Scribd Logo
Upload

Welcome to Scribd!

  • Kent: Science 1994, 266, 776

    Uploaded by

    as_ari281522
    6 views11 pages
    This document discusses protein structure at different levels including secondary structure elements like alpha helices and beta sheets. It provides examples of these secondary structures from different proteins like myoglobin and immunoglobulin and references classic papers from 1951 by Linus Pauling that described protein secondary structure. The document also mentions non-covalent interactions like n->pi* that contribute to the formation of secondary structures and shows diagrams of protein assemblies and the sizes of polypeptide chains.

    Original Description:

    Original Title

    09

    Copyright

    © Attribution Non-Commercial (BY-NC)

    Available Formats

    PPT, PDF, TXT or read online from Scribd

    Did you find this document useful?

    Is this content inappropriate?

    Report this Document
    This document discusses protein structure at different levels including secondary structure elements like alpha helices and beta sheets. It provides examples of these secondary structures from different proteins like myoglobin and immunoglobulin and references classic papers from 1951 by Linus Pauling that described protein secondary structure. The document also mentions non-covalent interactions like n->pi* that contribute to the formation of secondary structures and shows diagrams of protein assemblies and the sizes of polypeptide chains.

    Copyright:

    Attribution Non-Commercial (BY-NC)
    Download as PPT, PDF, TXT or read online from Scribd
    Flag for inappropriate content
    6 views11 pages

    Kent: Science 1994, 266, 776

    Uploaded by

    as_ari281522
    This document discusses protein structure at different levels including secondary structure elements like alpha helices and beta sheets. It provides examples of these secondary structures from different proteins like myoglobin and immunoglobulin and references classic papers from 1951 by Linus Pauling that described protein secondary structure. The document also mentions non-covalent interactions like n->pi* that contribute to the formation of secondary structures and shows diagrams of protein assemblies and the sizes of polypeptide chains.

    Copyright:

    Attribution Non-Commercial (BY-NC)
    Download as PPT, PDF, TXT or read online from Scribd
    Flag for inappropriate content
    of 11

    Kent: Science 1994, 266, 776

    Muir: PNAS 1998, 95, 6705


    Evans: Protein Sci. 1998, 7, 2256
    Conditional Protein Splicing

    Muir: JACS 2002, 124, 9044

    Muir: JACS 2003, 125, 10561


    Size of a
    300-Residue
    Polypeptide

    (1 nm = 10 Å)
    Levels of Protein Structure
    -Helix
    (from myoglobin)

    (no sidechains)

    Pauling: PNAS 37, 205 (1951)


    -Helix
    (from myoglobin)

    (no sidechains)

    Pauling: PNAS 37, 205 (1951)


    -Sheet
    (from immunoglobulin domain)

    (no sidechains)

    Pauling: PNAS 37, 251 and 729 (1951)


    n->π* Interaction

    -helix PPII helix


    Basis for Secondary Structures
    Protein
    Assemblies

    You might also like