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THE STRUCTURE OF PROTEINS
TWO HYDROGEN-BONDED
HELICAL CONFIGURATIONS OF THE POL YPEPTIDE
CHAIN (February 28 1951) JACS
Linus Carl Pauling, Robert B.Corey & H.R.Brason
The Nobel Prize in Chemistry 1954
Presented by
Yogesh Kumar
CSIR-CIMAP-JNU (Ph.D)
Protein Structures
All hydrogen bonds should be satisfied,
i.e. distance N-O of about 2.7Å and angle
between C = O and H – N less then ~30
Distances and angles
Between atoms
Determinants of helical structure
C-C=1.53Å ,
C==O = 1.23Å
C-N=1.32Å
N-CR=1.47
Models satisfies all constraints
3.6 residues per turn
The number of residues per turn in Pauling's final model was 3.6. Today alpha helix is
also known as (3.6 13 alpha ) helix . One helix contain 3.6 residues and 13 atoms
The helix with 5.1 residues per turn
The helix with 5.1 residues per turn.
The pi helix with 5.1 residues per turn--have yet to be found in nature and may not
exist at all.
The α-helix – one of the two common
structural elements in proteins
 Completes one turn every 3.6 residues
 Rises ~5.4 Å with each turn
 Has hydrogen bonds between the C=O of residue i
and the N-H of residue i+4
 Is right-handed
i
i+4
C
N
O
Complete one turn consist of 3.6 residues and each
residue take 1.5 Å rise. So ( 1.5*3.6=5.5 Å.)
Why did Pauling and Corey succeed where
others failed?
• The researchers who came up with earlier theories were crystallographers.
• They were used to crystals in which everything is made up of integral
numbers," said Eisenberg. "Pauling was a broader, structural chemist--he was
able to think outside the box.
• They did not consider only models with integer number of residues per turn!”
• Understanding the importance of hydrogen bonds
• Taking into account the planar peptide bond
• Better knowledge of covalent bond lengths and angles
• Pauling and Corey's work was not
without mistakes: research since the
1951 protein papers found the beta
sheet to be twisted, not flat as
suggested in Corey and Pauling's
research.
• Since Pauling and Corey's famous
series was first published, the ideas
their explanation have proceeded
from hypothesis to accepted fact to
common knowledge.
• Dramatic verification of their work
came in 1958, when the three-
dimensional structure of myoglobin
was found to be composed almost
solely of alpha helices
Mistakes
Proof came 7 years later…
John Cowdery Kendrew
The Nobel Prize in Chemistry 1962
Kendrew, J. C., Bodo, G., Dintzis, H. M. Parrish, R. G., Wyckoff, H.,
and Phillips, D. C. A Three-Dimensional Model of the Myoglobin
Molecule
Obtained by X-ray Analysis. Nature, 181, 662 (1958).
Hierarchy of Protein Structure
Linear chain made of 20 possible
amino acids
Alpha-helices, beta-sheets, turns
Motifs, domains
Oligomers, complexes
The Protein Data Bank (www.pdb.org)
Linus Pauling, Robert B.corey, and H. R. Branson* The structure of Proteins: Two Hydrogen-Bonded Helical Confirmations Of the
polypeptide chain,.JACS, Vol37, 1951
Thank You

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Protein structure by Pauling & corey

  • 1. THE STRUCTURE OF PROTEINS TWO HYDROGEN-BONDED HELICAL CONFIGURATIONS OF THE POL YPEPTIDE CHAIN (February 28 1951) JACS Linus Carl Pauling, Robert B.Corey & H.R.Brason The Nobel Prize in Chemistry 1954 Presented by Yogesh Kumar CSIR-CIMAP-JNU (Ph.D)
  • 3. All hydrogen bonds should be satisfied, i.e. distance N-O of about 2.7Å and angle between C = O and H – N less then ~30 Distances and angles Between atoms Determinants of helical structure C-C=1.53Å , C==O = 1.23Å C-N=1.32Å N-CR=1.47
  • 4. Models satisfies all constraints 3.6 residues per turn The number of residues per turn in Pauling's final model was 3.6. Today alpha helix is also known as (3.6 13 alpha ) helix . One helix contain 3.6 residues and 13 atoms
  • 5. The helix with 5.1 residues per turn The helix with 5.1 residues per turn. The pi helix with 5.1 residues per turn--have yet to be found in nature and may not exist at all.
  • 6. The α-helix – one of the two common structural elements in proteins  Completes one turn every 3.6 residues  Rises ~5.4 Å with each turn  Has hydrogen bonds between the C=O of residue i and the N-H of residue i+4  Is right-handed i i+4 C N O Complete one turn consist of 3.6 residues and each residue take 1.5 Å rise. So ( 1.5*3.6=5.5 Å.)
  • 7. Why did Pauling and Corey succeed where others failed? • The researchers who came up with earlier theories were crystallographers. • They were used to crystals in which everything is made up of integral numbers," said Eisenberg. "Pauling was a broader, structural chemist--he was able to think outside the box. • They did not consider only models with integer number of residues per turn!” • Understanding the importance of hydrogen bonds • Taking into account the planar peptide bond • Better knowledge of covalent bond lengths and angles
  • 8. • Pauling and Corey's work was not without mistakes: research since the 1951 protein papers found the beta sheet to be twisted, not flat as suggested in Corey and Pauling's research. • Since Pauling and Corey's famous series was first published, the ideas their explanation have proceeded from hypothesis to accepted fact to common knowledge. • Dramatic verification of their work came in 1958, when the three- dimensional structure of myoglobin was found to be composed almost solely of alpha helices Mistakes Proof came 7 years later… John Cowdery Kendrew The Nobel Prize in Chemistry 1962 Kendrew, J. C., Bodo, G., Dintzis, H. M. Parrish, R. G., Wyckoff, H., and Phillips, D. C. A Three-Dimensional Model of the Myoglobin Molecule Obtained by X-ray Analysis. Nature, 181, 662 (1958).
  • 9. Hierarchy of Protein Structure Linear chain made of 20 possible amino acids Alpha-helices, beta-sheets, turns Motifs, domains Oligomers, complexes
  • 10. The Protein Data Bank (www.pdb.org) Linus Pauling, Robert B.corey, and H. R. Branson* The structure of Proteins: Two Hydrogen-Bonded Helical Confirmations Of the polypeptide chain,.JACS, Vol37, 1951