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Related Concept Videos

From DNA to Protein03:06

From DNA to Protein

The flow of genetic information in cells from DNA to mRNA to protein is described by the central dogma, which states that genes specify the sequence of mRNAs, which in turn specify the sequence of amino acids making up all proteins. The decoding of one molecule to another is performed by specific proteins and RNAs. Because the information stored in DNA is so central to cellular function, it makes intuitive sense that the cell would make mRNA copies of this information for protein synthesis...
Prokaryotic Gene Structure and Organization01:28

Prokaryotic Gene Structure and Organization

Prokaryotic genomes exhibit a streamlined organization of coding and non-coding regions essential for gene expression and protein synthesis. While coding regions contain the genetic instructions for proteins or functional RNAs, non-coding regions regulate the precise transcription and translation of these genes.Coding Regions: Proteins and RNAsThe primary coding regions, known as structural genes, include sequences transcribed into messenger RNA (mRNA) and ultimately translated into...
Signal Sequences and Sorting Receptors01:41

Signal Sequences and Sorting Receptors

Signal sequences are short amino acid sequences that guide newly synthesized proteins to their proper location within the cell. Classical signal sequences are fifteen to sixty amino acids long and present at the N-terminus of a polypeptide chain. Each signal sequence has a conserved segment of basic residues towards their N terminus, a hydrophobic core, and a C-terminus rich in polar residues. The C-terminus also contains a signal cleavage site and features a -3 -1 sequence motif. The -3-1...
Structural Protein Function01:56

Structural Protein Function

Structural proteins are a category of proteins responsible for functions ranging from cell shape and movement to providing support to major structures such as bones, cartilage, hair, and muscles. This group includes proteins such as collagen, actin, myosin, and keratin.
Collagen, the most abundant protein in mammals, is found throughout the body. In connective tissue, such as skin, ligaments, and tendons, it provides tensile strength and elasticity.  In bones and teeth, it mineralizes to form...
Structural Protein Function01:56

Structural Protein Function

Structural proteins are a category of proteins responsible for functions ranging from cell shape and movement to providing support to major structures such as bones, cartilage, hair, and muscles. This group includes proteins such as collagen, actin, myosin, and keratin.
Collagen, the most abundant protein in mammals, is found throughout the body. In connective tissue, such as skin, ligaments, and tendons, it provides tensile strength and elasticity.  In bones and teeth, it mineralizes to form...
Protein Folding01:22

Protein Folding

Overview

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Updated: Jun 18, 2026

Residue-Specific Exchange of Proline by Proline Analogs in Fluorescent Proteins: How "Molecular Surgery" of the Backbone Affects Folding and Stability
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Residue-Specific Exchange of Proline by Proline Analogs in Fluorescent Proteins: How "Molecular Surgery" of the Backbone Affects Folding and Stability

Published on: February 3, 2022

A minimal sequence code for switching protein structure and function.

Patrick A Alexander1, Yanan He, Yihong Chen

  • 1Center for Advanced Research in Biotechnology, University of Maryland Biotechnology Institute, Rockville, MD 20850, USA.

Proceedings of the National Academy of Sciences of the United States of America
|November 20, 2009
PubMed
Summary
This summary is machine-generated.

This study reveals how proteins evolve new structures and functions through sequential mutations. A single amino acid change can switch a protein

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Area of Science:

  • Protein engineering and structural biology.
  • Investigating protein folding and conformational changes.
  • Exploring evolutionary pathways of protein function.

Background:

  • Understanding protein structure-function relationships is crucial.
  • Few studies explore gradual protein evolution via mutations.
  • Existing models lack detailed mechanistic insights into fold switching.

Purpose of the Study:

  • To describe mutation-driven protein fold and function transitions.
  • To map the mutational pathway between two distinct protein folds and functions.
  • To elucidate the mechanism of conformational switching.

Main Methods:

  • Designed two proteins with similar sequences but different folds and functions.
  • Analyzed mutational pathways using stability assays and NMR spectroscopy.
  • Determined high-resolution structures of key mutants.

Main Results:

  • Demonstrated transformation of an IgG-binding (4beta+alpha fold) to an albumin-binding (3-alpha fold) protein.
  • Identified a mutational pathway preserving structure and function.
  • Showed a single amino acid substitution can induce a complete fold switch.
  • Discovered a bifunctional intermediate with affinity for both IgG and albumin.

Conclusions:

  • Protein fold and function can evolve gradually through point mutations.
  • Conformational switching can be mediated by single amino acid substitutions.
  • Intermediate states can exhibit dual functions, providing evolutionary flexibility.