Protein Tertiary and Quaternary Structures: -Structural Diversity Reflects Functional Diversity in Globular Proteins

In a globular protein, different segments of a polypep tide chain (or multiple polypeptide chains) fold back on each other. As illustrated in Figure 4–15, this folding generates a compact form relative to polypeptides in a fully extended conformation. The folding also provides the structural diversity necessary for proteins to carry out a wide array of biological functions. Globular proteins include enzymes, transport proteins, motor proteins, regulatory proteins, immunoglobulins, and proteins with many other functions. As a new millennium begins, the number of known three-dimensional protein structures is in the thousands and more than doubles every two years. This wealth of structural information is revolutionizing our understanding of protein structure, the relation of structure

FIGURE 4–15 Globular protein structures are compact and varied. Human serum albumin (Mr 64,500) has 585 residues in a single chain. Given here are the approximate dimensions its single polypeptide chain would have if it occurred entirely in extended β conformation or as an α helix. Also shown is the size of the protein in its native globular form, as determined by X-ray crystallography; the polypeptide chain must be very compactly folded to fit into these dimensions.

to function, and even the evolutionary paths by which proteins arrived at their present state, which can be glimpsed in the family resemblances that are revealed as protein databases are sifted and sorted. The sheer variety of structures can seem daunting. Yet as new protein structures become available it is becoming increasingly clear that they are manifestations of a finite set of recognizable, stable folding patterns. Our discussion of globular protein structure begins with the principles gleaned from the earliest protein structures to be elucidated. This is followed by a de tailed description of protein substructure and comparative categorization. Such discussions are possible only because of the vast amount of information available over the Internet from resources such as the Protein Data Bank (PDB; www.rcsb.org/pdb), an archive of experi mentally determined three-dimensional structures of biological macromolecules.

اخر الاخبار

اخبار العتبة العباسية المقدسة

مؤسّسة الوافي تُهدي مكتبةَ مسجد الكوفة نسخةً من موسوعة فتوى الدفاع الكفائي

المجمع العلمي يقيم برنامج (سراج المنتظرين) في محافظة المثنى

قسم الشؤون الفكرية ينظم ندوة فكرية عن أبعاد نهضة الإمام الصادق (عليه السلام)

العتبة العباسية المقدسة تناقش تكثيف جهودها الإغاثية لدعم الشعبين الإيراني واللبناني

المزيد

الآخبار الصحية

دواء جديد يحمي القلب ويعزز علاج السرطان في آن واحد

سر غذائي بسيط لحماية القلب مع التقدم في العمر

علامات تشير إلى اختلال عمل الغدة الدرقية

السمنة واللقاحات.. دراسة تكشف تأثيراً سلبياً

المزيد

الآخبار التكنلوجية

البعوض في آيسلندا إشارة مبكرة على تحولات بيئية في القطب الشمالي

صاروخ يطلق قمرا اصطناعيا في مدار خاطئ

"أوبن إيه آي" تطلق نموذجا للعلوم الحيوية واكتشاف الأدوية

تفوق على البشر.. روبوت يحطم الرقم القياسي لسباق نصف ماراثون !

المزيد

مواضيع ذات صلة

Complementary Interactions between Proteins and Ligands: The Immune System and Immunoglobulins: -The Immune Response Features a Specialized Array of Cells and Proteins

Reversible Binding of a Protein to a Ligand: Oxygen-Binding Proteins: -Sickle-Cell Anemia Is a Molecular Disease of Hemoglobin

Reversible Binding of a Protein to a Ligand: Oxygen-Binding Proteins: -Oxygen Binding to Hemoglobin Is Regulated by 2,3-Bisphosphoglycerate

Protein Denaturation and Folding: - Loss of Protein Structure Results in Loss of Function

Protein Tertiary and Quaternary Structures: -There Are Limits to the Size of Proteins

Protein Tertiary and Quaternary Structures: -Protein Quaternary Structures Range from Simple Dimers to Large Complexes

Reversible Binding of a Protein to a Ligand: Oxygen-Binding Proteins: -Protein-Ligand Interactions Can Be Described Quantitatively

Reversible Binding of a Protein to a Ligand: Oxygen-Binding Proteins:- Myoglobin Has a Single Binding Site for Oxygen

Reversible Binding of a Protein to a Ligand: Oxygen-Binding Proteins:- Oxygen Can Be Bound to a Heme Prosthetic Group

Protein Denaturation and Folding:- Some Proteins Undergo Assisted Folding

Protein Denaturation and Folding:- Polypeptides Fold Rapidly by a Stepwise Process

Protein Denaturation and Folding: - Amino Acid Sequence Determines Tertiary Structure