This free course is available to start right now. Review the full course description and key learning outcomes and create an account and enrol if you want a free statement of participation.

Free course


1.3.1 Helices

A variety of helical structures can be identified in proteins using X-ray diffraction. A helix can be described by the number of units (amino acid residues) per turn (n) and by its pitch (p), which is the distance that the helix rises along its axis per turn. These parameters are indicated in Figure 8 for a number of helices. In proteins, n is rarely a whole number.

Figure 8 Examples of helices indicating the parameters of pitch (p), number of units per turn (n) and handedness (+ or –). The black circles denote amino acid residues.

An important point to note is that a helix has a ‘handedness’; that is, if viewed along its axis, the chain turns either in a clockwise direction (right-handed helix) or in an anticlockwise direction (left-handed helix). For example, helices (b) and (d) in Figure 8 are, respectively, right- and left-handed. By convention, the number of repeating units (n) is positive for right-handed helices and negative for lefthanded helices. A number of different helical structures have been identified in proteins. The most common is the α helix, depicted in Figure 9a with details of its conformational parameters.

Figure 9 (a) The right-handed α helix, first described by Linus Pauling in 1951, showing hydrogen bonds between peptide carbonyl groups (C=O) and peptide amino (N–H) groups that are four residues along. There are 3.6 residues per turn (n = 3.6) and the helix has a pitch (p) of 5.4 Å. (b) An extended polypeptide chain illustrating the groups that form hydrogen bonds in the right-handed helix.

The α helix was discovered by Linus Pauling in 1951, using a model-building approach. It was later identified experimentally in α-keratin, a protein component of skin, hair and nails. The α helix structure is stabilised by hydrogen bonds between peptide carbonyl groups (C=O) and the peptide amino (N–H) groups that are four residues along (Figure 9b). In this way, the full hydrogen bonding capacity of the polypeptide backbone is utilised. Note that the side-chains (R) all project outwards and backwards from the helix as it rises; thus steric interference with the backbone or with other side-chains is avoided. The helix core is tightly packed and stabilised by van der Waals interactions.

In globular proteins, a helical stretch will, on average, include 12 residues although some proteins include α helices that contain up to 50 residues.

  • If a 12-residue stretch of polypeptide adopts an α helix structure, how many turns will it contain and how long will it be? You can answer this question using the values for n and p for the right-handed α helix in Figure 9a.

  • It will contain 3.3 turns and will be 18 Å long.

Since the hydrophilic polypeptide backbone is optimally hydrogen-bonded to itself and hidden away at the core of the α helix, such regions of secondary structure are commonly seen in proteins that traverse the cell membrane, such as transmembrane receptors and transport proteins. In such cases, the side-chains, which project into the lipid environment, are typically non-polar.


Take your learning further

Making the decision to study can be a big step, which is why you'll want a trusted University. The Open University has 50 years’ experience delivering flexible learning and 170,000 students are studying with us right now. Take a look at all Open University courses.

If you are new to university level study, find out more about the types of qualifications we offer, including our entry level Access courses and Certificates.

Not ready for University study then browse over 900 free courses on OpenLearn and sign up to our newsletter to hear about new free courses as they are released.

Every year, thousands of students decide to study with The Open University. With over 120 qualifications, we’ve got the right course for you.

Request an Open University prospectus