structural proteins

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Structural Proteins Presented by: Andrew and Briana

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Structural Proteins. Presented by: Andrew and Briana. Structural Protein Overview. Largest class of proteins (75% of the dry weight in humans) Generally add stiffness and rigidity to fluid biological components Commonly very fibrous - PowerPoint PPT Presentation

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Page 1: Structural Proteins

Structural ProteinsPresented by: Andrew and Briana

Page 2: Structural Proteins

Structural Protein Overview• Largest class of proteins

(75% of the dry weight in humans)

• Generally add stiffness and rigidity to fluid biological components

• Commonly very fibrous• Provide support for both

large structures and microscopic structures

Microfilaments

Page 3: Structural Proteins

Role in Living Things• Keratin

– Form strong supercoils– Protective function such as hair, nails, scales, feathers,

and beaks• Elastin

– Forms connective tissue (allows for stretching)– Tendons, ligaments, skin flexibility, lungs, arteries

• Myosin– Role in muscle movement such as hydrolysis of ATP

• Fibroin– Insoluble – Parallel sheets form silk used by insects and spiders

Page 4: Structural Proteins

More Roles in Organisms• Microtubules

– Protein = Tubulin– Cytoskeleton, cellular movement, mitotic spindle

• Microfilaments– Protein = Actin– Cytoskeleton, muscle contraction, organelle movement

• Intermediate Filaments– Protein = Keratin– Cytoskeleton– Not involved directly in movement

Page 5: Structural Proteins

How do they function?• Formation of fibers and filaments contribute to

structural strength of proteins• Movement and re-adjustment such as actin or

elastin require ATP• Other vitamins such as vitamin C are required for

synthesis

Polymerization ATP Dependent

Page 6: Structural Proteins

Shape and Function• Rigidity of Proteins

– Antiparallel chains form super coils– Hardened by hydrogen bonding and disulfide bridges

• Flexibility of Proteins– Solubility allows for globular proteins such as tubulin and actin to

form into strands– Lateral imperfect helix allows for elongation

• Transportation Ability– Polarization allows for transportation of molecules

• One negative and one positive end in the structure

ActinF-Actin

Dissolve/Polymerize

Page 7: Structural Proteins

Synthesis of Proteins • Message sent to

cell and genetic process begins

• Formation of mRNA (Units of 3)

Page 8: Structural Proteins

Synthesis of Proteins Cont.• Enters the

cytoplasm• Binds to a

ribosome

Page 9: Structural Proteins

Synthesis of Proteins Cont. • tRNA brings the

amino acid to the corresponding code on mRNA

• tRNA continues coming until chain is complete (peptide bonds)

Page 10: Structural Proteins

Synthesis Miscellaneous• Protein synthesis

inhibitors such as the toxin ricin stops the production of protein

• Disruptions in translation can lead to mutations and a change in function (1 in 10,000)

• Example of such mutation is sickle cell (hemoglobin)

• Disruption of protein manufacture can be disastrous

Page 11: Structural Proteins

Specific Example: Collagen• The most abundant protein in mammals

(25-35%)• Plays a large role in body structure

through ligaments and tendons (holds bones and muscles together)

• Vital for skin flexibility• Found in stiffer forms such as bone or cartilage

Page 12: Structural Proteins

Collagen Structure• 3 alpha peptide strands

bonded together• Forms a super helix or 3

part coil• Glycine accounts for 1/3

of the structure to repeated pattern– No R-Group allows for

closer connection among helixes, so hydrogen bonding and linking is facilitated

• Formation of bundles impact function such as bone vs. ligaments (parallel or unparalleled)

Collagen Type 1 Helix

Page 13: Structural Proteins

Collagen Genetics• Partial amino sequence: mhpglwlllv tlclteelaa ageksygkpc ggqdcsgscq

cfpekgargr pgpigiqgpt (repeat of g)• Similar to:

– Collagen alpha-6(IV) chain, partial [Macaca mulatta] 96%– Collagen alpha-6(IV) chain, partial [Macaca fascicularis] 96%

• Many others predicted relatedness to primates• Indicated a possible conserved gene which shows that many animals

may have had similar functional needs and the protein provided similar adaptive advantages

Page 14: Structural Proteins

Collagen Disorders• Non-Genetically Related

– Osteoporosis, from old age, leads to inflexibility in joints, thinner skin, and weaker bones

• Genetically Related– Osteogenesis imperfecta – Mutation leads to weak

bones and irregular connective tissue– Ehler-Danlos Syndrome – Varying mutations and

effects such as rupture of arteries or deformed connective tissue

Impact of Osteogenesis imperfecta EDS Symptoms

Page 15: Structural Proteins

In-Depth Disorder: Scurvy• Cause:

– Hydroxylation of lysines and prolines is a step that requires vitamin C as a cofactor. In scurvy, the lack of hydroxylation of prolines and lysines causes a looser triple helix (which is formed by 3 alpha peptides)

• Symptoms:– Spots on skin– Spongy gums– Loss of teeth– Pain in joints/Overall weakness

• Proposed Drug:– Target protein synthesis– A Vitamin C tablet that will provide necessary amounts of vitamins so

that collagen can form• Treatment applies to animals such as primates that cannot form their own

vitamin C. Other animals produce their own Vitamin C.

Page 16: Structural Proteins

THANKS FOR LISTENINGFrom Andrew and Briana