In fact, most successful protein designs have involved globular proteins.

The relationship of structure to function in fibrous and globular proteins.

These studies have shown that the folding of globular proteins affects its function.

Beta-sheets are very common in globular proteins and most contain less than six strands.

Enzymes are generally globular proteins, acting alone or in larger complexes.

Globular proteins are a common type of protein.

Among the most known globular proteins is Hemoglobin, a member of the globin protein family.

Almost all globular proteins are soluble and many are enzymes.

For example, 2-chloroethanol causes an increase in a-helix content in globular proteins.

In opposite case chaotropic salts force globular proteins to unfold.

Describe the main structural classes of globular proteins.

Outline the difference between fibrous and globular proteins, with reference to two examples of each protein type.

However, albumins are also globular proteins, but are not globulins.

In structure, they are large Y-shaped globular proteins.

Having proposed a model of globular proteins, Wrinch investigated whether it was consistent with the available structural data.

The globins are a family of globular proteins, which are thought to share a common ancestor.

In their model, the lipid bilayer was coated on either side with a layer of globular proteins.

Scleroproteins tend not to denature as easily as globular proteins.

Content: Nearly all biochemical reactions are catalysed by globular proteins called enzymes.

Regulation of other molecules is also done by globular proteins rather than fibrous proteins.

The model describes a phospholipid bilayer that lies between two layers of globular proteins.

Hemoglobin has a quaternary structure characteristic of many multi-subunit globular proteins.

Regulatory roles are also performed by globular proteins rather than fibrous proteins.

They are cysteine-rich globular proteins containing five disulfide bonds.

Because globular proteins have very complex shapes this makes them ideal for their role as enzymes because they can be highly specific.

Globular proteins or spheroproteins are spherical ("globe-like") proteins and are one of the common protein types (the others being fibrous, disordered and membrane proteins).

Globular proteins are a type of protein commonly found in all living organisms.

These studies have shown that the folding of globular proteins affects its function.

There are three ordered layers to destrin which is a globular protein.

It is a 275-residue globular protein with several alpha-helices, and a large beta-sheet.

Among the most known globular proteins is Hemoglobin, a member of the globin protein family.

Almost all globular proteins are soluble and many are enzymes.

The cyclol hypothesis is the first structural model of a folded, globular protein.

Most globular proteins are readily soluble in water or dilute salt solutions.

The term "globulin" is sometimes used synonymously with "globular protein".

The globins are a family of globular proteins, which are thought to share a common ancestor.

In structure, they are large Y-shaped globular proteins.

Having proposed a model of globular proteins, Wrinch investigated whether it was consistent with the available structural data.

However, albumins are also globular proteins, but are not globulins.

A few examples of globular proteins include enzymes, myoglobin and hemoglobin.

Scleroproteins tend not to denature as easily as globular proteins.

NCS-1 is a globular protein consisting of ten alpha-helices.

Tubulin is one of several members of a small family of globular proteins.

In their model, the lipid bilayer was coated on either side with a layer of globular proteins.

Globular proteins tend to denature more easily than fibrous proteins.

Using pepsin, they were the first to discern the diffraction pattern of a wet, globular protein.

Regulatory roles are also performed by globular proteins rather than fibrous proteins.

Such high glycine and regular repetitions are never found in globular proteins save for very short sections of their sequence.

Hemoglobin has a quaternary structure characteristic of many multi-subunit globular proteins.

They are cysteine-rich globular proteins containing five disulfide bonds.

Whey protein is the name of globular proteins that can be isolated from whey.