DOI: 10.1110/ps.4550102. Polyproline II helical structure in protein unfolded states: Lysine peptides revisited

Polyproline II helical structure in protein unfolded states: Lysine peptides revisited

10.1110/ps.4550102

Crossref journal-article

Wiley

Protein Science (311)

Abstract

AbstractThe left‐handed polyproline II (PPII) helix gives rise to a circular dichroism spectrum that is remarkably similar to that of unfolded proteins. This similarity has been used as the basis for the hypothesis that unfolded proteins possess considerable PPII helical content. It has long been known that homopolymers of lysine adopt the PPII helical conformation at neutral pH, presumably a result of electrostatic repulsion between side chains. It is shown here that a seven‐residue lysine peptide also adopts the PPII conformation. In contrast with homopolymers of lysine, this short peptide is shown to retain PPII helical character under conditions in which side‐chain charges are heavily screened or even neutralized. The most plausible explanation for these observations is that the peptide backbone favors the PPII conformation to maximize favorable interactions with solvent. These data are evidence that unfolded proteins do indeed possess PPII content, indicating that the ensemble of unfolded states is significantly smaller than is commonly assumed.

Bibliography

Rucker, A. L., & Creamer, T. P. (2002). Polyproline II helical structure in protein unfolded states: Lysine peptides revisited. Protein Science, 11(4), 980â985. Portico.

Authors 2

Adam L. Rucker (first)
Trevor P. Creamer (additional)

References 36 Referenced 217

10.1006/jmbi.1993.1047
10.1126/science.181.4096.223
10.1016/S0167-4838(96)00191-4
{'key': 'e_1_2_6_5_1', 'first-page': '183', 'volume-title': 'polypeptides', 'author': 'Bhatnagar R.S.', 'year': '1996'} / polypeptides by Bhatnagar R.S. (1996)
10.1021/bi00734a027
10.1002/pro.5560030514
10.1002/(SICI)1097-0134(19981101)33:2<218::AID-PROT6>3.0.CO;2-E
10.1002/1097-0134(20000815)40:3<443::AID-PROT100>3.0.CO;2-L
10.1146/annurev.bi.60.070191.004051
10.1016/0301-4622(88)80019-X
10.1002/bip.360311409
10.1111/j.1399-3011.1982.tb03028.x
10.1002/bip.1968.360060306
10.1021/bi011043a
10.1002/ijch.197400018
10.1021/bi00186a015
10.1002/prot.340200108
10.1006/jmbi.1994.1153
10.1126/science.2237416
10.1002/bip.360340816
10.1021/bi00807a001
10.1002/(SICI)1097-0282(1999)51:2<121::AID-BIP2>3.0.CO;2-O
10.1073/pnas.97.23.12565
10.1021/bi00078a033
10.1002/pro.5560060809
10.1021/bi00140a006
10.1126/science.1060438
10.1002/(SICI)1097-0134(19990901)36:4<400::AID-PROT3>3.0.CO;2-B
10.1110/ps.8.3.587
10.1002/bip.1968.360061212
10.1002/bip.1968.360060911
10.1002/bip.1972.360111109
10.1021/ja00131a034
10.1042/bj2970249
10.1021/bi961314v
{'key': 'e_1_2_6_37_1', 'first-page': '37', 'article-title': 'Circular dichroism and conformation of unordered polypeptides', 'volume': '2', 'author': 'Woody R.W.', 'year': '1992', 'journal-title': 'Adv. Biophys. Chem.'} / Adv. Biophys. Chem. / Circular dichroism and conformation of unordered polypeptides by Woody R.W. (1992)

Dates

Type	When
Created	23 years, 1 month ago (July 26, 2002, 7:59 p.m.)
Deposited	1 year, 10 months ago (Oct. 8, 2023, 8:23 a.m.)
Indexed	4 days, 8 hours ago (Aug. 31, 2025, 7:27 p.m.)
Issued	23 years, 5 months ago (April 1, 2002)
Published	23 years, 5 months ago (April 1, 2002)
Published Online	16 years, 8 months ago (Jan. 1, 2009)
Published Print	23 years, 5 months ago (April 1, 2002)

Funders 0

None

BibTeX

@article{Rucker_2002, title={Polyproline II helical structure in protein unfolded states: Lysine peptides revisited}, volume={11}, ISSN={1469-896X}, url={http://dx.doi.org/10.1110/ps.4550102}, DOI={10.1110/ps.4550102}, number={4}, journal={Protein Science}, publisher={Wiley}, author={Rucker, Adam L. and Creamer, Trevor P.}, year={2002}, month=apr, pages={980–985} }

