Fibrous Proteins

These flashcards cover fundamental terms and definitions related to fibrous proteins, their structure, synthesis, and role in the human body.

Fibrous Proteins

Proteins that have elongated rope-like structures, providing mechanical strength.

Scleroproteins

A class of fibrous proteins that are insoluble in water, primarily found in connective tissues.

Nonpolar Amino Acids

Amino acids that contain side chains with hydrophobic characteristics.

Thermostable

Referring to substances that are stable at high temperatures.

Collagen

The most abundant fibrous protein, providing structural support in various tissues.

Keratin

A fibrous protein forming the key structural material of hair, nails, and skin.

Elastin

A protein that allows tissues to stretch and recoil, found in skin and blood vessels.

Hydrophobic Interactions

Interactions that occur between nonpolar molecules in an aqueous environment.

Mechanical Strength

The ability of fibrous proteins to withstand deformation.

Types of Proteins

The classification of proteins based on their structure: fibrous and globular.

Amino Acid Sequence

The specific order of amino acids in a protein that determines its structure.

Structural Properties

Characteristics that define the arrangement and organization of proteins.

Secondary Structure

The local folded structures that form within a polypeptide due to interactions between adjacent amino acids.

Tertiary Structure

The overall three-dimensional structure of a single polypeptide chain.

Quaternary Structure

The structure formed by the assembly of multiple polypeptide chains.

Postranslational Modification

Chemical changes to proteins that occur after they are synthesized.

Glycosaminoglycans (GAGs)

Polysaccharides that play a role in cell signaling and structural integrity in the extracellular matrix.

Fibronectin

An adhesive protein that helps maintain the structural integrity of tissues.

Type I Collagen

Collagen found in skin, bone, tendons, and ligaments.

Type II Collagen

Collagen primarily found in cartilage.

Type III Collagen

Collagen found in blood vessels and fetal skin.

Type IV Collagen

Network-forming collagen found in the basement membrane.

Disulfide Bonds

Covalent bonds that form between cysteine residues in proteins, providing stability.

Hydroxylation

The addition of a hydroxyl group, crucial for collagen stability.

Translation

The process of synthesizing proteins based on messenger RNA (mRNA) templates.

Hydroxylation of Proline and Lysine

The post-translational modification critical for collagen stability, requiring vitamin C.

Procollagen

An inactive precursor of collagen that undergoes processing to become functional collagen.

Tropocollagen

The basic structural unit of collagen formed after the cleavage of procollagen.

Collagen Fibrils

Assembled structures of tropocollagen that contribute to the tensile strength of connective tissues.

Synthesis Steps of Collagen

The multi-step process that entails the formation of collagen from pro-α chains to mature collagen.

Signaling Pathways

Biological mechanisms through which tissues respond to signals from their environment.

Integrins

Transmembrane proteins that facilitate cell-extracellular matrix adhesion.

Extracellular Matrix (ECM)

A complex network of proteins and carbohydrates that provide structural and biochemical support to surrounding cells.

Osteogenesis Imperfecta

A genetic disorder characterized by fragile bones due to collagen deficiencies.

Ehlers-Danlos Syndrome

A group of connective tissue disorders caused by genetic defects in collagen synthesis.

Hypermobility Syndrome

A condition that results in excessive joint movement due to connective tissue laxity.

Cysteine

An amino acid that contains sulfur and is involved in forming disulfide bonds in proteins.

α-Keratin

A type of keratin found in hair and nails, known for its strength.

β-Keratin

A type of keratin found in the feathers of birds and the shells of reptiles.

Hydrolyzed Keratin

Keratin that has been broken down into smaller peptides for cosmetic use.

Keratinization

The process by which keratinocytes form a protective layer of keratin in the skin.

Fibroin

The main structural protein in silk fibers, known for its strength and flexibility.

Desmosine and Isodesmosine

Covalent crosslinks formed in elastin that enhance its elasticity.

Tropoelastin

The soluble precursor to elastin, secreted by fibroblasts.

Fibrillin

A glycoprotein that provides a scaffold for the assembly of elastic fibers.

