Jove
Visualize
Contact Us
JoVE
x logofacebook logolinkedin logoyoutube logo
ABOUT JoVE
OverviewLeadershipBlogJoVE Help Center
AUTHORS
Publishing ProcessEditorial BoardScope & PoliciesPeer ReviewFAQSubmit
LIBRARIANS
TestimonialsSubscriptionsAccessResourcesLibrary Advisory BoardFAQ
RESEARCH
JoVE JournalMethods CollectionsJoVE Encyclopedia of ExperimentsArchive
EDUCATION
JoVE CoreJoVE BusinessJoVE Science EducationJoVE Lab ManualFaculty Resource CenterFaculty Site
Terms & Conditions of Use
Privacy Policy
Policies

Related Concept Videos

Protein Denaturation01:28

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...
Blood Transfusion and Agglutination02:45

Blood Transfusion and Agglutination

Blood transfusion is a therapeutic measure to restore the blood volume after extensive blood loss due to an accident or a medical procedure. Blood transfusion involves drawing a certain amount of blood from a suitable donor and infusing it into the recipient.
History
The history of blood transfusion dates back to the 17th century, when early attempts were made in animals. In 1818 James Blundell, a British doctor, performed the first successful human blood transfusion. Later in 1900, Karl...
Globular Proteins01:27

Globular Proteins

In organisms, proteins are the most abundant macromolecules. They act as the building blocks of life and play various crucial roles in the body. Proteins can be broadly classified into two distinct subtypes based on their shape and solubilities: globular proteins and fibrous proteins.
Globular proteins serve many important physiological functions, such as acting as enzymes, cellular messengers, and molecular transporters. These roles often require the proteins to be soluble in the aqueous...
Decreased Body Temperature01:29

Decreased Body Temperature

A decreased body temperature can occur in patients with hypothermia and frostbite. Heat loss with extended cold exposure overpowers the body's ability to create heat, resulting in hypothermia. Core temperature readings help classify hypothermia. Mild hypothermia is temperatures between 32 °C (89.6 °F) and 35°C (95 °F) and is caused by impaired thermoregulation. Moderate hypothermia is temperatures between 28 C (82.4 °F) and 32 °C (89.6 °F) caused by sustained extreme cold exposure, and severe...
Conjugated Proteins02:50

Conjugated Proteins

Simple proteins and protein complexes contain only amino acids. In contrast, many other proteins, called conjugated proteins, covalently bond with non-protein moieties.
Nucleoproteins are protein complexes that contain nucleic acids, categorized as deoxyribonucleoproteins (DNPs) or ribonucleoproteins (RNPs) respectively. The nucleosome is a typical example of a DNP where nuclear DNA is associated with histone proteins. The major antigen for the Covid-19 virus SARS-CoV is an RNP that is critical...
Hemoglobin01:24

Hemoglobin

Hemoglobin is a globular protein made up of four subunits. Two of these subunits are alpha chains, and the other two are beta chains. Each subunit contains a molecule of heme, which has an iron atom and can bind to oxygen. When an oxygen molecule binds to one heme group, it changes the shape of hemoglobin, making it easier for the other heme groups to bind oxygen as well.
When all four heme groups are bound to oxygen, the resulting molecule is called oxyhemoglobin. As a result, arterial blood...

You might also read

Related Articles

Articles linked to this work by shared authors, journal, and citation graph.

Sort by
Same author

Synovial fluid Lipocalin-2 as a biomarker for chronic prosthetic joint infection: Prospective validation in hip and knee revision arthroplasty.

Revista espanola de cirugia ortopedica y traumatologia·2026
Same author

Synovial fluid Lipocalin-2 as a biomarker for chronic prosthetic joint infection: Prospective validation in hip and knee revision arthroplasty.

Revista espanola de cirugia ortopedica y traumatologia·2026
Same author

Clinical Outcomes of Intra-Abdominal Candidiasis by Initial Antifungal Therapy.

Mycoses·2026
Same author

Assessing short- and medium-term fluctuations of EEG spectral content in Minimally Conscious State patients.

Annual International Conference of the IEEE Engineering in Medicine and Biology Society. IEEE Engineering in Medicine and Biology Society. Annual International Conference·2025
Same author

Impact of latency jitter correction on offline P300-based classification: a preliminary study for BCI applications in MCS patients.

Annual International Conference of the IEEE Engineering in Medicine and Biology Society. IEEE Engineering in Medicine and Biology Society. Annual International Conference·2025
Same author

The role of intralaminar damages on the delamination evolution in laminated composite structures.