JSON

{
  "indexed": {
    "date-parts": [
      [
        2025,
        8,
        31
      ]
    ],
    "date-time": "2025-08-31T23:27:18Z",
    "timestamp": 1756682838662
  },
  "reference-count": 36,
  "publisher": "Wiley",
  "issue": "4",
  "license": [
    {
      "start": {
        "date-parts": [
          [
            2009,
            1,
            1
          ]
        ],
        "date-time": "2009-01-01T00:00:00Z",
        "timestamp": 1230768000000
      },
      "content-version": "vor",
      "delay-in-days": 2467,
      "URL": "http://onlinelibrary.wiley.com/termsAndConditions#vor"
    }
  ],
  "content-domain": {
    "domain": [],
    "crossmark-restriction": false
  },
  "published-print": {
    "date-parts": [
      [
        2002,
        4
      ]
    ]
  },
  "abstract": "<jats:title>Abstract</jats:title><jats:p>The left\u2010handed polyproline II (PPII) helix gives rise to a circular dichroism spectrum that is remarkably similar to that of unfolded proteins. This similarity has been used as the basis for the hypothesis that unfolded proteins possess considerable PPII helical content. It has long been known that homopolymers of lysine adopt the PPII helical conformation at neutral pH, presumably a result of electrostatic repulsion between side chains. It is shown here that a seven\u2010residue lysine peptide also adopts the PPII conformation. In contrast with homopolymers of lysine, this short peptide is shown to retain PPII helical character under conditions in which side\u2010chain charges are heavily screened or even neutralized. The most plausible explanation for these observations is that the peptide backbone favors the PPII conformation to maximize favorable interactions with solvent. These data are evidence that unfolded proteins do indeed possess PPII content, indicating that the ensemble of unfolded states is significantly smaller than is commonly assumed.</jats:p>",
  "DOI": "10.1110/ps.4550102",
  "type": "journal-article",
  "created": {
    "date-parts": [
      [
        2002,
        7,
        26
      ]
    ],
    "date-time": "2002-07-26T23:59:58Z",
    "timestamp": 1027727998000
  },
  "page": "980-985",
  "source": "Crossref",
  "is-referenced-by-count": 217,
  "title": "Polyproline II helical structure in protein unfolded states: Lysine peptides revisited",
  "prefix": "10.1002",
  "volume": "11",
  "author": [
    {
      "given": "Adam L.",
      "family": "Rucker",
      "sequence": "first",
      "affiliation": []
    },
    {
      "given": "Trevor P.",
      "family": "Creamer",
      "sequence": "additional",
      "affiliation": []
    }
  ],
  "member": "311",
  "published-online": {
    "date-parts": [
      [
        2009,
        1
      ]
    ]
  },
  "reference": [
    {
      "key": "e_1_2_6_2_1",
      "doi-asserted-by": "publisher",
      "DOI": "10.1006/jmbi.1993.1047"
    },
    {
      "key": "e_1_2_6_3_1",
      "doi-asserted-by": "publisher",
      "DOI": "10.1126/science.181.4096.223"
    },
    {
      "key": "e_1_2_6_4_1",
      "doi-asserted-by": "publisher",
      "DOI": "10.1016/S0167-4838(96)00191-4"
    },
    {
      "key": "e_1_2_6_5_1",
      "first-page": "183",
      "volume-title": "polypeptides",
      "author": "Bhatnagar R.S.",
      "year": "1996"
    },
    {
      "key": "e_1_2_6_6_1",
      "doi-asserted-by": "publisher",
      "DOI": "10.1021/bi00734a027"
    },
    {
      "key": "e_1_2_6_7_1",
      "doi-asserted-by": "publisher",
      "DOI": "10.1002/pro.5560030514"
    },
    {
      "key": "e_1_2_6_8_1",
      "doi-asserted-by": "publisher",
      "DOI": "10.1002/(SICI)1097-0134(19981101)33:2<218::AID-PROT6>3.0.CO;2-E"
    },
    {
      "key": "e_1_2_6_9_1",
      "doi-asserted-by": "publisher",
      "DOI": "10.1002/1097-0134(20000815)40:3<443::AID-PROT100>3.0.CO;2-L"
    },
    {
      "key": "e_1_2_6_10_1",
      "doi-asserted-by": "publisher",
      "DOI": "10.1146/annurev.bi.60.070191.004051"
    },
    {
      "key": "e_1_2_6_11_1",
      "doi-asserted-by": "publisher",
      "DOI": "10.1016/0301-4622(88)80019-X"
    },
    {
      "key": "e_1_2_6_12_1",
      "doi-asserted-by": "publisher",
      "DOI": "10.1002/bip.360311409"
    },
    {
      "key": "e_1_2_6_13_1",
      "doi-asserted-by": "publisher",
      "DOI": "10.1111/j.1399-3011.1982.tb03028.x"
    },
    {
      "key": "e_1_2_6_14_1",
      "doi-asserted-by": "publisher",
