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Related Concept Videos

Protein Families02:47

Protein Families

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Protein families are groups of homologous proteins; that is, they have similarities in amino acid sequences and three-dimensional structures. Protein families usually occur because of gene duplication, where an additional copy of a gene is inserted into the genome of an organism.   Mutations that change the amino acids but still allow the protein to be properly synthesized, will lead to new protein family members.   If these new proteins contain similar amino acids in key...
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Proteins are one of the most abundant organic molecules in living systems and have the most diverse range of functions of all macromolecules. Proteins may be structural, regulatory, contractile, or protective. They may serve in transport, storage, or membranes; or they may be toxins or enzymes. Their structures, like their functions, vary greatly. They are all, however, amino acid polymers arranged in a linear sequence.
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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.
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Gene Families01:57

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Gene families consist of groups of genes proposed to have originated from a common ancestor. Typically these arise through events in which a gene or genes are mistakenly duplicated during cell division. Unlike their parent genes (which are subject to selection pressure to maintain function), these gene copies do not need to preserve their sequences and may evolve at a relatively faster rate.
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Globular and Fibrous Proteins02:21

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Many proteins can be classified into two distinct subtypes - globular or fibrous. These two types differ in their shapes and solubilities.
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Measurement of Heme Synthesis Levels in Mammalian Cells
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Variation in protein structure and function: Primate hemoglobins.

B Sullivan1

  • 1Department of Biochemistry, Duke Medical Center and Duke Marine Laboratory, 28516, Beaufort, North Carolina, USA.

Journal of Molecular Evolution
|November 1, 2013
PubMed
Summary
This summary is machine-generated.

Structural variations in primate hemoglobins correlate with functional differences, suggesting natural selection drives these changes for improved fitness, not random genetic drift.

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Area of Science:

  • Evolutionary biology
  • Molecular evolution
  • Primate genetics

Background:

  • Hemoglobin structure and function are critical for oxygen transport.
  • Primate hemoglobin evolution exhibits significant diversity.
  • Understanding evolutionary mechanisms is key to molecular biology.

Purpose of the Study:

  • To investigate the relationship between structural variations and functional differences in primate hemoglobins.
  • To evaluate the role of natural selection versus genetic drift in shaping hemoglobin evolution.

Main Methods:

  • Comparative analysis of primate hemoglobin sequences.
  • Functional assays to assess hemoglobin properties.
  • Phylogenetic analysis to infer evolutionary history.

Main Results:

  • Primate hemoglobin structural variations are directly linked to functional variations.
  • Evidence supports adaptive evolution driven by natural selection.
  • The study refutes the neutral theory as the primary driver for these substitutions.

Conclusions:

  • Natural selection is the predominant force behind observed substitutions in primate hemoglobins.
  • Functional advantages conferred by structural changes likely led to their fixation.
  • Evolutionary changes in hemoglobin are adaptive rather than neutral.