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Protein Structure and Function

Proteins serve crucial functions in all biological processes by acting as catalysts, transporting molecules, providing structure and immune protection, generating movement, transmitting signals, and controlling growth. Their diverse functions are enabled by several key properties. Proteins are polymers built from amino acids that spontaneously fold into three-dimensional structures determined by their sequence. This allows them to participate in a wide range of activities. Proteins contain various functional groups that account for their broad functions. They can also interact to form complex assemblies with capabilities beyond individual components, like DNA replication machinery. Some proteins are rigid while others are flexible, acting as hinges, springs or levers important to their function and assembly.

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138 views

Protein Structure and Function

Proteins serve crucial functions in all biological processes by acting as catalysts, transporting molecules, providing structure and immune protection, generating movement, transmitting signals, and controlling growth. Their diverse functions are enabled by several key properties. Proteins are polymers built from amino acids that spontaneously fold into three-dimensional structures determined by their sequence. This allows them to participate in a wide range of activities. Proteins contain various functional groups that account for their broad functions. They can also interact to form complex assemblies with capabilities beyond individual components, like DNA replication machinery. Some proteins are rigid while others are flexible, acting as hinges, springs or levers important to their function and assembly.

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Janine Ginog Ferrer
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Protein Structure and Function

Proteins are the most versatile macromolecules in living systems and serve crucial functions in essentially all
biological processes. They function as catalysts, they transport and store other molecules such as oxygen, they
provide mechanical support and immune protection, they generate movement, they transmit nerve impulses, and
they control growth and differentiation. Indeed, much of this text will focus on understanding what proteins do
and how they perform these functions.
Several key properties enable proteins to participate in such a wide range of functions.
1.
Proteins are linear polymers built of monomer units called amino acids. The construction of a vast array
of macromolecules from a limited number of monomer building blocks is a recurring theme in
biochemistry. Does protein function depend on the linear sequence of amino acids? The function of a
protein is directly dependent on its threedimensional structure (Figure 3.1). Remarkably, proteins
spontaneously fold up into three-dimensional structures that are determined by the sequence of amino
acids in the protein polymer. Thus, proteins are the embodiment of the transition from the one-
dimensional world of sequences to the three-dimensional world of molecules capable of diverse
activities.
2.
Proteins contain a wide range of functional groups. These functional groups include alcohols, thiols,
thioethers, carboxylic acids, carboxamides, and a variety of basic groups. When combined in various
sequences, this array of functional groups accounts for the broad spectrum of protein function. For
instance, the chemical reactivity associated with these groups is essential to the function of enzymes, the
proteins that catalyze specific chemical reactions in biological systems (see Chapters 8–10).
3.
Proteins can interact with one another and with other biological macromolecules to form complex
assemblies. The proteins within these assemblies can act synergistically to generate capabilities not
afforded by the individual component proteins (Figure 3.2). These assemblies include macro-molecular
machines that carry out the accurate replication of DNA, the transmission of signals within cells, and
many other essential processes.
4.
Some proteins are quite rigid, whereas others display limited flexibility. Rigid units can function as
structural elements in the cytoskeleton (the internal scaffolding within cells) or in connective tissue.
Parts of proteins with limited flexibility may act as hinges, springs, and levers that are crucial to protein
function, to the assembly of proteins with one another and with other molecules into complex units, and
to the transmission of information within and between cells (Figure 3.3).

Figure
Crystals of human insulin
Insulin is a protein hormone, crucial for maintaining blood sugar at appropriate levels. (Below) Chains of amino
acids in a specific sequence (the primary structure) define a protein like insulin. These chains fold into well-
defined structures (the tertiary structure)—in this case a single insulin molecule. Such structures assemble with
other chains to form arrays such as the complex of six insulin molecules shown at the far right (the quarternary
structure). These arrays can often be induced to form well-defined crystals (photo at left), which allows
determination of these structures in detail.[(Left) Alfred Pasieka/Peter Arnold.]

Figure 3.1
S

Figure 3.1Structure Dictates Function

 A protein component of the DNA replication machinery surrounds a section of DNA double helix. The
structure of the protein allows large segments of DNA to be copied without the replication machinery
dissociating from the DNA.
Figure 3.2

Figure 3.2A Complex Protein Assembly


An electron micrograph of insect flight tissue in cross section shows a hexagonal array of two kinds of protein
filaments. [Courtesy of Dr. Michael Reedy.]

Figure 3.3
Figure 3.3Flexibility and Function

 Upon binding iron, the protein lactoferrin undergoes conformational changes that allow other
molecules to distinguish between the iron-free and the iron-bound forms.
3.1. Proteins Are Built from a Repertoire of 20 Amino Acids
3.2. Primary Structure: Amino Acids Are Linked by Peptide Bonds to Form Polypeptide Chains
3.3. Secondary Structure: Polypeptide Chains Can Fold Into Regular Structures Such as the Alpha Helix, the
Beta Sheet, and Turns and Loops
3.4. Tertiary Structure: Water-Soluble Proteins Fold Into Compact Structures with Nonpolar Cores
3.5. Quaternary Structure: Polypeptide Chains Can Assemble Into Multisubunit Structures
3.6. The Amino Acid Sequence of a Protein Determines Its Three-Dimensional Structure

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