      "DOI": "10.1002/bip.1968.360060306"
    },
    {
      "key": "e_1_2_6_15_1",
      "doi-asserted-by": "publisher",
      "DOI": "10.1021/bi011043a"
    },
    {
      "key": "e_1_2_6_16_1",
      "doi-asserted-by": "publisher",
      "DOI": "10.1002/ijch.197400018"
    },
    {
      "key": "e_1_2_6_17_1",
      "doi-asserted-by": "publisher",
      "DOI": "10.1021/bi00186a015"
    },
    {
      "key": "e_1_2_6_18_1",
      "doi-asserted-by": "publisher",
      "DOI": "10.1002/prot.340200108"
    },
    {
      "key": "e_1_2_6_19_1",
      "doi-asserted-by": "publisher",
      "DOI": "10.1006/jmbi.1994.1153"
    },
    {
      "key": "e_1_2_6_20_1",
      "doi-asserted-by": "publisher",
      "DOI": "10.1126/science.2237416"
    },
    {
      "key": "e_1_2_6_21_1",
      "doi-asserted-by": "publisher",
      "DOI": "10.1002/bip.360340816"
    },
    {
      "key": "e_1_2_6_22_1",
      "doi-asserted-by": "publisher",
      "DOI": "10.1021/bi00807a001"
    },
    {
      "key": "e_1_2_6_23_1",
      "doi-asserted-by": "publisher",
      "DOI": "10.1002/(SICI)1097-0282(1999)51:2<121::AID-BIP2>3.0.CO;2-O"
    },
    {
      "key": "e_1_2_6_24_1",
      "doi-asserted-by": "publisher",
      "DOI": "10.1073/pnas.97.23.12565"
    },
    {
      "key": "e_1_2_6_25_1",
      "doi-asserted-by": "publisher",
      "DOI": "10.1021/bi00078a033"
    },
    {
      "key": "e_1_2_6_26_1",
      "doi-asserted-by": "publisher",
      "DOI": "10.1002/pro.5560060809"
    },
    {
      "key": "e_1_2_6_27_1",
      "doi-asserted-by": "publisher",
      "DOI": "10.1021/bi00140a006"
    },
    {
      "key": "e_1_2_6_28_1",
      "doi-asserted-by": "publisher",
      "DOI": "10.1126/science.1060438"
    },
    {
      "key": "e_1_2_6_29_1",
      "doi-asserted-by": "publisher",
      "DOI": "10.1002/(SICI)1097-0134(19990901)36:4<400::AID-PROT3>3.0.CO;2-B"
    },
    {
      "key": "e_1_2_6_30_1",
      "doi-asserted-by": "publisher",
      "DOI": "10.1110/ps.8.3.587"
    },
    {
      "key": "e_1_2_6_31_1",
      "doi-asserted-by": "publisher",
      "DOI": "10.1002/bip.1968.360061212"
    },
    {
      "key": "e_1_2_6_32_1",
      "doi-asserted-by": "publisher",
      "DOI": "10.1002/bip.1968.360060911"
    },
    {
      "key": "e_1_2_6_33_1",
      "doi-asserted-by": "publisher",
      "DOI": "10.1002/bip.1972.360111109"
    },
    {
      "key": "e_1_2_6_34_1",
      "doi-asserted-by": "publisher",
      "DOI": "10.1021/ja00131a034"
    },
    {
      "key": "e_1_2_6_35_1",
      "doi-asserted-by": "publisher",
      "DOI": "10.1042/bj2970249"
    },
    {
      "key": "e_1_2_6_36_1",
      "doi-asserted-by": "publisher",
      "DOI": "10.1021/bi961314v"
    },
    {
      "key": "e_1_2_6_37_1",
      "first-page": "37",
      "article-title": "Circular dichroism and conformation of unordered polypeptides",
      "volume": "2",
      "author": "Woody R.W.",
      "year": "1992",
      "journal-title": "Adv. Biophys. Chem."
    }
  ],
  "container-title": "Protein Science",
  "original-title": [],
  "language": "en",
  "link": [
    {
      "URL": "https://api.wiley.com/onlinelibrary/tdm/v1/articles/10.1110%2Fps.4550102",
      "content-type": "unspecified",
      "content-version": "vor",
      "intended-application": "text-mining"
    },
    {
      "URL": "https://onlinelibrary.wiley.com/doi/pdf/10.1110/ps.4550102",
      "content-type": "unspecified",
      "content-version": "vor",
      "intended-application": "similarity-checking"
    }
  ],
  "deposited": {
    "date-parts": [
      [
        2023,
        10,
        8
      ]
    ],
    "date-time": "2023-10-08T12:23:42Z",
    "timestamp": 1696767822000
  },
  "score": 1,
  "resource": {
    "primary": {
      "URL": "https://onlinelibrary.wiley.com/doi/10.1110/ps.4550102"
    }
  },
  "subtitle": [],
  "short-title": [],
  "issued": {
    "date-parts": [
      [
        2002,
        4
      ]
    ]
  },
  "references-count": 36,
  "journal-issue": {
    "issue": "4",
    "published-print": {
      "date-parts": [
        [
          2002,
          4
        ]
      ]
    }
  },
  "alternative-id": [
    "10.1110/ps.4550102"
  ],
  "URL": "http://dx.doi.org/10.1110/ps.4550102",
  "relation": {},
  "ISSN": [
    "0961-8368",
    "1469-896X"
  ],
  "subject": [],
  "container-title-short": "Protein Science",
  "published": {
    "date-parts": [
      [
        2002,
        4
      ]
    ]
  }
}