Silkworm Silk

Silk produced by silkworms, primarily composed of fibroin.

Vitamin C

A vital vitamin required for hydroxylation in collagen synthesis.

Striated Appearance

The characteristic banding seen in collagen fibrils due to their staggered arrangement.

Collagen Types

More than 25 types exist, each with a specific tissue distribution and function.

Constancy of Collagen Structure

Collagen retains its structural integrity across different types.

Connective Tissue

Tissue that supports, binds together, and protects tissues and organs.

Elastic Fibers

Fibers composed of elastin that allow for tissue elasticity.

Amino Acid Modification

Chemical alterations to amino acids that may affect protein function.

Keratinocytes

Epithelial cells that produce keratin and form the outer layer of skin.

Tenascin

A glycoprotein involved in tissue repair and development.

Laminin

A key protein in the basement membrane that influences cell differentiation.

Intrachain Disulfide Bonds

Disulfide bonds formed within the same polypeptide chain, enhancing the protein's stability.

Interchain Disulfide Bonds

Disulfide bonds formed between different polypeptide chains.

Collagen Synthesis Disorders

Genetic or nutritional issues that can disrupt normal collagen formation.

Functional Role of Proteins

The physiological roles that proteins perform in biological systems.

Receptor Proteins

Proteins that bind to specific molecules, initiating cellular responses.

Carrier Proteins

Proteins that transport substances across biological membranes.

Storage Proteins

Proteins that store amino acids or nutrients for future use.

Cytoskeletal Proteins

Proteins that provide structural support and shape to cells.

Adhesive Proteins

Proteins that facilitate adhesion between cells and tissues.

Extracellular Domain

Part of a protein that extends outside the cell, often involved in signaling.

Basement Membrane

A thin layer of the extracellular matrix that separates epithelial cells from connective tissue.

Disulfide Bridge

A covalent bond between sulfur atoms of cysteine residues that stabilizes protein structure.

Mechanical Metabolism

The metabolic processes that contribute to tissue resilience and strength.

Phenylalanine

An essential amino acid that serves as a precursor to tyrosine.

Valine

An essential amino acid important for muscle metabolism and tissue repair.

Lysine

An essential amino acid crucial for protein synthesis and collagen formation.

Proline

An amino acid that plays a significant role in the structure of collagen.

Glycine

The simplest amino acid that is abundant in collagen and elastin.

Tryptophan

An amino acid that serves as a precursor to serotonin and melatonin.

Isoleucine

An essential branched-chain amino acid important for muscle metabolism.

Understanding of Collagen

A foundational knowledge of collagen's structure, synthesis, and function in the body.

Impact of Nutritional Deficiency

How a lack of nutrients can affect collagen synthesis and overall health.

Diseases Related to Collagen

Disorders that arise from defects in collagen structure or synthesis.

Research Advances

Recent findings in the study of collagen and its role in medicine.

Histological Analysis

The microscopic examination of tissues to study their structure.

Protein Crosslinking

The formation of covalent bonds between different protein molecules.

Cell Adhesion Molecules (CAMs)

Molecules located on the cell surface involved in binding with other cells or extracellular matrix.

Mucopolysaccharides

Another term for glycosaminoglycans, emphasizing their role in hydration.

Bonding in Proteins

Refers to the various chemical bonds that stabilize protein structures.

Structural Role of Proteins

Proteins that provide support and shape to tissues, as opposed to metabolic functions.

Antibodies

Proteins produced by the immune system to identify and neutralize pathogens.

Enzymes

Proteins that act as biological catalysts to accelerate chemical reactions.

Regulatory Proteins

Proteins that regulate various activities and processes in the body.

Hormonal Proteins

Proteins that function as hormones to regulate physiological processes.

Storage as a Protein Function

A role that includes storing nutrients and supplies for later growth or energy.

Physiological Mechanisms

The systems and processes by which biological functions occur.

Influence of Genetic Variation

The effect that genetic differences have on collagen and other protein structures.

Therapeutic Applications

The use of knowledge about proteins in medicine and treatments.

Elastin and Collagen Interaction

The complementary roles that elastin and collagen playing connective tissue strength and flexibility.