Related Experiment Video
Updated: Jul 28, 2026
08:58
Characterization of Glycoproteins with the Immunoglobulin Fold by X-Ray Crystallography and Biophysical Techniques
Published on: July 5, 2018
Determining the crystal structure of fibrinogen
1Center for Molecular Genetics, University of California, San Diego, La Jolla, CA 92093-0634, USA. rdoolittle@ucsd.edu
Journal of Thrombosis and Haemostasis : JTH
|April 22, 2004
Summary
This historical sketch reviews the journey toward understanding blood coagulation, highlighting both the triumphs and setbacks in achieving long-term scientific goals.
Area of Science:
- Hematology
- Medical History
Background:
- This article follows a tradition of historical sketches in the Journal of Thrombosis and Haemostasis.
- It draws inspiration from previous works on factor VIII and activated protein C resistance.
Observation:
- The author reflects on the process of scientific discovery in the field of thrombosis and hemostasis.
- The narrative emphasizes the emotional and intellectual journey of researchers.
Findings:
- The sketch captures the excitement and disappointments inherent in pursuing long-term scientific objectives.
- It provides insights into the challenges and rewards of advancing knowledge in hemostasis and thrombosis.
Implications:
- Understanding the history of scientific progress can inform future research directions.
- This historical perspective may inspire researchers facing similar challenges in their work.
Related Concept Videos
01:22Protein Folding
Overview
02:15Protein and Protein Structure
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.
A protein's shape is critical to its function. For example, an enzyme can...
A protein's shape is critical to its function. For example, an enzyme can...
02:21Globular and Fibrous Proteins
Many proteins can be classified into two distinct subtypes - globular or fibrous. These two types differ in their shapes and solubilities.
Globular proteins are also known as spheroproteins and typically are approximately round in shape. They contain a mix of amino acid types and contain differing sequences in their primary structures. Globular proteins have many different functions, such as enzymes, cellular messengers, and molecular transporters. These roles often require the proteins to be...
Globular proteins are also known as spheroproteins and typically are approximately round in shape. They contain a mix of amino acid types and contain differing sequences in their primary structures. Globular proteins have many different functions, such as enzymes, cellular messengers, and molecular transporters. These roles often require the proteins to be...
01:25Protein Folding
Proteins are chains of amino acids linked together by peptide bonds. Upon synthesis, a protein folds into a three-dimensional conformation, critical to its biological function. Interactions between its constituent amino acids guide protein folding, and hence the protein structure is primarily dependent on its amino acid sequence.
Protein Structure Is Critical to Its Biological Function
Proteins perform a wide range of biological functions such as catalyzing chemical reactions, providing...
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00:55Fibrous Proteins
Fibrous proteins are either long and narrow proteins or assemble to form long and thin structures. They contain repetitive units and usually consist of either alpha helices or beta sheets and, in rare cases, a mix of both. The amino acids in the primary structure often consist of repeating amino acid sequences. The role of fibrous proteins is primarily structural. Many are located in the extracellular matrix and are present in connective tissues to impart strength and joint mobility. They are...
01:29Determination of Crystal Structures
In the late 1800s, the revelation that light extended beyond visible wavelengths led to the discovery of X-rays by Wilhelm Roentgen. Recognized as high-energy electromagnetic radiation with short wavelengths, X-rays prompted exploration into their interaction with crystals. Max von Laue proposed in 1912 that the periodic arrangement of atoms, ions, or molecules in crystals would cause them to diffract X-rays, a hypothesis confirmed through experiments with copper sulfate and zinc sulfide...