takes place under specific conditions that energetically favor the folded conformation. In contrast, protein denaturation occurs spontaneously under unfavorable conditions that disrupt the integrity of the folded conformation. Thus, the chemical and physical environment of a protein, such as significant changes in pH...

Mutations in Microorganisms

Mutations in Microorganisms

Mutations are heritable changes in an organism’s genome involving alterations in the base sequence of DNA or RNA. These changes can influence cellular processes and phenotypic traits, potentially transforming the unaltered wild type into a mutant form. Such changes, termed forward mutations, are pivotal in shaping the genetic diversity of organisms.RNA viruses exhibit the highest mutation rates due to the absence of robust proofreading mechanisms during genome replication. In contrast,...

Lysosomal Hydrolases

Lysosomal Hydrolases

Lysosomes are the site for the degradation of macromolecules and biological polymers released during membrane trafficking events such as secretory, endocytic, autophagic, and phagocytic pathways. The membrane-enclosed area of the lysosome, called the lumen, contains hydrolytic enzymes active in an acidic environment. These acid hydrolases are functional at a pH between 4.5 and 5 and are involved in cellular processes such as cell signaling, energy metabolism, restoration of the plasma membrane,...

Spontaneous and Induced Mutations

Spontaneous and Induced Mutations

Spontaneous mutations arise infrequently during DNA replication due to errors in the process. A key factor behind these errors is tautomeric shifts in nitrogenous bases, where bases transition from keto to enol forms or amino to imino forms. This shift can alter base-pairing rules, leading to mutations. Additionally, reactive oxygen species (ROS) arising from aerobic metabolism can damage DNA, resulting in depurination (loss of a purine base) or depyrimidination (loss of a pyrimidine base).

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Single-mutation-induced stability loss in protein lysozyme.

L Ye¹, Z Wu, M Eleftheriou

¹Department of Computer Science, Zhejiang University, Hangzhou 310027, People's Republic of China.

Biochemical Society Transactions

|November 23, 2007

Summary

A single mutation in hen's egg white lysozyme (W62G) disrupts protein stability by breaking crucial long-range interactions. Molecular dynamics simulations reveal Trp(62) acts as a key structural bridge, essential for protein folding and stability.

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Area of Science:

Protein Biochemistry
Structural Biology
Computational Biophysics

Background:

Single residue mutations can significantly impact protein stability and function.
Understanding the molecular mechanisms behind protein destabilization is crucial for protein engineering and drug design.

Purpose of the Study:

To elucidate the molecular mechanism by which a W62G mutation in hen's egg white lysozyme leads to loss of protein stability.
To investigate the role of Trp(62) in mediating long-range interactions and stabilizing the protein structure.

Main Methods:

Large-scale molecular modeling and extensive molecular dynamics (MD) simulations (10+ micros) in 8 M urea.
Application of a novel wavelet method for analyzing local structural clusters in wild-type and mutant folding trajectories.

Main Results:

The wild-type protein features a Trp(62) residue acting as a crucial bridge, forming an Arg-Trp-Arg 'sandwich-like' structure via pi-type hydrogen bonds and pi-cation interactions.
This bridging structure facilitates cooperative long-range interactions, extending to other clusters like Trp(111) through Arg(112), thereby stabilizing the wild-type protein.
The W62G mutant lacks this bridging effect, exhibits fewer local clusters and contacts, leading to a significantly less stable structure.

Conclusions:

The Trp(62) residue is essential for maintaining the cooperative long-range interactions and overall stability of hen's egg white lysozyme.
The W62G mutation disrupts these interactions by eliminating the key bridging role of Trp(62), resulting in protein destabilization.
These findings provide a detailed molecular explanation for the experimental observations, highlighting the importance of specific residue interactions in protein structure and stability.