Heliyon·2023
Same journal

Genomic analysis of Desulfobulbaceae strain B35, a new hydrothermal vent species of mesophilic bacterium that disproportionates sulfur and respires Fe(III).

Marine genomics·2026
Same journal

Complete genome sequencing reveals the carbohydrate-degrading potential of Leeuwenhoekiella obamensis LY010 isolated from the Kuroshio Extension in the Northwestern Pacific.

Marine genomics·2026
Same journal

Complete genome sequences of two strains of Shewanella sp. FeAMO and Shewanella sp. JL219SE-S6 isolated from deep-sea hydrothermal sediments.

Marine genomics·2026
Same journal

Whole-genome sequencing uncovers the extreme adaptation mechanisms of Pseudomonas sp. Ma2-10 screened from the Antarctic sea sediment near King George Island.

Marine genomics·2026
Same journal

The first transcriptome of the diaphanous deep-sea hatchetfish Sternoptyx diaphana Hermann, 1781 (Teleostei: Sternoptychidae).

Marine genomics·2026
Same journal

Genomic analysis of Tenacibaculum sp. IMCC1 reveals its genetic potential for chitin degradation.

Marine genomics·2026
See all related articles

Related Experiment Video

Updated: May 30, 2026

Strategies for Study of Neuroprotection from Cold-preconditioning
16:27

Strategies for Study of Neuroprotection from Cold-preconditioning

Published on: September 2, 2010

Hemoproteins in the cold.

C Verde1, D Giordano, R Russo

  • 1Institute of Protein Biochemistry, CNR, Via Pietro Castellino 111, I-80131 Naples, Italy.

Marine Genomics
|July 30, 2011
PubMed
Summary
This summary is machine-generated.

This review explores the biochemistry of cold-adapted hemoproteins in fish and bacteria. It specifically discusses heme hexacoordination involving internal amino acid residues in these proteins.

More Related Videos

LabVIEW-operated Novel Nanoliter Osmometer for Ice Binding Protein Investigations
09:32

LabVIEW-operated Novel Nanoliter Osmometer for Ice Binding Protein Investigations

Published on: February 4, 2013

HeLa Based Cell Free Expression Systems for Expression of Plasmodium Rhoptry Proteins
09:03

HeLa Based Cell Free Expression Systems for Expression of Plasmodium Rhoptry Proteins

Published on: June 10, 2015

Related Experiment Videos

Last Updated: May 30, 2026

Strategies for Study of Neuroprotection from Cold-preconditioning
16:27

Strategies for Study of Neuroprotection from Cold-preconditioning

Published on: September 2, 2010

LabVIEW-operated Novel Nanoliter Osmometer for Ice Binding Protein Investigations
09:32

LabVIEW-operated Novel Nanoliter Osmometer for Ice Binding Protein Investigations

Published on: February 4, 2013

HeLa Based Cell Free Expression Systems for Expression of Plasmodium Rhoptry Proteins
09:03

HeLa Based Cell Free Expression Systems for Expression of Plasmodium Rhoptry Proteins

Published on: June 10, 2015

Area of Science:

  • Biochemistry
  • Molecular Biology
  • Structural Biology

Background:

  • Cold-adapted organisms possess unique biochemical adaptations to survive in low-temperature environments.
  • Hemoproteins, crucial for various biological processes, exhibit altered structures and functions in cold-adapted species.
  • Understanding these adaptations is key to fields like cryobiology and biotechnology.

Purpose of the Study:

  • To review the biochemical characteristics of hemoproteins from cold-adapted fish and bacteria.
  • To focus on the specific structural feature of heme hexacoordination in these proteins.
  • To provide insights into the molecular mechanisms underlying cold adaptation.

Main Methods:

  • Literature review of existing studies on cold-adapted hemoproteins.
  • Analysis of structural data related to heme hexacoordination.
  • Comparative biochemistry of hemoproteins across different temperature adaptations.

Main Results:

  • Cold-adapted hemoproteins often display modified heme environments.
  • Heme hexacoordination, with the sixth ligand from an internal amino acid, is a notable feature.
  • This structural arrangement likely contributes to protein stability and function at low temperatures.

Conclusions:

  • Internal amino acid-mediated heme hexacoordination is a significant adaptation in cold-adapted hemoproteins.
  • This structural motif may enhance enzymatic activity and stability in cold conditions.
  • Further research into these hemoproteins could yield biotechnological applications.